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MYLK (myosin light chain kinase)

Written2012-06Kui Shen, Ting Wang, Joe GN Garcia
Institute of Personalized Respiratory Medicine, Department of Medicine, University of Illinois, Chicago, IL 60612, USA

(Note : for Links provided by Atlas : click)

Identity

Alias_namesmyosin
Alias_symbol (synonym)MLCK
smMLCK
MYLK1
MLCK1
Other aliasAAT7
KRP
MLCK108
MLCK210
MSTP083
HGNC (Hugo) MYLK
LocusID (NCBI) 4638
Atlas_Id 43364
Location 3q21.1  [Link to chromosome band 3q21]
Location_base_pair Starts at 123612296 and ends at 123884302 bp from pter ( according to hg19-Feb_2009)  [Mapping MYLK.png]
Fusion genes
(updated 2016)
CAPZB (1p36.13) / MYLK (3q21.1)HSPA1B (6p21.33) / MYLK (3q21.1)MYD88 (3p22.2) / MYLK (3q21.1)
MYLK (3q21.1) / MYLK (3q21.1)MYLK (3q21.1) / NXPH1 (7p21.3)MYLK (3q21.1) / SIAE (11q24.2)
MYLK (3q21.1) / TXK (4p12)SLC12A8 (3q21.2) / MYLK (3q21.1)TNFSF13B (13q33.3) / MYLK (3q21.1)
Note Strand: Reverse (minus, -); Genomic Size: 272007.
This gene, a member of the immunoglobulin gene superfamily, encodes myosin light chain kinase (MLCK), which is a calcium/calmodulin dependent kinase that phosphorylates myosin regulatory light chains (Potier et al., 1995) to regulate cell contractility (De Lanerolle et al., 1991; Garcia et al., 1995; Garcia et al., 1997b; Katoh et al., 2001) and cytokinesis (Dulyaninova et al., 2004; Fishkind et al., 1991; Matsumura et al., 2011; Poperechnaya et al., 2000). Multiple transcript variants of this gene have been identified that produce both nonmuscle and smooth muscle isoforms of MLCK (Garcia et al., 1997a; Lazar and Garcia, 1999; Verin et al., 1998b). In addition, using a separate promoter in an intron in the 3' region, it encodes telokin, a small protein identical in sequence to the C-terminus of MLCK (Gallagher and Herring, 1991; Watterson et al., 1999), which functions to stabilize unphosphorylated myosin filaments in smooth muscle (Kudryashov et al., 2002; Shirinsky et al., 1993). A pseudogene of MYLK is located on the p arm of chromosome 3 (Brand-Arpon et al., 1999; Giorgi et al., 2001; Han et al., 2011) (modified from RefSeq, July 2008).

DNA/RNA

 
  The MYLK gene viewed at three different levels of detail (highlighted between two red vertical boundary lines). (1) Overview within chromosome 3. (2) Partial regional view within chromosome 3q21.1-3q21.2. (3) Detailed view within chromosome 3q21.1 showing six of the transcription variants of MLCK, which include nmMLCK1 (NM_053025), 2 (NM_053026), 3A (NM_053027), 3B (NM_053028), and two telokins (NM_053031 and NM_053032). The transcripts are not drawn in exact proportion so that their introns and exons, including CDSs and UTRs, can all be seen at a limited resolution. Abbreviations: Chr, chromosome; CDS, coding sequence; UTR, untranslated region.
Description The gene is composed of 34 exons, 31 out of which are coding exons.
Transcription Multiple MLCK isoforms are produced from the same MYLK gene by alternative splicing or alternative initiation (Lazar and Garcia, 1999; Verin et al., 1998b; Watterson et al., 1999). Six transcript variants have been identified that produce four kinase domain-encoding isoforms and two isoforms of telokin. Additional variants exist but lack full length transcripts. The longest transcript (nmMLCK1), which encodes the full length nonmuscle isoform (NM_053025), is a 7852 bp mRNA with a 5745 bp open reading frame from base pair 283 to 6027.
Pseudogene PGOHUM00000250243, PGOHUM00000238157, and PGOHUM00000238160 (Human Pseudogenes, Build 61). Note: Partially duplicated from the original MYLK gene, the MYLKP1 pseudogene (PGOHUM00000250243) is proposed to negatively regulate MYLK gene expression (Han et al., 2011).

Protein

 
  Representative MLCK protein isoforms shown with select structural/functional information, as compared with the full length isoform (nmMLCK1). The nonmuscle MLCK isoform variants (nmMLCK 1, 2, 3A, 3B) differ in the presence or absence of exons 11 and 30. All nmMLCK variants possess unique amino termini that are absent in the smooth muscle isoform, smMLCK, and two isoforms of telokin. The longer isoform of telokin, differing by one amino acid from its shorter version (with the aa 1790 deletion), is identical to the C-termini of nmMLCK and smMLCK isoforms shown (Watterson et al., 1999). Abbreviations: aa, amino acid; CaM, calmodulin; IgC2, immunoglobulin C-2 type domain; FN3, fibronectin type 3 domain. *Note: NCBI RefSeq NM_053030.2 (NP_444258.1) was permanently suppressed because there was insufficient support for the transcript and the CDS was partial.
Description The full length isoform nmMLCK1 is a 1914-aa protein with a molecular weight of 210715 Da. All isoforms including telokin bind calmodulin (Davis et al., 1996; Gallagher and Herring, 1991; Geguchadze et al., 2004; Katoh et al., 2001). Various MLCK protein isoforms that result from the same MYLK gene (Lazar and Garcia, 1999) by alternative splicing or alternative initiation may be differentially regulated to achieve a tissue-specific spatiotemporal control of the binding (Davis et al., 1996; Dudek et al., 2002; Dudek et al., 2004; Hatch et al., 2001; Kishi et al., 1998) and catalytic activity of MLCK. The full length isoform nmMLCK1 is activated by post-translational modifications (PTMs) such as phosphorylation on Tyr-464 and Tyr-471 (coded by exon 11) (Birukov et al., 2001; Dudek et al., 2010). These PTMs are catalyzed by c-Abl (Dudek et al., 2010), p60Src (Birukov et al., 2001; Garcia et al., 1999), cAMP-dependent protein kinase (PKA) (Garcia et al., 1997a; Verin et al., 1998a) and p21-activated kinases (Goeckeler et al., 2000; Sanders et al., 1999). Additional regulatory mechanisms involve acetylation (Shin et al., 2009), carboxyl-terminal deglutamylation (Rogowski et al., 2010), and kinase activation after thrombin, tumor necrosis factor (TNF), sphingosine 1-phosphate, G proteins, and during cell cycle (Garcia et al., 1995; Petrache et al., 2003; Poperechnaya et al., 2000; Somlyo and Somlyo, 2003; Ye et al., 2006; Ye and Ma, 2008).
Expression The nmMLCK or smMLCK isoforms and telokin are ubiquitously expressed in various adult and fetal tissues and in cultured endothelium with qualitative expression appearing to be neither tissue- nor development-specific (Garcia et al., 1997a; Lazar and Garcia, 1999; Potier et al., 1995; Verin et al., 1998b; Watterson et al., 1999). The nmMLCK 1 and 2 isoforms are dominant isoforms in nonmuscle (endothelial) cells (Brown et al., 2010; Garcia et al., 1997a; Lazar and Garcia, 1999; Verin et al., 1998b).
Localisation Lamellipodium; cytoplasm; cytoskeleton; stress fiber; cytosol; cleavage furrow.
Function Belongs to protein kinase superfamily, non-receptor Ser/Thr protein kinase, EC 2.7.11.18, calcium/calmodulin-dependent protein kinase (CAMK) group, MLCK family. Regulates smooth muscle and nonmuscle cell contractile processes (De Lanerolle et al., 1991; Garcia et al., 1995; Katoh et al., 2001; Somlyo and Somlyo, 2003), via phosphorylation of myosin light chains (MLC), or through a non-kinase activity (Dudek et al., 2004; Herring et al., 2006; Kudryashov et al., 2002; Nakamura et al., 2008; Shirinsky et al., 1993). Regulates cytogenesis (Dulyaninova et al., 2004; Fishkind et al., 1991; Matsumura et al., 2011; Poperechnaya et al., 2000). Regulates other related cellular processes including cell adhesion, migration, morphology, and inflammatory responses (Garcia et al., 1998; Savkovic et al., 2001), e.g., apoptosis (Mills et al., 1998; Petrache et al., 2003; Wright et al., 1993), and vascular permeability (Dudek et al., 2004; Garcia et al., 1995; Garcia et al., 1998; Shen et al., 2010; Vandenbroucke et al., 2008; Yuan et al., 2002), all via the regulation of cytoskeletal rearrangements. Genetic variants in MYLK are implicated in inflammatory disorders such as asthma and acute lung injury (Flores et al., 2007; Gao et al., 2006; Gao et al., 2007). Implicated in tumor formation and metastasis (see below).
Homology The human MYLK gene is conserved in Euteleostomi, with a high percentage of identity in the pairwise alignment of protein/DNA vs. chimpanzee (99,1% / 99,4%), monkey (97,3% / 97,0%), dog (89,1% / 89,0%), mouse (85,9% / 85,6%), rat (85,4% / 86,0%), chicken (71,4% / 68,8%), and zebrafish (63,0% / 65,5%) (Homologene). The paralogs of human MYLK gene include MYLK2-4, DAPK1-3, STK17A and STK17B, and SPEG (Ensembl) (Manning et al., 2002).

Mutations

Note Some protein-coding somatic mutations in MYLK are associated with cancers (Catalogue of Somatic Mutations in Cancer–COSMIC) (Greenman et al., 2007). Several variants of MYLK are associated with familial aortic dissections (Wang et al., 2010). A few race-specific single nucleotide polymorphism (SNP) variants of MYLK, both in coding and noncoding regions, are associated with the susceptibility to acute lung injury, sepsis and severe asthma (Flores et al., 2007; Gao et al., 2006; Gao et al., 2007).
 
  Cancer-associated somatic mutations in MYLK in the protein coding region (Catalogue of Somatic Mutations in Cancer–COSMIC). Abbreviations: CaM, calmodulin; IgC2, immunoglobulin C-2 type domain; FN3, fibronectin type 3 domain; Complex, complex substitutions; Missense, missense substitutions; Nonsense, nonsense substitutions; Silent, silent substitutions.

Implicated in

Note
  
Entity Cancers
Note Myosin light chain kinase (MLCK) plays a crucial role in the cell migration and tumor metastasis. Some somatic mutations in MYLK are associated with cancers (Greenman et al., 2007). MLCK is critical for adhesion turnover at the cell front, a process central to migration (Webb et al., 2004) and it is involved in membrane blebbing (Godin and Ferguson, 2010). Deficiency in MLC phosphorylation causes cytokinesis failure and multipolarity (hence genomic instability) in cancer cells (Wu et al., 2010).
  
  
Entity Breast cancer
Note MLCK activity correlates the recruitment of nonmuscle myosin IIA and myosin IIB into the spreading margin of MDA-MB-231 breast cancer cells, with both myosin isoforms required for cell migration but only myosin IIB critical to lamellar protrusion (Betapudi et al., 2006). MLC phosphorylation by MLCK through β1-integrin is required for actin stress fiber formation and the dormancy-to-proliferation metastatic switch for latent breast cancer cells (Barkan et al., 2008; Barkan et al., 2011). MLCK functions downstream of Ras, MAP kinase kinase (MEK) and extracellular signal regulated kinase (ERK) to promote invasive migration of breast cancer cells in an integrin-selective manner, i.e., mediated by a β1-integrin (probably α5β1) and α5β5, but not by α5β3 (Mierke, 2011; Mierke et al., 2011b; Nguyen et al., 1999; Zhou et al., 2008). Endothelial nmMLCK is activated by invasive breast cancer cells at the invasion site, leading to regional MLC diphosphorylation and myosin contraction. Blocking endothelial MLC diphosphorylation blunts tumor transcellular (i.e., through individual endothelial cells), but not paracellular (i.e., through cell-cell junctions) invasion (Khuon et al., 2010). Human mammary tumor cells exhibit at least two modes of invasive migration, including the extracellular proteolysis-dependent mesenchymal mode (invadopodia-associated extracellular matrix degradation) (Alexander et al., 2008) and the proteolysis-independent amoeboid mode, with both modes mediated by MLCK and Rho kinase ROCK (Alexander et al., 2008; Torka et al., 2006). TNF induction of apoptosis and DNA fragmentation requires MLCK activation in mammary carcinoma and other cancer cell lines (Wright et al., 1993). MLCK is responsible for high proliferative ability of breast cancer cells via anti-apoptosis (Cui et al., 2010). The increase in MLC phosphorylation correlates with apoptotic blebbing (Mills et al., 1998). Subsequent MLC dephosphorylation that results from a proapoptotic agent or MLCK inhibition (inhibitor or antibody) precedes caspase activation (Fazal et al., 2005), which further induces apoptosis in vitro and in vivo, and retards the growth of mammary cancer cells in mice (Fazal et al., 2005; Gu et al., 2006).
  
  
Entity Lung cancer
Note The invasiveness of tumor cells depends in part on their motility, which in turn depends on cytoskeletal function (Minamiya et al., 2005). The expression level of MLCK, the cytoskeletal regulator, correlates with disease recurrence and distant metastasis in non-small cell lung cancer (NSCLC) (Minamiya et al., 2005). E1AF, an Ets family transcription factor frequently overexpressed in NSCLCs, induces motility and invasion as well as tumorigenesis and metastasis in NSCLC cells in a MLCK-dependent pathway (Hakuma et al., 2005). A few anti-cancer drug candidates, including glabridin, 7-chloro-6-piperidin-1-yl-quinoline-5,8-dione (PT-262), and all-trans-retinoic acid (ATRA), inhibit cell metastasis by decreasing cancer cell migration and invasion of human lung adenocarcinoma A549 cells via modulation of expression (Gui et al., 2011) or activity (Tsai et al., 2011a; Tsai et al., 2011b) of MLCK. Glycosylphosphatidylinositol-anchored receptor CD24 is found to enhance invasion of A125 human lung cancer cells through increased generation or transmission of contractile forces which is dependent on MLCK activity (Mierke et al., 2011a).
  
  
Entity Colon cancer
Note MLCK is differentially expressed in microsatellite stable (MSS) sporadic colon cancer and hereditary nonpolyposis colorectal cancer (HNPCC) (Lee et al., 2008). It is suggested to be a potential colon tumor marker. MLCK regulates transendothelial migration of colon cancer cells in E-selectin-mediated activation of p38 MAPK (Tremblay et al., 2006), and possibly via changing cellular contractility by regulation of adhesion sites and stress fibers (Krndija et al., 2010). Inhibition of MLCK suppresses peripheral accumulation of phospho-MLC and Src-induced formation of integrin-dependent adhesions in KM12C colon cancer cells, whereas at the same time restoring E-cadherin redistribution to regions of cell-cell contact (Avizienyte et al., 2004; Avizienyte et al., 2005; Nguyen et al., 2002).
  
  
Entity Prostate cancer
Note Inhibitors of MLCK markedly reduce the invasiveness of prostate cancer cells due to impaired cellular motility (Tohtong et al., 2003). These inhibitors also retard the growth of established prostate tumor in vivo (Gu et al., 2006). MLCK is considered as a central mediator of migration, proliferation and invasion of prostatic adenocarcinoma cell line (Tohtong et al., 2003) downstream of PKC delta (Kharait et al., 2007), boric acid, and phenylboronic acid (McAuley et al., 2011) in DU145 cell line (metastatic prostate cancer cell line). The MYLK gene is one of the top seven most informative genes that discriminate between normal and tumoral prostate conditions by analyzing cDNA microarrays of approximately 25000 genes (Fujita et al., 2008). MLCK is down-regulated by androgens in human prostate cancer cells (Leveille et al., 2009).
  
  
Entity Other cancers
Note MLC phosphorylation or MLCK activation is directly involved in the activation of membrane-associated actomyosin required for the collection of surface proteins into a cap structure in mouse T-lymphoma cells (analogous to muscle cell sliding filament contraction) (Bourguignon et al., 1981; Kerrick and Bourguignon., 1984). Inhibitors of MLCK (ML-7 and ML-9) induce differentiation of human monoblastic leukemia U937 cells (Makishima et al., 1991; Makishima et al., 1993; Yamamoto-Yamaguchi et al., 1996). Apoptotic membrane blebbing is accompanied by increased MLC phosphorylation and regulated by MLCK in PC12, a neuroendocrine tumor cell line (Mills et al, 1998). MLCK regulates the activation of volume-sensitive organic osmolyte/anion channels (VSOAC) by mediating hypotonicity-induced Ca2+ entry (not correlating with MLC phosphorylation) in cervical cancer cells (Shen et al., 2002).
  

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J Muscle Res Cell Motil. 2002;23(4):341-51.
PMID 12630709
 
A single human myosin light chain kinase gene (MLCK; MYLK).
Lazar V, Garcia JG.
Genomics. 1999 Apr 15;57(2):256-67.
PMID 10198165
 
Identification of differentially expressed genes in microsatellite stable HNPCC and sporadic colon cancer.
Lee WS, Seo G, Shin HJ, Yun SH, Yun H, Choi N, Lee J, Son D, Cho J, Kim J, Cho YB, Chun HK, Lee WY.
J Surg Res. 2008 Jan;144(1):29-35. Epub 2007 Oct 22.
PMID 17950328
 
Androgens down-regulate myosin light chain kinase in human prostate cancer cells.
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J Steroid Biochem Mol Biol. 2009 Apr;114(3-5):174-9. Epub 2009 Feb 13.
PMID 19429448
 
Differentiation of human monoblastic leukemia U937 cells induced by inhibitors of myosin light chain kinase and prevention of differentiation by granulocyte-macrophage colony-stimulating factor.
Makishima M, Honma Y, Hozumi M, Nagata N, Motoyoshi K.
Biochim Biophys Acta. 1993 Apr 16;1176(3):245-9.
PMID 8471626
 
The protein kinase complement of the human genome.
Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S.
Science. 2002 Dec 6;298(5600):1912-34. (REVIEW)
PMID 12471243
 
Myosin light chain kinases and phosphatase in mitosis and cytokinesis.
Matsumura F, Yamakita Y, Yamashiro S.
Arch Biochem Biophys. 2011 Jun 15;510(2):76-82. Epub 2011 Mar 21. (REVIEW)
PMID 21396909
 
Phenylboronic acid is a more potent inhibitor than boric acid of key signaling networks involved in cancer cell migration.
McAuley EM, Bradke TA, Plopper GE.
Cell Adh Migr. 2011 Sep-Oct;5(5):382-6.
PMID 21975546
 
Contractile forces contribute to increased glycosylphosphatidylinositol-anchored receptor CD24-facilitated cancer cell invasion.
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J Biol Chem. 2011a Oct 7;286(40):34858-71. Epub 2011 Aug 2.
PMID 21828044
 
Integrin alpha5beta1 facilitates cancer cell invasion through enhanced contractile forces.
Mierke CT, Frey B, Fellner M, Herrmann M, Fabry B.
J Cell Sci. 2011b Feb 1;124(Pt 3):369-83. Epub 2011 Jan 11.
PMID 21224397
 
Cancer cells regulate biomechanical properties of human microvascular endothelial cells.
Mierke CT.
J Biol Chem. 2011 Nov 18;286(46):40025-37. Epub 2011 Sep 22.
PMID 21940631
 
Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation.
Mills JC, Stone NL, Erhardt J, Pittman RN.
J Cell Biol. 1998 Feb 9;140(3):627-36.
PMID 9456322
 
Increased expression of myosin light chain kinase mRNA is related to metastasis in non-small cell lung cancer.
Minamiya Y, Nakagawa T, Saito H, Matsuzaki I, Taguchi K, Ito M, Ogawa J.
Tumour Biol. 2005 May-Jun;26(3):153-7. Epub 2005 Jun 20.
PMID 15970650
 
Role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, a review dedicated to Dr. Setsuro Ebashi.
Nakamura A, Xie C, Zhang Y, Gao Y, Wang HH, Ye LH, Kishi H, Okagaki T, Yoshiyama S, Hayakawa K, Ishikawa R, Kohama K.
Biochem Biophys Res Commun. 2008 Apr 25;369(1):135-43. Epub 2007 Nov 29. (REVIEW)
PMID 18053800
 
Myosin light chain kinase functions downstream of Ras/ERK to promote migration of urokinase-type plasminogen activator-stimulated cells in an integrin-selective manner.
Nguyen DH, Catling AD, Webb DJ, Sankovic M, Walker LA, Somlyo AV, Weber MJ, Gonias SL.
J Cell Biol. 1999 Jul 12;146(1):149-64.
PMID 10402467
 
RhoA- and RhoD-dependent regulatory switch of Galpha subunit signaling by PAR-1 receptors in cellular invasion.
Nguyen QD, Faivre S, Bruyneel E, Rivat C, Seto M, Endo T, Mareel M, Emami S, Gespach C.
FASEB J. 2002 Apr;16(6):565-76.
PMID 11919159
 
Caspase-dependent cleavage of myosin light chain kinase (MLCK) is involved in TNF-alpha-mediated bovine pulmonary endothelial cell apoptosis.
Petrache I, Birukov K, Zaiman AL, Crow MT, Deng H, Wadgaonkar R, Romer LH, Garcia JG.
FASEB J. 2003 Mar;17(3):407-16.
PMID 12631580
 
Localization and activity of myosin light chain kinase isoforms during the cell cycle.
Poperechnaya A, Varlamova O, Lin PJ, Stull JT, Bresnick AR.
J Cell Biol. 2000 Oct 30;151(3):697-708.
PMID 11062269
 
The human myosin light chain kinase (MLCK) from hippocampus: cloning, sequencing, expression, and localization to 3qcen-q21.
Potier MC, Chelot E, Pekarsky Y, Gardiner K, Rossier J, Turnell WG.
Genomics. 1995 Oct 10;29(3):562-70.
PMID 8575746
 
A family of protein-deglutamylating enzymes associated with neurodegeneration.
Rogowski K, van Dijk J, Magiera MM, Bosc C, Deloulme JC, Bosson A, Peris L, Gold ND, Lacroix B, Grau MB, Bec N, Larroque C, Desagher S, Holzer M, Andrieux A, Moutin MJ, Janke C.
Cell. 2010 Nov 12;143(4):564-78.
PMID 21074048
 
Inhibition of myosin light chain kinase by p21-activated kinase.
Sanders LC, Matsumura F, Bokoch GM, de Lanerolle P.
Science. 1999 Mar 26;283(5410):2083-5.
PMID 10092231
 
EPEC-activated ERK1/2 participate in inflammatory response but not tight junction barrier disruption.
Savkovic SD, Ramaswamy A, Koutsouris A, Hecht G.
Am J Physiol Gastrointest Liver Physiol. 2001 Oct;281(4):G890-8.
PMID 11557508
 
Myosin light chain kinase modulates hypotonicity-induced Ca2+ entry and Cl- channel activity in human cervical cancer cells.
Shen MR, Furla P, Chou CY, Ellory JC.
Pflugers Arch. 2002 May;444(1-2):276-85. Epub 2002 Mar 6.
PMID 11976941
 
Myosin light chain kinase in microvascular endothelial barrier function.
Shen Q, Rigor RR, Pivetti CD, Wu MH, Yuan SY.
Cardiovasc Res. 2010 Jul 15;87(2):272-80. Epub 2010 May 17. (REVIEW)
PMID 20479130
 
Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase.
Shin DH, Chun YS, Lee KH, Shin HW, Park JW.
PLoS One. 2009 Oct 14;4(10):e7451.
PMID 19826488
 
A kinase-related protein stabilizes unphosphorylated smooth muscle myosin minifilaments in the presence of ATP.
Shirinsky VP, Vorotnikov AV, Birukov KG, Nanaev AK, Collinge M, Lukas TJ, Sellers JR, Watterson DM.
J Biol Chem. 1993 Aug 5;268(22):16578-83.
PMID 8344938
 
Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase.
Somlyo AP, Somlyo AV.
Physiol Rev. 2003 Oct;83(4):1325-58. (REVIEW)
PMID 14506307
 
Dependence of metastatic cancer cell invasion on MLCK-catalyzed phosphorylation of myosin regulatory light chain.
Tohtong R, Phattarasakul K, Jiraviriyakul A, Sutthiphongchai T.
Prostate Cancer Prostatic Dis. 2003;6(3):212-6.
PMID 12970723
 
ROCK signaling mediates the adoption of different modes of migration and invasion in human mammary epithelial tumor cells.
Torka R, Thuma F, Herzog V, Kirfel G.
Exp Cell Res. 2006 Nov 15;312(19):3857-71. Epub 2006 Sep 3.
PMID 17010335
 
Regulation of transendothelial migration of colon cancer cells by E-selectin-mediated activation of p38 and ERK MAP kinases.
Tremblay PL, Auger FA, Huot J.
Oncogene. 2006 Oct 26;25(50):6563-73. Epub 2006 May 22.
PMID 16715142
 
7-Chloro-6-piperidin-1-yl-quinoline-5,8-dione (PT-262), a novel ROCK inhibitor blocks cytoskeleton function and cell migration.
Tsai CC, Liu HF, Hsu KC, Yang JM, Chen C, Liu KK, Hsu TS, Chao JI.
Biochem Pharmacol. 2011a Apr 1;81(7):856-65. Epub 2011 Jan 26.
PMID 21276421
 
Glabridin inhibits migration, invasion, and angiogenesis of human non-small cell lung cancer A549 cells by inhibiting the FAK/rho signaling pathway.
Tsai YM, Yang CJ, Hsu YL, Wu LY, Tsai YC, Hung JY, Lien CT, Huang MS, Kuo PL.
Integr Cancer Ther. 2011b Dec;10(4):341-9. Epub 2010 Nov 8.
PMID 21059620
 
Regulation of endothelial junctional permeability.
Vandenbroucke E, Mehta D, Minshall R, Malik AB.
Ann N Y Acad Sci. 2008 Mar;1123:134-45. (REVIEW)
PMID 18375586
 
Biochemical regulation of the nonmuscle myosin light chain kinase isoform in bovine endothelium.
Verin AD, Gilbert-McClain LI, Patterson CE, Garcia JG.
Am J Respir Cell Mol Biol. 1998a Nov;19(5):767-76.
PMID 9806741
 
Expression of a novel high molecular-weight myosin light chain kinase in endothelium.
Verin AD, Lazar V, Torry RJ, Labarrere CA, Patterson CE, Garcia JG.
Am J Respir Cell Mol Biol. 1998b Nov;19(5):758-66.
PMID 9806740
 
Mutations in myosin light chain kinase cause familial aortic dissections.
Wang L, Guo DC, Cao J, Gong L, Kamm KE, Regalado E, Li L, Shete S, He WQ, Zhu MS, Offermanns S, Gilchrist D, Elefteriades J, Stull JT, Milewicz DM.
Am J Hum Genet. 2010 Nov 12;87(5):701-7. Epub 2010 Nov 4.
PMID 21055718
 
Analysis of the kinase-related protein gene found at human chromosome 3q21 in a multi-gene cluster: organization, expression, alternative splicing, and polymorphic marker.
Watterson DM, Schavocky JP, Guo L, Weiss C, Chlenski A, Shirinsky VP, Van Eldik LJ, Haiech J.
J Cell Biochem. 1999 Dec 1;75(3):481-91.
PMID 10536370
 
FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly.
Webb DJ, Donais K, Whitmore LA, Thomas SM, Turner CE, Parsons JT, Horwitz AF.
Nat Cell Biol. 2004 Feb;6(2):154-61. Epub 2004 Jan 25.
PMID 14743221
 
Role of protein phosphorylation in TNF-induced apoptosis: phosphatase inhibitors synergize with TNF to activate DNA fragmentation in normal as well as TNF-resistant U937 variants.
Wright SC, Zheng H, Zhong J, Torti FM, Larrick JW.
J Cell Biochem. 1993 Nov;53(3):222-33.
PMID 8263039
 
Deficiency in myosin light-chain phosphorylation causes cytokinesis failure and multipolarity in cancer cells.
Wu Q, Sahasrabudhe RM, Luo LZ, Lewis DW, Gollin SM, Saunders WS.
Oncogene. 2010 Jul 22;29(29):4183-93. Epub 2010 May 24.
PMID 20498637
 
Reversible differentiation of human monoblastic leukemia U937 cells by ML-9, an inhibitor of myosin light chain kinase.
Yamamoto-Yamaguchi Y, Makishima M, Kanatani Y, Kasukabe T, Honma Y.
Exp Hematol. 1996 May;24(6):682-9.
PMID 8635523
 
Molecular mechanism of tumor necrosis factor-alpha modulation of intestinal epithelial tight junction barrier.
Ye D, Ma I, Ma TY.
Am J Physiol Gastrointest Liver Physiol. 2006 Mar;290(3):G496-504.
PMID 16474009
 
Cellular and molecular mechanisms that mediate basal and tumour necrosis factor-alpha-induced regulation of myosin light chain kinase gene activity.
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J Cell Mol Med. 2008 Aug;12(4):1331-46. Epub 2008 Mar 14.
PMID 18363837
 
Myosin light chain phosphorylation in neutrophil-stimulated coronary microvascular leakage.
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Circ Res. 2002 Jun 14;90(11):1214-21.
PMID 12065325
 
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Citation

This paper should be referenced as such :
Shen, K ; Wang, T ; Garcia, JGN
MYLK (myosin light chain kinase)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(12):901-908.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/MYLKID43364ch3q21.html


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


External links

Nomenclature
HGNC (Hugo)MYLK   7590
Cards
AtlasMYLKID43364ch3q21
Entrez_Gene (NCBI)MYLK  4638  myosin light chain kinase
AliasesAAT7; KRP; MLCK; MLCK1; 
MLCK108; MLCK210; MSTP083; MYLK1; smMLCK
GeneCards (Weizmann)MYLK
Ensembl hg19 (Hinxton)ENSG00000065534 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000065534 [Gene_View]  chr3:123612296-123884302 [Contig_View]  MYLK [Vega]
ICGC DataPortalENSG00000065534
TCGA cBioPortalMYLK
AceView (NCBI)MYLK
Genatlas (Paris)MYLK
WikiGenes4638
SOURCE (Princeton)MYLK
Genetics Home Reference (NIH)MYLK
Genomic and cartography
GoldenPath hg38 (UCSC)MYLK  -     chr3:123612296-123884302 -  3q21.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)MYLK  -     3q21.1   [Description]    (hg19-Feb_2009)
EnsemblMYLK - 3q21.1 [CytoView hg19]  MYLK - 3q21.1 [CytoView hg38]
Mapping of homologs : NCBIMYLK [Mapview hg19]  MYLK [Mapview hg38]
OMIM600922   613780   
Gene and transcription
Genbank (Entrez)###############################################################################################################################################################################################################################################################
RefSeq transcript (Entrez)NM_001321309 NM_005965 NM_053025 NM_053026 NM_053027 NM_053028 NM_053029 NM_053030 NM_053031 NM_053032
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)MYLK
Cluster EST : UnigeneHs.477375 [ NCBI ]
CGAP (NCI)Hs.477375
Alternative Splicing GalleryENSG00000065534
Gene ExpressionMYLK [ NCBI-GEO ]   MYLK [ EBI - ARRAY_EXPRESS ]   MYLK [ SEEK ]   MYLK [ MEM ]
Gene Expression Viewer (FireBrowse)MYLK [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)4638
GTEX Portal (Tissue expression)MYLK
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ15746   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ15746  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ15746
Splice isoforms : SwissVarQ15746
Catalytic activity : Enzyme2.7.11.18 [ Enzyme-Expasy ]   2.7.11.182.7.11.18 [ IntEnz-EBI ]   2.7.11.18 [ BRENDA ]   2.7.11.18 [ KEGG ]   
PhosPhoSitePlusQ15746
Domaine pattern : Prosite (Expaxy)FN3 (PS50853)    IG_LIKE (PS50835)    PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_ST (PS00108)   
Domains : Interpro (EBI)FN3_dom    Ig-like_dom    Ig-like_fold    Ig_I-set    Ig_sub    Ig_sub2    Kinase-like_dom    Prot_kinase_dom    Protein_kinase_ATP_BS    Ser/Thr_kinase_AS    Telokin/Myosin_light_ch_kin   
Domain families : Pfam (Sanger)fn3 (PF00041)    I-set (PF07679)    Pkinase (PF00069)   
Domain families : Pfam (NCBI)pfam00041    pfam07679    pfam00069   
Domain families : Smart (EMBL)FN3 (SM00060)  IG (SM00409)  IGc2 (SM00408)  S_TKc (SM00220)  
Conserved Domain (NCBI)MYLK
DMDM Disease mutations4638
Blocks (Seattle)MYLK
PDB (SRS)2CQV    2K0F    2YR3   
PDB (PDBSum)2CQV    2K0F    2YR3   
PDB (IMB)2CQV    2K0F    2YR3   
PDB (RSDB)2CQV    2K0F    2YR3   
Structural Biology KnowledgeBase2CQV    2K0F    2YR3   
SCOP (Structural Classification of Proteins)2CQV    2K0F    2YR3   
CATH (Classification of proteins structures)2CQV    2K0F    2YR3   
SuperfamilyQ15746
Human Protein AtlasENSG00000065534
Peptide AtlasQ15746
HPRD02952
IPIIPI00336081   IPI00221255   IPI00855853   IPI00955810   IPI00791924   IPI00221259   IPI00791032   IPI00736561   IPI01015026   IPI00385099   IPI00550936   IPI00946657   
Protein Interaction databases
DIP (DOE-UCLA)Q15746
IntAct (EBI)Q15746
FunCoupENSG00000065534
BioGRIDMYLK
STRING (EMBL)MYLK
ZODIACMYLK
Ontologies - Pathways
QuickGOQ15746
Ontology : AmiGOstress fiber  actin binding  myosin light chain kinase activity  protein binding  calmodulin binding  ATP binding  cytoplasm  cytosol  protein phosphorylation  muscle contraction  smooth muscle contraction  smooth muscle contraction  tonic smooth muscle contraction  lamellipodium  positive regulation of cell migration  bleb assembly  cleavage furrow  metal ion binding  positive regulation of calcium ion transport  aorta smooth muscle tissue morphogenesis  extracellular exosome  cellular hypotonic response  positive regulation of wound healing  
Ontology : EGO-EBIstress fiber  actin binding  myosin light chain kinase activity  protein binding  calmodulin binding  ATP binding  cytoplasm  cytosol  protein phosphorylation  muscle contraction  smooth muscle contraction  smooth muscle contraction  tonic smooth muscle contraction  lamellipodium  positive regulation of cell migration  bleb assembly  cleavage furrow  metal ion binding  positive regulation of calcium ion transport  aorta smooth muscle tissue morphogenesis  extracellular exosome  cellular hypotonic response  positive regulation of wound healing  
Pathways : KEGGCalcium signaling pathway    Vascular smooth muscle contraction    Focal adhesion    Regulation of actin cytoskeleton    Gastric acid secretion   
REACTOMEQ15746 [protein]
REACTOME PathwaysR-HSA-5627123 [pathway]   
NDEx NetworkMYLK
Atlas of Cancer Signalling NetworkMYLK
Wikipedia pathwaysMYLK
Orthology - Evolution
OrthoDB4638
GeneTree (enSembl)ENSG00000065534
Phylogenetic Trees/Animal Genes : TreeFamMYLK
HOVERGENQ15746
HOGENOMQ15746
Homologs : HomoloGeneMYLK
Homology/Alignments : Family Browser (UCSC)MYLK
Gene fusions - Rearrangements
Fusion : MitelmanHSPA1B/MYLK [6p21.33/3q21.1]  [t(3;6)(q21;p21)]  
Fusion : MitelmanMYLK/NXPH1 [3q21.1/7p21.3]  [t(3;7)(q21;p21)]  
Fusion : MitelmanMYLK/SIAE [3q21.1/11q24.2]  [t(3;11)(q21;q24)]  
Fusion : MitelmanMYLK/TXK [3q21.1/4p12]  [t(3;4)(q21;p12)]  
Fusion : MitelmanTNFSF13B/MYLK [13q33.3/3q21.1]  [t(3;13)(q21;q33)]  
Fusion: TCGAHSPA1B 6p21.33 MYLK 3q21.1 PRAD
Fusion: TCGAMYLK 3q21.1 NXPH1 7p21.3 KIRC
Fusion: TCGAMYLK 3q21.1 SIAE 11q24.2 KIRC
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerMYLK [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)MYLK
dbVarMYLK
ClinVarMYLK
1000_GenomesMYLK 
Exome Variant ServerMYLK
ExAC (Exome Aggregation Consortium)MYLK (select the gene name)
Genetic variants : HAPMAP4638
Genomic Variants (DGV)MYLK [DGVbeta]
DECIPHERMYLK [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisMYLK 
Mutations
ICGC Data PortalMYLK 
TCGA Data PortalMYLK 
Broad Tumor PortalMYLK
OASIS PortalMYLK [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICMYLK  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDMYLK
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 MYLK
DgiDB (Drug Gene Interaction Database)MYLK
DoCM (Curated mutations)MYLK (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)MYLK (select a term)
intoGenMYLK
NCG5 (London)MYLK
Cancer3DMYLK(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM600922    613780   
Orphanet12138   
MedgenMYLK
Genetic Testing Registry MYLK
NextProtQ15746 [Medical]
TSGene4638
GENETestsMYLK
Target ValidationMYLK
Huge Navigator MYLK [HugePedia]
snp3D : Map Gene to Disease4638
BioCentury BCIQMYLK
ClinGenMYLK (curated)
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD4638
Chemical/Pharm GKB GenePA31388
Clinical trialMYLK
Miscellaneous
canSAR (ICR)MYLK (select the gene name)
Probes
Litterature
PubMed114 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineMYLK
EVEXMYLK
GoPubMedMYLK
iHOPMYLK
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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