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ACTN4 (actinin, alpha 4)

Written2013-04Dimitar P Zankov, Hisakazu Ogita
Department of Biochemistry, Molecular Biology, Shiga University of Medical Science, Seta Tsukinowa-cho, Otsu, Shiga 520-2192, Japan

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Identity

Alias_namesFSGS1
focal segmental glomerulosclerosis 1
Other aliasACTININ-4
FSGS
HGNC (Hugo) ACTN4
LocusID (NCBI) 81
Atlas_Id 562
Location 19q13.2  [Link to chromosome band 19q13]
Location_base_pair Starts at 39138267 and ends at 39221171 bp from pter ( according to hg19-Feb_2009)  [Mapping ACTN4.png]
Local_order EIF3K, ACTN4, CAPN12.
 
  Scheme of ACTN4 genomic locus. The fragment of chromosome 19q13.2 (19:39109722-39235114, GRCh37.p10 Primary Assembly) containing ACTN4 and surrounding DNA sequence was shown. Genes are drawn as arrows with the length approximately corresponding to the number of bases in each gene. Arrowheads point at the direction of transcription (5' to 3' end).
Fusion genes
(updated 2016)
ABCD4 (14q24.3) / ACTN4 (19q13.2)ACTN4 (19q13.2) / ACTN4 (19q13.2)ACTN4 (19q13.2) / CAPZB (1p36.13)
ACTN4 (19q13.2) / DAB2 (5p13.1)ACTN4 (19q13.2) / DLGAP1 (18p11.31)ACTN4 (19q13.2) / DSG2 (18q12.1)
ACTN4 (19q13.2) / ETV5 (3q27.2)ACTN4 (19q13.2) / FTO (16q12.2)ACTN4 (19q13.2) / HNRNPL (19q13.2)
ACTN4 (19q13.2) / IGF2BP2 (3q27.2)ACTN4 (19q13.2) / KMT2A (11q23.3)ACTN4 (19q13.2) / MALAT1 (11q13.1)
ACTN4 (19q13.2) / MYO15A (17p11.2)ACTN4 (19q13.2) / MZB1 (5q31.2)ACTN4 (19q13.2) / SERPING1 (11q12.1)
ACTN4 (19q13.2) / U2AF1 (21q22.3)ACTN4 (19q13.2) / URM1 (9q34.11)ACTN4 (19q13.2) / VCP (9p13.3)
ACTN4 (19q13.2) / YIF1B (19q13.2)APPL2 (12q23.3) / ACTN4 (19q13.2)BOLA2 (16p11.2) / ACTN4 (19q13.2)
CGGBP1 (3p11.1) / ACTN4 (19q13.2)EIF3K (19q13.2) / ACTN4 (19q13.2)FUS (16p11.2) / ACTN4 (19q13.2)
KMT2A (11q23.3) / ACTN4 (19q13.2)LSM14A (19q13.11) / ACTN4 (19q13.2)MZB1 (5q31.2) / ACTN4 (19q13.2)
PRNP (20p13) / ACTN4 (19q13.2)TAPBPL (12p13.31) / ACTN4 (19q13.2)TTC6 (14q21.1) / ACTN4 (19q13.2)
Note ACTN4 is positioned between EIF3K and CAPN12. Human CAPN12 and ACTN4 share 339 bases of non-coding DNA sequence at their 3' ends (NC_000019.9, green box in the diagram). In mouse genome the two genes overlap in a similar manner (Dear et al., 2000).

DNA/RNA

Description The genomic DNA of ACTN4 (NC_000019.9) spans 82905 base pairs between coordinates 39138267 and 39221171 on chromosome 19, GRCh37.p10 Primary Assembly. ACTN4 contains 21 exons.
ACTN4 single nucleotide variants and insertions/deletions included in dbSNP137 (NCBI) count 1776 entities.
Transcription The mRNA of ACTN4 (NM_004924.4) comprises 3966 bases and bases 120-2855 form the coding sequence. Honda et al. (2004) described alternatively spliced variant originally identified in small cell lung cancer that is also detectable in normal brain and testis tissues. In the variant, the same length alternative sequence originating from the intron 8 replaces usual exon 8. Alternatively spliced α-actinin 4 has substitutions in the following aa: N248G, A250L, S262C and higher affinity to filamentous actin in in vitro co-sedimentation assay. Alternative splicing of exon 19 alters calcium sensitivity of α-actinin 4 and has been detected in mouse brain but not in other of the investigated mouse tissue samples (Lek et al., 2010; Foley and Young, 2013).
Yeast two-hybrid screen of human cDNA library captured another splice variant lacking nt 263-1433 of the full-length mRNA thus removing part of the first and second calponin-homology domain, the first and partially second spectrin-like repeat from α-actinin 4 (Chakraborty et al., 2006).
Pseudogene There are 2 known pseudogenes for ACTN4: ACTN4P1 (NG_022074.1) is located on chromosome 4q26 and ACTN4P2 (HGNC: 44032) is located on chromosome 1p34.3.

Protein

 
  Organization and domain structure of α-actinin 4 molecule. Functional protein is antiparallel homodimer (upper panel). Lower panel: domains of the protein ordered from N to C-terminus. Abbreviations: CH - calponin-homology domain (CH1, aa 50-154 and CH2, aa 163-269); S - spectrin-like repeats (S1, aa 293-403, S2, aa 413-518, S3, aa 528-639, and S4, aa 649-752); EF - EF-hand motifs (EF1, aa 765-800 and EF2, aa 806-841). Amino acid positions in the α-actinin 4 are indicated according to UniprotKB/Swiss-Prot database.
Description α-Actinins are members of the spectrin superfamily proteins. There are four isoforms, product of different genes. Isoform 2 and 3 ("muscle" α-actinin) are constituents of sarcomeres in the heart and skeletal muscle. Isoform 1 and 4 are "non-muscle" α-actinins found practically in every tissue.
α-Actinin 4 is a ~100 kDa protein. It has high degree of similarity to α-actinin 1 isoforms: 87% identical to isoform b (NP_001093.1) and 85% to isoform a (NP_001123476.1). α-Actinin 4 is cloned and characterized by Honda et al. (1998) in cancer cells although earlier description of two non-muscle α-actinins in chick lung exists (Imamura and Masaki, 1992). All spectrin-related proteins share similar structure: N-terminal actin-binding site formed by a pair of calponin-homology domains, central rod domain containing variable number spectrin-like repeats and C-terminal calmodulin domain with two EF-hand motifs (Broderick and Winder, 2002). Human α-actinin harbors 4 spectrin repeats and functions as antiparallel homodimer so that N-terminal lateral domains effectively bundle the actin filaments. Surprisingly, very recent study has discovered α-actinin 1/α-actinin 4 heterodimers in several cancer cell lines (Foley and Young, 2013).
Expression α-Actinin 4 is ubiquitously expressed in normal non-muscle cells and neoplastic tissue although the degree varies.
Localisation α-Actinin 4 predominantly localizes in the cytoplasmic regions, and in some cells it can be found likewise in the nucleus. Activation of intracellular biochemical pathways or actin depolimerization may force the protein to translocate to the nucleus. α-Actinin 4 commutes between cytosol and nucleus through the nuclear pore complexes as a result of hydrophobic interaction between the rod domain and proteins of the pores; nuclear localization is also cell cycle dependent (Kumeta et al., 2010). Subcellular distribution of α-actinin 4 has been contrasted to that of α-actinin 1 isoform in endometrial fibroblasts (Honda et al., 1998). α-Actinin 1 has been found at the ends of actin stress fibers and adherens junctions i.e. cell membrane associated; on the other hand α-actinin 4 colocalized with the F-actin and was allocated in the cytosol and nucleus. However, there are reports showing involvement of α-actinin 4 in the structure of tight junctions (TJs) (Nakatsuji et al., 2008).
Another characteristic residence of α-actinin 4 is peripheral and dorsal cell protrusions associated with cell movement (Araki et al., 2000). In the kidney α-actinin 4 is highly expressed and located in the foot processes of glomerular podocytes where it is essential for the kidney barrier function.
Function ACTN4 product is a versatile protein. Structure of the molecule, particularly the central spectrin repeats (Djinovic-Carugo et al., 2002), allows the rod domain to serve as a docking site of wide variety of cytosolic and nuclear proteins. This fact defines participation of α-actinin 4 in multiple cellular processes. Majority of the known functional interactions at present are listed below:

i/ Cytoskeletal organization and cell motility. Ability of α-actinin 4 to crosslink actin stress fibers and binding of transmembrane proteins in the cell junctions contributes to the maintenance of cell shape and anchoring to the adjacent extracellular matrix. α-Actinin 4 is involved in targeting JRAB/MICAL-L2 complex (important for recycling of occludin) to plasma membrane of TJs and participates in TJ formation (Nakatsuji et al., 2008).
Together with α-actinin 1, α-actinin 4 is essential for the formation of dorsal stress fibers in the migrating cells, composition and maturation of focal adhesions. Tyrosine phosphorylation of α-actinins is critical in those processes. In the absence of α-actinins focal adhesions have reduced affinity to extracellular matrix proteins (Feng et al., 2013).
Expression of α-actinin 4 is upregulated in the migrating cells and localized in their protrusions (Honda et al., 1998). In the stepwise process of cell movement it is believed that α-actinin 4 (most probably both non-muscle isoforms) is important for the detachment of rear cell end through organized disassembly of focal adhesions by calpain (Bhatt et al., 2002; Shao et al., 2013). Complementary mechanism promoting focal adhesions disassembly is binding of PIP3, a lipid product of phoshoinositide 3-kinase, to the α-actinins CH2 domain. That interaction reduces affinity of α-actinins to actin and integrin (Greenwood et al., 2000).

ii/ Modulation of gene transcription. It has been shown that α-actinin 4 interacts with nuclear receptors (estrogen receptor α in MCF-7 cells, vitamin D receptor in CV-1 cells, retinoic acid receptor and peroxisome proliferator-activated receptor γ in podocytes) and transcriptional co-activators (PCAF, SRC-1) through its LXXLL motif (Khurana et al., 2012a; Khurana et al., 2012b). Binding affinity to the nuclear factors was stronger in the alternatively spliced (short) isoform identified in a human cDNA library during earlier study (Chakraborty et al., 2006). All the above interactions enhance gene transcription. In addition, α-actinin 4 antagonizes histone deacetylase 7 thereby potentiating myocyte enhancer factor-2 in HeLa cells (Khurana et al., 2011).
ACTN4 product also is transcriptional co-activator of RelA/p65 subunit of NF-kB (Aksenova et al., 2013). Together with nuclear factor-Y, α-actinin 4 modulates transcription of CYP1A1, gene involved in pathogenesis of certain cases of lung and breast cancer (Poch et al., 2004).
α-Actinin 4 interacts with INO80 chromatin-remodeling complex and promote Cyclin B1 expression. In the mitotic phase, α-actinin 4 associates with upstream binding factor-dependent transcriptional complex (Kumeta et al., 2010).

iii/ Apoptosis. Endonuclease DNaseY is involved in apoptotic DNA degradation. α-Actinin 4 physically associates with DNaseY and dramatically enhances activity of the enzyme and percentage of PC12 cells developing apoptosis induced by teniposide (Liu et al., 2004).

iv/ Clathrin-mediated endocytosis. α-Actinin has been found in isolated plasma membranes containing clathrin (Burridge et al., 1980) and association of α-actinin 4 and clathrin heavy chain has been identified in prostate cancer cells. Overexpression of α-actinin 4 facilitated transferrin endocytosis (Hara et al., 2007).

v/ Function in glomerular podocytes. The presence of intact α-actinin 4 in the foot processes of podocytes is vital for the proper glomerular filtration. Elimination of the gene function in animal experiments (ACTN4 knockout mice) and mutations in human ACTN4 result in the development of focal segmental glomerulosclerosis (Kos et al., 2003; Kaplan et al., 2000).

vi/ Other. Exhaustive listing of α-actinin 4 interactions is beyond the scope of this structured review article. More details can be found at least in several excellent review publications (Sjöblom et al., 2008; Otey and Carpen, 2004; Oikonomou et al., 2011).

Homology In variety of species there are orthologs with high identity to human ACTN4 isoform: Pongo abelii 99% (NP_001127286.1), Bos Taurus 99% (NP_001091521.1), Rattus norvegicus 98% (NP_113863.2), Mus musculus 98% (NP_068695.1), Gallus gallus 92% (NP_990457.1), Xenopus laevis 90% (NP_001087030.1), Danio rerio 86% (NP_955880.1). Molecular evolution of α-actinin has been studied (Virel and Backman, 2004).

Mutations

Note Mice deficient in ACTN4 develop progressive proteinuria, glomerular disease, and die in several months of age. Cell motility in the absence of ACTN4 (lymphocyte chemotaxis) is increased (Kos et al., 2003).
Germinal Autosomal dominant point mutations in ACTN4 have been found in familial focal segmental glomerulosclerosis (FSGS). Kaplan et al., 2000 identified missense substitutions K228Q, T232I, and S235P in 3 families affected by FSGS.
Somatic Point mutation K122N has been discovered in the cell line derived from large cell carcinoma of the lung. The ACTN4-encoded protein was detected in the cDNA library and the ORF lacked the first 53 aa of the protein (Echchakir et al., 2001). This variant was missing in the α-actinin 4 purified from B-cells in the same patient.

Implicated in

Note
  
Entity Cancer
Note ACTN4 product protein is associated with disease progress and metastatic processes in variety of neoplasms due to its crucial involvement in cell adhesion and motility mechanisms. Elevated α-actinin 4 in neoplastic tissue is usually negative predictor of disease prognosis although there are reports proposing suppressive effects on tumor cells growth and malignant phenotype. In some cancer types ACTN4 is candidate oncogene.
  
  
Entity Pancreatic cancer
Note Increased level of α-actinin 4 has been determined as independent prognostic factor associated with most unfavorable prognosis in a group of 173 patients with invasive ductal carcinoma of the pancreas (Kikuchi et al., 2008).
Amplification of chromosome 19q13.1-q13.2 has been reported in pancreatic cancer-derived cell lines and pancreatic cancer tissue. ACTN4 is one of the putative oncogenes in that locus (Miwa et al., 1996; Höglund et al., 1998).
  
  
Entity Breast cancer
Note α-Actinin 4 is detected in many histological subtypes of breast cancer and subcellular localization of the molecule (nucleus vs. cytosol) is related to disease outcome. Cytosolic localization has been found in the types of cancer with more malignant histological subtype, metastasis, and worse survival (Honda et al., 1998). Proliferation of MCF-7 breast cancer cells is promoted by α-actinin 4 although the precise mechanism was not identified (Khurana et al., 2011).
  
  
Entity Colorectal cancer
Note Specimens from 26 patients with colorectal cancer were immunostained to visualize the expression of α-actinin 4. In 19 preparations (73.1%) the expression was increased especially in the malignant cells in the "focal dedifferentiation" areas. In the cell line DLD1 (derived from colorectal adenocarcinoma) stable expression of ACTN4 protein dramatically changed cell morphology and increased motility. When those cells are injected into the spleens of the mice with severe combined immunodeficiency metastasis developed in the surrounding lymph nodes. On the other hand, injection of original DLD1 cells did not induce metastatic disease (Honda et al., 2005). These findings suggest involvement of ACTN4 in progression of colorectal carcinoma.
  
  
Entity Lung cancer
Note ACTN4 gene product has been reported to exert multiple effects on human lung cancer cell biology and disease prognosis. Moreover, the available data so far has shown that α-actinin 4 is able to promote as well as suppress the malignant development reflecting probably the diversity of mechanisms involved in oncogenesis of lung cancer. Several mutations and splice variants in ACTN4 that influence the lung cancer cell phenotype have been described.
Using highly specific monoclonal antibody, alternatively spliced variant of ACTN4 has been identified exclusively in high-grade neuroendocrine lung tumors compared to non-neuroendocrine lung cancers, 96 of 176 (55%) versus 3 of 378 (0.8%) of investigated patients, respectively. Statistical analysis revealed that variant α-actinin 4 is independent negative prognostic factor. The protein binds F-actin with higher avidity (Miyanaga et al., 2013).
Analysis of gene expression by microarray technology proved α-actinin 4 as a marker of worse disease development in non-small cell lung cancer. Higher expression of α-actinin 4 has been correlated to significantly lower survival (Yamagata et al., 2003).
Small cell lung cancer (SCLC) cell lines and tissue from the patient biopsies express ACTN4 alternatively spliced variant, normally found in the testis. Variant α-actinin 4 binds F-actin with higher affinity. This splice variant was proposed as diagnostic marker in SCLC (Honda et al., 2004).
Immune response against the mutated ACTN4 in the patient with large cell lung cancer has been involved in the clinical evolution of the disease. Furthermore, after extraction of the primary tumor the cytotoxic T lymphocyte clone targeting mutated α-actinin 4 persisted many years in the patient's blood (Echchakir et al., 2001). In the subsequent study, it has been shown that the above point mutation removes antiproliferative effect of ACTN4 protein in the cancer cell line and supports the notion that ACTN4 may be both tumor suppressor as well as tumor promoter gene (Menez et al., 2004).
  
  
Entity Nervous system neoplasms
Note Similar to various carcinomas, increase of ACTN4 protein levels also appears to be involved in progression of certain brain tumors. In human astrocytoma contrasted to normal human brain tissue, Western blot densitometric quantification demonstrated ~2 times higher levels of α-actinin 4 in the tumor samples; furthermore, in higher grades astrocytomas (III-IV) α-actinin 4 has additional 1.9 fold increase compared to low grades astrocytomas (I-II). In vitro downregulation of α-actinin 4 (RNAi) in human astrocytoma cell lines U-373, U-87, and A172 reduced cell adhesion and motility, cortical actin localization, and RhoA mRNA and protein. In U-373 cells only α-actinin 4 promoted cell growth (Quick and Skalli, 2010).
However, some experimental data support the opposite concept: a number of cytoskeleton-associated proteins show reduced expression in cancer cells and recovering their levels (e.g., in vitro transfection) transform the cells phenotype to less malignant (Glück et al., 1993). Human neuroblastoma cell lines with high malignant phenotype express lower level of α-actinin 4 compared to more differentiated and less malignant neuroblastoma cell lines. Transfection with ACTN4 has suppressed tumorigenicity and has converted neuroblasts from high to low malignant phenotype. The effect persisted until the level of α-actinin 4 in transfected cells was maintained and initial high malignancy phenotype recovered when α-actinin 4 declined (Nikolopoulos et al, 2000).
  
  
Entity Esophageal cancer
Note In a Chinese cohort of 12 patients suffering esophageal squamous cell carcinoma, α-actinin 4 overexpression has been detected in tumor tissue and proposed as a marker for prognostic evaluation of the disease (Fu et al., 2007).
  
  
Entity Prostate cancer
Note Involvement of α-actinin 4 in tumor pathophysiology is undoubtedly mediated by various mechanisms because of the large number of binding partner molecules that have been identified. In human prostate cancer cell lines (22RV1, PC-3, LNCaP) ACTN4 protein product was less abundant than in normal human prostate epithelial cells, an observation that is conflicting with the findings in the most reports investigating relationship ACTN4-cancer development. Increasing the level of α-actinin 4 in those prostate cancer cells markedly suppressed cell-growth (Hara et al., 2007). In the same report the authors propose disturbance in clathrin-mediated endocytosis as the main mechanism associated with α-actinin 4 mediated cellular effects.
  
  
Entity Bladder cancer
Note The promoting effect of ACTN4 gene product on cancer invasion has also been found in the bladder cancer cell lines (T24, J82) and tissue from superficial and invasive bladder cancers. ACTN4 mRNA and protein levels are higher in malignant cell lines and the tissues from the patients versus disease-free state. RNAi silencing of ACTN4 resulted in decreased cell invasion as measured by in vitro assay but did not affect the cell growth (Koizumi et al., 2010).
  
  
Entity Ovarian cancer
Note Increased expression of α-actinin 4 and 19q12-13 genetic locus amplification has been detected in 21% of 136 cases of advanced-stage ovarian cancer. Statistical analysis associated higher copy number of ACTN4 as negative prognostic factor in the patients with ovarian cancer (Yamamoto et al., 2007).
ACTN4 is a candidate oncogene in epithelial ovarian cancer. In subset of patients it has been found that the chromosome 19q12-q13 region is amplified correlating with higher expression of α-actinin 4 protein (Yamamoto et al., 2009).
  
  
Entity Glomerular kidney disease - Focal segmental glomerulosclerosis (FSGS)
Note Autosomal dominant point mutations in ACTN4 are associated with inherited form of FSGS. Aberrant α-actinin 4 disrupts glomerular podocytes especially their foot processes, which are essential in blood-urine barrier function. Clinically the disease causes proteinuria and deteriorating renal function. Mutant α-actinin 4 aggregates in the cytosol of podocytes and degrades faster than the normal molecule (Yao et al., 2004).
  
  
Entity Autoimmune diseases - Systemic lupus erythematodes (SLE)
Note Autoantibodies against double stranded DNA cross-reacting with α-actinin in the renal structures are associated with the development lupus nephritis (Mostoslavsky et al., 2001). Lupus-prone mouse strain overexpresses α-actinin 1 and 4 in glomerular mesangial cells (Zhao et al., 2006). In patients with lupus nephritis clinical studies have suggested the link between anti-α-actinin autoantibodies and kidney involvement (Becker-Merok et al., 2006), however in the reports there is no discrimination between the 2 "non-muscle" α-actinin isoforms. Given the fact that α-actinin 4 is highly expressed in the affected renal structures in SLE nephritis, the involvement of isoform 4 is probable.
  
  
Entity Autoimmune hepatitis type I
Note Autoantibodies against α-actinin are proposed as markers for severity and activity of autoimmune hepatitis type I (Gueguen et al., 2006). However, there is no report so far describing the exact α-actinin isoform as a target antigen.
  

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Liu QY, Lei JX, LeBlanc J, Sodja C, Ly D, Charlebois C, Walker PR, Yamada T, Hirohashi S, Sikorska M.
Cell Death Differ. 2004 Jun;11(6):645-54.
PMID 15002038
 
Mutant alpha-actinin-4 promotes tumorigenicity and regulates cell motility of a human lung carcinoma.
Menez J, Le Maux Chansac B, Dorothee G, Vergnon I, Jalil A, Carlier MF, Chouaib S, Mami-Chouaib F.
Oncogene. 2004 Apr 8;23(15):2630-9.
PMID 15048094
 
Isolation of DNA sequences amplified at chromosome 19q13.1-q13.2 including the AKT2 locus in human pancreatic cancer.
Miwa W, Yasuda J, Murakami Y, Yashima K, Sugano K, Sekine T, Kono A, Egawa S, Yamaguchi K, Hayashizaki Y, Sekiya T.
Biochem Biophys Res Commun. 1996 Aug 23;225(3):968-74.
PMID 8780719
 
Diagnostic and prognostic significance of the alternatively spliced ACTN4 variant in high-grade neuroendocrine pulmonary tumours.
Miyanaga A, Honda K, Tsuta K, Masuda M, Yamaguchi U, Fujii G, Miyamoto A, Shinagawa S, Miura N, Tsuda H, Sakuma T, Asamura H, Gemma A, Yamada T.
Ann Oncol. 2013 Jan;24(1):84-90. doi: 10.1093/annonc/mds215. Epub 2012 Aug 10.
PMID 22887464
 
Lupus anti-DNA autoantibodies cross-react with a glomerular structural protein: a case for tissue injury by molecular mimicry.
Mostoslavsky G, Fischel R, Yachimovich N, Yarkoni Y, Rosenmann E, Monestier M, Baniyash M, Eilat D.
Eur J Immunol. 2001 Apr;31(4):1221-7.
PMID 11298348
 
Involvement of actinin-4 in the recruitment of JRAB/MICAL-L2 to cell-cell junctions and the formation of functional tight junctions.
Nakatsuji H, Nishimura N, Yamamura R, Kanayama HO, Sasaki T.
Mol Cell Biol. 2008 May;28(10):3324-35. doi: 10.1128/MCB.00144-08. Epub 2008 Mar 10.
PMID 18332111
 
The human non-muscle alpha-actinin protein encoded by the ACTN4 gene suppresses tumorigenicity of human neuroblastoma cells.
Nikolopoulos SN, Spengler BA, Kisselbach K, Evans AE, Biedler JL, Ross RA.
Oncogene. 2000 Jan 20;19(3):380-6.
PMID 10656685
 
Alpha-actinin: a multidisciplinary protein with important role in B-cell driven autoimmunity.
Oikonomou KG, Zachou K, Dalekos GN.
Autoimmun Rev. 2011 May;10(7):389-96. doi: 10.1016/j.autrev.2010.12.009. Epub 2011 Jan 15. (REVIEW)
PMID 21241830
 
Alpha-actinin revisited: a fresh look at an old player.
Otey CA, Carpen O.
Cell Motil Cytoskeleton. 2004 Jun;58(2):104-11. (REVIEW)
PMID 15083532
 
Two distinct classes of CCAAT box elements that bind nuclear factor-Y/alpha-actinin-4: potential role in human CYP1A1 regulation.
Poch MT, Al-Kassim L, Smolinski SM, Hines RN.
Toxicol Appl Pharmacol. 2004 Sep 15;199(3):239-50.
PMID 15364540
 
Alpha-actinin 1 and alpha-actinin 4: contrasting roles in the survival, motility, and RhoA signaling of astrocytoma cells.
Quick Q, Skalli O.
Exp Cell Res. 2010 Apr 15;316(7):1137-47. doi: 10.1016/j.yexcr.2010.02.011. Epub 2010 Feb 12.
PMID 20156433
 
The carboxyl tail of alpha-actinin-4 regulates its susceptibility to m-calpain and thus functions in cell migration and spreading.
Shao H, Travers T, Camacho CJ, Wells A.
Int J Biochem Cell Biol. 2013 Jun;45(6):1051-63. doi: 10.1016/j.biocel.2013.02.015. Epub 2013 Mar 1.
PMID 23466492
 
Alpha-actinin structure and regulation.
Sjoblom B, Salmazo A, Djinovic-Carugo K.
Cell Mol Life Sci. 2008 Sep;65(17):2688-701. doi: 10.1007/s00018-008-8080-8. (REVIEW)
PMID 18488141
 
Molecular evolution and structure of alpha-actinin.
Virel A, Backman L.
Mol Biol Evol. 2004 Jun;21(6):1024-31. Epub 2004 Mar 10.
PMID 15014165
 
A training-testing approach to the molecular classification of resected non-small cell lung cancer.
Yamagata N, Shyr Y, Yanagisawa K, Edgerton M, Dang TP, Gonzalez A, Nadaf S, Larsen P, Roberts JR, Nesbitt JC, Jensen R, Levy S, Moore JH, Minna JD, Carbone DP.
Clin Cancer Res. 2003 Oct 15;9(13):4695-704.
PMID 14581339
 
Actinin-4 gene amplification in ovarian cancer: a candidate oncogene associated with poor patient prognosis and tumor chemoresistance.
Yamamoto S, Tsuda H, Honda K, Onozato K, Takano M, Tamai S, Imoto I, Inazawa J, Yamada T, Matsubara O.
Mod Pathol. 2009 Apr;22(4):499-507. doi: 10.1038/modpathol.2008.234. Epub 2009 Jan 16.
PMID 19151661
 
Alpha-actinin-4-mediated FSGS: an inherited kidney disease caused by an aggregated and rapidly degraded cytoskeletal protein.
Yao J, Le TC, Kos CH, Henderson JM, Allen PG, Denker BM, Pollak MR.
PLoS Biol. 2004 Jun;2(6):e167. Epub 2004 Jun 15.
PMID 15208719
 
Differential binding of cross-reactive anti-DNA antibodies to mesangial cells: the role of alpha-actinin.
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J Immunol. 2006 Jun 15;176(12):7704-14.
PMID 16751418
 

Citation

This paper should be referenced as such :
Zankov, DP ; Ogita, H
ACTN4 (actinin, alpha 4)
Atlas Genet Cytogenet Oncol Haematol. 2013;17(10):663-669.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/ACTN4ID562ch19q13.html


Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 1 ]
  Lung: Translocations in Squamous Cell Carcinoma


External links

Nomenclature
HGNC (Hugo)ACTN4   166
Cards
AtlasACTN4ID562ch19q13
Entrez_Gene (NCBI)ACTN4  81  actinin alpha 4
AliasesACTININ-4; FSGS; FSGS1
GeneCards (Weizmann)ACTN4
Ensembl hg19 (Hinxton)ENSG00000130402 [Gene_View]  chr19:39138267-39221171 [Contig_View]  ACTN4 [Vega]
Ensembl hg38 (Hinxton)ENSG00000130402 [Gene_View]  chr19:39138267-39221171 [Contig_View]  ACTN4 [Vega]
ICGC DataPortalENSG00000130402
TCGA cBioPortalACTN4
AceView (NCBI)ACTN4
Genatlas (Paris)ACTN4
WikiGenes81
SOURCE (Princeton)ACTN4
Genetics Home Reference (NIH)ACTN4
Genomic and cartography
GoldenPath hg19 (UCSC)ACTN4  -     chr19:39138267-39221171 +  19q13   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)ACTN4  -     19q13   [Description]    (hg38-Dec_2013)
EnsemblACTN4 - 19q13 [CytoView hg19]  ACTN4 - 19q13 [CytoView hg38]
Mapping of homologs : NCBIACTN4 [Mapview hg19]  ACTN4 [Mapview hg38]
OMIM603278   604638   
Gene and transcription
Genbank (Entrez)AA478431 AA847056 AK299955 AK304554 AK309361
RefSeq transcript (Entrez)NM_001322033 NM_004924
RefSeq genomic (Entrez)NC_000019 NC_018930 NG_007082 NT_011109 NW_004929415
Consensus coding sequences : CCDS (NCBI)ACTN4
Cluster EST : UnigeneHs.270291 [ NCBI ]
CGAP (NCI)Hs.270291
Alternative Splicing GalleryENSG00000130402
Gene ExpressionACTN4 [ NCBI-GEO ]   ACTN4 [ EBI - ARRAY_EXPRESS ]   ACTN4 [ SEEK ]   ACTN4 [ MEM ]
Gene Expression Viewer (FireBrowse)ACTN4 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)81
GTEX Portal (Tissue expression)ACTN4
Protein : pattern, domain, 3D structure
UniProt/SwissProtO43707   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtO43707  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProO43707
Splice isoforms : SwissVarO43707
PhosPhoSitePlusO43707
Domaine pattern : Prosite (Expaxy)ACTININ_1 (PS00019)    ACTININ_2 (PS00020)    CH (PS50021)    EF_HAND_1 (PS00018)    EF_HAND_2 (PS50222)   
Domains : Interpro (EBI)Actinin_actin-bd_CS    ACTN4    CH-domain    EF-hand-dom_pair    EF-hand_Ca_insen    EF_Hand_1_Ca_BS    EF_hand_dom    Spectrin/alpha-actinin    Spectrin_repeat   
Domain families : Pfam (Sanger)CH (PF00307)    EFhand_Ca_insen (PF08726)    Spectrin (PF00435)   
Domain families : Pfam (NCBI)pfam00307    pfam08726    pfam00435   
Domain families : Smart (EMBL)CH (SM00033)  EFh (SM00054)  SPEC (SM00150)  
Conserved Domain (NCBI)ACTN4
DMDM Disease mutations81
Blocks (Seattle)ACTN4
PDB (SRS)1WLX    1YDI    2R0O   
PDB (PDBSum)1WLX    1YDI    2R0O   
PDB (IMB)1WLX    1YDI    2R0O   
PDB (RSDB)1WLX    1YDI    2R0O   
Structural Biology KnowledgeBase1WLX    1YDI    2R0O   
SCOP (Structural Classification of Proteins)1WLX    1YDI    2R0O   
CATH (Classification of proteins structures)1WLX    1YDI    2R0O   
SuperfamilyO43707
Human Protein AtlasENSG00000130402
Peptide AtlasO43707
HPRD05222
IPIIPI00013808   IPI00845465   IPI00908776   IPI00908458   IPI01015738   IPI00942539   
Protein Interaction databases
DIP (DOE-UCLA)O43707
IntAct (EBI)O43707
FunCoupENSG00000130402
BioGRIDACTN4
STRING (EMBL)ACTN4
ZODIACACTN4
Ontologies - Pathways
QuickGOO43707
Ontology : AmiGORNA polymerase II regulatory region sequence-specific DNA binding  response to hypoxia  stress fiber  nucleoside binding  platelet degranulation  actin binding  integrin binding  calcium ion binding  protein binding  extracellular region  extracellular space  intracellular  nucleus  cytoplasm  brush border  cell-cell junction  focal adhesion  protein transport  actin cytoskeleton  Z disc  vesicle transport along actin filament  positive regulation of cell migration  ligand-dependent nuclear receptor transcription coactivator activity  intracellular ribonucleoprotein complex  cortical cytoskeleton  platelet alpha granule lumen  pseudopodium  chromatin DNA binding  positive regulation of sodium:proton antiporter activity  nuclear hormone receptor binding  peroxisome proliferator activated receptor signaling pathway  protein homodimerization activity  protein homodimerization activity  retinoic acid receptor binding  regulation of apoptotic process  neuron projection  protein complex  ion channel binding  poly(A) RNA binding  protein N-terminus binding  retinoic acid receptor signaling pathway  perinuclear region of cytoplasm  positive regulation of pinocytosis  actin filament binding  actin filament binding  actin filament bundle assembly  negative regulation of cellular component movement  positive regulation of cellular component movement  positive regulation of cellular component movement  extracellular exosome  bicellular tight junction assembly  negative regulation of substrate adhesion-dependent cell spreading  positive regulation of NIK/NF-kappaB signaling  protein localization to bicellular tight junction  regulation of nucleic acid-templated transcription  
Ontology : EGO-EBIRNA polymerase II regulatory region sequence-specific DNA binding  response to hypoxia  stress fiber  nucleoside binding  platelet degranulation  actin binding  integrin binding  calcium ion binding  protein binding  extracellular region  extracellular space  intracellular  nucleus  cytoplasm  brush border  cell-cell junction  focal adhesion  protein transport  actin cytoskeleton  Z disc  vesicle transport along actin filament  positive regulation of cell migration  ligand-dependent nuclear receptor transcription coactivator activity  intracellular ribonucleoprotein complex  cortical cytoskeleton  platelet alpha granule lumen  pseudopodium  chromatin DNA binding  positive regulation of sodium:proton antiporter activity  nuclear hormone receptor binding  peroxisome proliferator activated receptor signaling pathway  protein homodimerization activity  protein homodimerization activity  retinoic acid receptor binding  regulation of apoptotic process  neuron projection  protein complex  ion channel binding  poly(A) RNA binding  protein N-terminus binding  retinoic acid receptor signaling pathway  perinuclear region of cytoplasm  positive regulation of pinocytosis  actin filament binding  actin filament binding  actin filament bundle assembly  negative regulation of cellular component movement  positive regulation of cellular component movement  positive regulation of cellular component movement  extracellular exosome  bicellular tight junction assembly  negative regulation of substrate adhesion-dependent cell spreading  positive regulation of NIK/NF-kappaB signaling  protein localization to bicellular tight junction  regulation of nucleic acid-templated transcription  
Pathways : KEGGFocal adhesion    Adherens junction    Tight junction    Leukocyte transendothelial migration    Regulation of actin cytoskeleton    Amoebiasis    Viral carcinogenesis    Systemic lupus erythematosus    Arrhythmogenic right ventricular cardiomyopathy (ARVC)   
REACTOMEO43707 [protein]
REACTOME Pathways114608 [pathway]   373753 [pathway]   
NDEx NetworkACTN4
Atlas of Cancer Signalling NetworkACTN4
Wikipedia pathwaysACTN4
Orthology - Evolution
OrthoDB81
GeneTree (enSembl)ENSG00000130402
Phylogenetic Trees/Animal Genes : TreeFamACTN4
HOVERGENO43707
HOGENOMO43707
Homologs : HomoloGeneACTN4
Homology/Alignments : Family Browser (UCSC)ACTN4
Gene fusions - Rearrangements
Fusion : MitelmanACTN4/CAPZB [19q13.2/1p36.13]  
Fusion : MitelmanACTN4/FTO [19q13.2/16q12.2]  [t(16;19)(q12;q13)]  
Fusion : MitelmanACTN4/IGF2BP2 [19q13.2/3q27.2]  [t(3;19)(q27;q13)]  
Fusion : MitelmanACTN4/YIF1B [19q13.2/19q13.2]  [t(19;19)(q13;q13)]  
Fusion : MitelmanLSM14A/ACTN4 [19q13.11/19q13.2]  [t(19;19)(q13;q13)]  
Fusion : MitelmanTTC6/ACTN4 [14q21.1/19q13.2]  [t(14;19)(q21;q13)]  
Fusion : COSMICACTN4 [19q13.2]  -  KMT2A [11q23.3]  [fusion_2027]  [fusion_2028]  
Fusion : COSMICKMT2A [11q23.3]  -  ACTN4 [19q13.2]  [fusion_2025]  [fusion_2026]  [fusion_2029]  
Fusion: TCGAACTN4 19q13.2 CAPZB 1p36.13 BRCA
Fusion: TCGAACTN4 19q13.2 FTO 16q12.2 BRCA
Fusion: TCGAACTN4 19q13.2 YIF1B 19q13.2 LUAD
Fusion: TCGALSM14A 19q13.11 ACTN4 19q13.2 BRCA
Fusion: TCGATTC6 14q21.1 ACTN4 19q13.2 PRAD
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerACTN4 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)ACTN4
dbVarACTN4
ClinVarACTN4
1000_GenomesACTN4 
Exome Variant ServerACTN4
ExAC (Exome Aggregation Consortium)ACTN4 (select the gene name)
Genetic variants : HAPMAP81
Genomic Variants (DGV)ACTN4 [DGVbeta]
DECIPHER (Syndromes)19:39138267-39221171  ENSG00000130402
CONAN: Copy Number AnalysisACTN4 
Mutations
ICGC Data PortalACTN4 
TCGA Data PortalACTN4 
Broad Tumor PortalACTN4
OASIS PortalACTN4 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICACTN4  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDACTN4
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch ACTN4
DgiDB (Drug Gene Interaction Database)ACTN4
DoCM (Curated mutations)ACTN4 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)ACTN4 (select a term)
intoGenACTN4
NCG5 (London)ACTN4
Cancer3DACTN4(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM603278    604638   
Orphanet12191   
MedgenACTN4
Genetic Testing Registry ACTN4
NextProtO43707 [Medical]
TSGene81
GENETestsACTN4
Huge Navigator ACTN4 [HugePedia]
snp3D : Map Gene to Disease81
BioCentury BCIQACTN4
ClinGenACTN4
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD81
Chemical/Pharm GKB GenePA23
Clinical trialACTN4
Miscellaneous
canSAR (ICR)ACTN4 (select the gene name)
Probes
Litterature
PubMed182 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineACTN4
EVEXACTN4
GoPubMedACTN4
iHOPACTN4
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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