HSPB1 (Heat-Shock 27 kDa Protein 1)

2009-03-01   Ewa Laskowska  , Dorota Kuczyńska-Wiśnik  , Ewelina Matuszewska  

Department of Biochemistry, University of Gdańsk, Kładki 24, 80-952 Gdańsk, Poland

Identity

HGNC
LOCATION
7q11.23
LOCUSID
ALIAS
CMT2F,HEL-S-102,HMN2B,HS.76067,HSP27,HSP28,Hsp25,SRP27
FUSION GENES

DNA/RNA

Description

The DNA sequence (1.69 Kb) contains 3 exons.

Transcription

The transcript is 847 bp.

Pseudogene

Two pseudogenes have been identified:
- a processed retropseudogene lacking promoter elements on Xp11.23 (Hickey et al., 1996);
- a 5-truncated semiprocessed retropseudogene on 9q13-9q21 (Kappe et al., 2003).

Proteins

Note

HspB1 belongs to the ubiquitous family of small heat shock proteins (sHsps). sHsps are characterized by low molecular mass (12-30 kDa), a conserved C-terminal "a-crystallin" domain and oligomeric structure. sHsps bind denatured proteins and facilitate their refolding by the ATP-dependent molecular chaperones of the Hsp70 family (Haslbeck et al., 2005; Sun and MacRae, 2005).
Atlas Image
Fig.1. HspB1 contains an N-terminal hydrophobic domain with a WDFP motif and an alpha-crystallin domain at residues Glu87-Pro168. The arrows indicate phosphorylation sites at serines 15, 78 and 82.

Description

HspB1 is a protein of 205 amino acids (22783 Da), which can be phosphorylated at serines 15, 78 and 82 by mitogen- activated protein kinases associated protein kinases (MAPKAP kinase 2, MAPKAP kinase 3). Various signals modulate HspB1 phosphorylation: growth factors, tumor necrosis factor, differentiating agents, heat and oxidative stress (Arrigo et al., 2007). HspB1 forms oligomers up to 1000 kDa, which are dynamic structures. Phosphorylation results in a decrease size of the oligomers (Kato et al., 1994; Rogalla et al., 1999). Dissociation of the oligomers is required for recognition of protein substrates (Shashidharamurthy et al., 2005). It has been reported that HspB1 forms heterooligomers with other sHsps: alphaB-crystallin (HspB5) and Hsp20 (HspB6) (Zantema et al., 1992; Sugiyama et al., 2000; Bukach et al., 2009).

Expression

Ubiquitous, produced constutively at high levels in heart and skeletal muscles (Sugiyama et al., 2000); overexpressed in response to a wide variety of physiological and environmental insults; produced at high levels in many tumors (Garrido et al., 2006). Increased expression of HspB1 in response to the aggregation of proteins specific for conformational diseases have been reported by several authors (Outeiro et al., 2006; Vleminckx et al., 2002).

Localisation

Cytosol, nucleus. HspB1 has been identified as a component of the nuclear speckles, structures implied in RNA processing (Bryantsev et al., 2007).
HspB1 interacts with actin, intermediat filaments and microtubules (Landry and Huot, 1995; Mounier and Arrigo, 2002; Lee et al., 2005; Hino et al., 2000; Jonak et al., 2002). During ischemia in muscles, HspB1 is translocated from the cytosol to myofibryls (Golenhoffen et al., 2004).
HspB1 accumulates in protein aggregates associated with conformational diseases: Parkinsons disease (Outeiro et al., 2006; Zourlidou et al., 2004), Alexander disease (Iwaki et al., 1993), Alzheimers disease (Wilhelmus et al., 2006).
HspB1 was also detected as a surface membrane protein in some cancer cell types (Shin et al., 2003).

Function

HspB1 acts as an ATP-independent molecular chaperone and prevents irreversible aggregation of bound substrates in vitro (Jakob et al., 1993).
HspB1 is involved in the remodeling of cytoskeleton during embryogenesis and protection of the cytoskeleton in cells exposed to various stresses, particularly in the skeletal and cardiac muscles (Mounier and Arrigo, 2002; Sugiyama et al., 2000; Golenhofen et al., 2004; Salinthone et al., 2008). HspB1 phosphorylated by p38 MAP kinase is necessary for migration of vascular smooth muscle cells, neutrophils, fibroblasts and breast epithelial cells (Salinthone et al., 2008).
HspB1 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes (Cuesta et al., 2000).
HspB1 interacts with different proteins of the programmed cell death machinery and thereby blocks apoptosis at distinct key points. It has been demonstrated that HspB1 sequesters cytochrome C and thus, prevents assembly of the apoptosome (Bruey et al., 2000a; Concannon et al., 2001). The release of Smac/Diablo from mitochondria is also blocked by HspB1 (Chauhan et al., 2003). In addition, HspB1 inhibits activation of procaspase-3 by caspase 9 (Garrido et al., 1999; Concannon et al., 2001). HspB1 prevents translocation of pro-apoptotic Bid to mitochondria by stabilization of actin microfilaments (Paul et al., 2002). Havasi et al. (2008) demonstrated that HspB1 inhibits activation of pro-apoptotic Bax protein via a phosphatidylinositol 3-kinase-dependent mechanism. In the extrinsic pathway (receptor-mediated cell death) HspB1 prevents interaction of DAXX (death domain associated protein) with Fas death receptor and protein kinase Ask1 in caspase-independent pathway (Charette et al., 2000). It has been reported by Rane et al. (2003) that HspB1 controls apoptosis by binding cytoprotective protein kinase B (Akt). Anti-oxidant properties of HspB1 play an important function in the regulation of apoptosis. HspB1 maintain glutathione in its reduced form and decrease the amount of reactive oxygen species (ROS) produced in cells exposed to oxidative stress or tumor necrosis factor TNFalpha (Arrigo et al., 2007). HspB1 may indirectly affect apoptosis by promoting degradation of death regulatory proteins by ubiquitin-proteasome pathway. Under stress conditions HspB1 stimulates ubiquitination of I-kappaBalpha, an inhibitor of the anti-apoptotic transcription factor NF-kappaB, and p27Kip1, a cyclin-dependent kinase inhibitor. The HspB1- mediated proteolysis of p27Kip1 facilitates progression from Go/G1 to S-phase of the cell cycle (Parcellier et al., 2006).
In cancer cells HspB1 participates in oncogenesis and resistance to chemotherapy (see below). It has also been reported that expression of recombinant HspB1 at elevated levels leads to protection of human mammary epithelial cells from doxorubicin. The protection is associated with suppression of the doxorubicin-induced senescence, where HspB1 inhibits p53-mediated induction of p21 (OCallaghan-Sunol et al., 2007). However, Venkatakrishnan and co-workers (2008) demonstrated that HspB1 causes p21 upregulation and G2/M phase cell cycle arrest in doxorubicin-treated fibroblasts.

Homology

HspB1 shares homology trough the conserved alpha-crystallin domain with other members of the sHsps family. Eleven human sHsps have been identified so far: HspB1 (Hsp27) HspB2, HspB3, alphaA-crystallin (HspB4), alphaB-crystallin (HspB5), Hsp20 (HspB6), cvHsp (HspB7), HspB8 (H11), HspB9, HspB10 (ODF1) and Hsp16.2 (Kappe et al., 2003; Bellyei et al., 2007).

Mutations

Atlas Image
Fig2. Distribution of HSPB1 mutations in dHMN II and CMT2F patients.
dHMN: distal hereditary motor neuropathy, CMT: Charcot-Marie-Tooth type 2F disease, AD: autosomal dominant, AR: autosomal recessive.

Germinal

Mutations in the HSPB1 gene were found to cause distal hereditary motor neuropathy type II (dHMN II) or Charcot-Marie-Tooth disease type 2F (CMT2F). Five of the mutations are located in the alpha-crystallin domain (see figure 2).
Dierick and co-workers (2007) identified a HSPB1 promoter variant (c.-217T>C) in an ALS patient, which drastically impaired the HSPB1 heat shock response.

Somatic

Not known.

Implicated in

Entity name
Various cancers
Disease
Increased levels of HspB1 have been detected in breast cancer, ovarian cancer, osteosarcomas, endometrial cancer and leukemias (Garrido et al., 2006; Ciocca and Calderwood, 2005). It was also reported that the pattern of HspB1 phosphorylation in tumor cells is different from that observed in nontransformed cells (Sarto et al., 2004; Tremolada et al., 2005).
Prognosis
Overexpression of HspB1 correlates with poor prognosis in gastric, liver, prostate carcinoma and osteosarcomas (Glaessgen et al., 2008; Romani et al., 2007; Ciocca and Calderwood., 2005).
Increased IbpB1 expression is associated with a favorable prognosis in schistosomiasis-associated bladder carcinoma (El-Meghawry El-Kenawy et al., 2008), neuroblastoma (Zanini et al., 2007) and non-small cell lung carcinoma (Malusecka et al., 2008).
Patients with reduced HspB1 expression have poorer survival rates in oral squamous cell carcinoma (Lo Muzio et al., 2004) and ovarian carcinoma (Geisler et al., 2004).
Lower lymphocyte HspB1 level is associated with an increased risk of lung cancer (Wang et al., 2008).
Cytogenetics
Not reported.
Hybrid gene
Not known.
Fusion protein
Not known.
Oncogenesis
HspB1 is involved in oncogenesis and resistance to various anti-cancer therapies due to its cytoprotective activities. It is suggested that HspB1 plays a crucial function during metastasis formation (Zhao et al., 2007).
Strategies combining chemo- or radiotherapy with down-regulation of HspB1 have been proposed as effective anti-cancer treatments. The HspB1 knockdown by using small interfering RNA (siRNA) increases sensitivity of human epithelial cells to geldanamycin (McCollum et al., 2006) and pancreatic cancer cells to gemcitabine (Mori-Iwamoto et al., 2007). Blocking HspB1 by antisense RNA restores apoptosis induced by drugs in multiple myeloma cells (Chauhan et al., 2003) and human bladder cancer cells (Kamada et al., 2007). Various cancer cells transfected with antisense Hsp27 cDNA exhibits increased sensitivity to gamma-irradiation (Aloy et al., 2008). Down regulation of HspB1 by interferon C enhances drug sensitivity in oral squamous cell carcinoma (Yonekura et al., 2003). Kim et al. (2007) has demonstrated that a heptapeptide derived from protein kinase C delta (PKC delta)-V5 region sequesters HspB1 and sensitizes human cancer cells to irradiation and cisplatine.
Entity name
Charcot-Marie-Tooth type IIF disease (CMT-IIF) / distal hereditary motor neuropathy (dHMN)
Note
A number of mutations in HspB1 has been identified that are associated with dHMNII or CMT2F (table of figure 2). The exact pathogenic mechanism of the HspB1 mutations is not yet understood. Expression of the mutant HspB1 (P182S) results in the formation of insoluble aggregates, affects assembly of neurofilament network and axonal transport in cortical neurons (Ackerley et al., 2006; Evgrafov et al., 2004; Zhai et al., 2007).
Disease
CMT disease and dHMN belong to a clinically heterogeneous group of disorders characterized by progressive weakness and distal limb muscle atrophy due to nerve degeneration. The neuropathy of CMT affects both motor and sensory nerves. The phenotype of dHMN II resembles CMT2F, but sensory abnormalities are absent in dHMNII.
Entity name
Conformational disorders
Disease
One of the characteristics of neurodegenerative diseases such as Alzheimers disease (AD), Parkinsons disease (PD), amylotrophic lateral sclerosis (ALS) and Huntington disease is the formation of protein aggregates. HspB1 and other molecular chaperones are often detected as components of these aggregates.
Cerebral deposits of intracellular neurofibrylllary tangles and extracellular aggregates of amyloid beta peptide (Abeta) are the pathological hallmarks of Alzheimers disease. Intracellular Lewy bodies associated with Parkinsons disease contain alpha-synuclein. In Huntingtons disease (HD), a proteolytic fragment of the huntingtin protein that contains an expanded polyglutamine tract (polyQ), misfolds and forms aggregates. Rosenthal fibers of Alexander disease are cytoplasmic inclusions within astrocytes, which contain glial fibrillary acidic protein (GFAP) (Iwaki et al., 1993; Der Perng et al., 2006).
Numerous studies indicate that molecular chaperones associated with intra- and extracellular protein deposits, affects their production and toxicity.
It has been reported that HspB1 inhibits assembly of Abeta fibryls in vitro and reduces cerebrovascular toxicity of Abeta (Wilhelmus et al., 2006). HspB1 also inhibits GFAP polymerization (Der Perng et al., 2006) and toxicity induced by overexpression of alpha-synuclein or polyQ in neuronal cells (Outeiro et al., 2006; Zourlidou et al., 2004; Wyttenbach et al., 2002). It is proposed that the sequestering of HspB1 by Rosenthal fibers diminishes its function as an anti-apoptotic factor which in turn results in astrocytes degeneration (Mignot et al., 2004). Similarly, association of HspB1 with mutated Cu/Zn superoxide dismutase 1 (SOD1) may induce apoptosis (Okado-Matsumoto and Fridovich, 2002). Missense mutations in the gene coding for SOD1 cause familial cases of amyotrophic lateral sclerosis (ALS) characterized by the death of large motor neurons in the cerebral cortex and spinal cord (Rakhit and Chakrabartty, 2006).
Entity name
Williams syndrome
Note
Stock et al. (2003) used FISH to map the HspB1 gene and they found that the band 7q11.23 also contains the site of the deletion associated with Williams sydrome (WS). The HSPB1 gene was deleted in three out of six WS patients examined in this study.
Disease
Williams syndrome (WS, also known as Williams- Beuren syndrome, WBS) is a rare neurodevelopmental disorder characterized by multiple anomalies including: typical facial dysmorphisms (elfin face), congenital heart defects, infantile hypercalcemia, mental retardation and growth deficiency.

Article Bibliography

Pubmed IDLast YearTitleAuthors
163687112006A mutation in the small heat-shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes.Ackerley S et al
179805092008Protective role of Hsp27 protein against gamma radiation-induced apoptosis and radiosensitization effects of Hsp27 gene silencing in different human tumor cells.Aloy MT et al
174677012007Hsp27 (HspB1) and alphaB-crystallin (HspB5) as therapeutic targets.Arrigo AP et al
171364962007Inhibition of cell death by a novel 16.2 kD heat shock protein predominantly via Hsp90 mediated lipid rafts stabilization and Akt activation pathway.Bellyei S et al
109807062000Hsp27 negatively regulates cell death by interacting with cytochrome c.Bruey JM et al
176500722007Regulation of stress-induced intracellular sorting and chaperone function of Hsp27 (HspB1) in mammalian cells.Bryantsev AL et al
191008702009Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20).Bukach OV et al
110036562000Inhibition of Daxx-mediated apoptosis by heat shock protein 27.Charette SJ et al
128555652003Hsp27 inhibits release of mitochondrial protein Smac in multiple myeloma cells and confers dexamethasone resistance.Chauhan D et al
185872682008Distal hereditary motor neuropathy in Korean patients with a small heat shock protein 27 mutation.Chung KW et al
160384062005Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications.Ciocca DR et al
114445292001Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c.Concannon CG et al
108591652000Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes.Cuesta R et al
168265122006The Alexander disease-causing glial fibrillary acidic protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and HSP27.Der Perng M et al
176234842007Genetic variant in the HSPB1 promoter region impairs the HSP27 stress response.Dierick I et al
191992682008Heat shock protein expression independently predicts survival outcome in schistosomiasis-associated urinary bladder cancer.El-Meghawry El-Kenawy A et al
151222542004Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy.Evgrafov OV et al
171062612006Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties.Garrido C et al
150322732004HSP27 in patients with ovarian carcinoma: still an independent prognostic indicator at 60 months follow-up.Geisler JP et al
191329822008Heat shock proteins 27, 60 and 70 as prognostic markers of prostate cancer.Glaessgen A et al
154807352004Comparison of the small heat shock proteins alphaB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle.Golenhofen N et al
162057092005Some like it hot: the structure and function of small heat-shock proteins.Haslbeck M et al
182993202008Hsp27 inhibits Bax activation and apoptosis via a phosphatidylinositol 3-kinase-dependent mechanism.Havasi A et al
30198321986Molecular cloning of sequences encoding the human heat-shock proteins and their expression during hyperthermia.Hickey E et al
107776972000Small heat shock protein 27 (HSP27) associates with tubulin/microtubules in HeLa cells.Hino M et al
188321412008Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and sporadic distal HMN/CMT type 2.Houlden H et al
189522412009A clinical phenotype of distal hereditary motor neuronopathy type II with a novel HSPB1 mutation.Ikeda Y et al
83936181993Alpha B-crystallin and 27-kd heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers.Iwaki T et al
80936121993Small heat shock proteins are molecular chaperones.Jakob U et al
121001792002Subcorneal colocalization of the small heat shock protein, hsp27, with keratins and proteins of the cornified cell envelope.Jonak C et al
172186372007Hsp27 knockdown using nucleotide-based therapies inhibit tumor growth and enhance chemotherapy in human bladder cancer cells.Kamada M et al
128206542003The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1-10.Kappé G et al
81576581994Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27.Kato K et al
161557362005Small heat shock protein 27 mutation in a Japanese patient with distal hereditary motor neuropathy.Kijima K et al
176166922007Inhibition of heat shock protein 27-mediated resistance to DNA damaging agents by a novel PKC delta-V5 heptapeptide.Kim EH et al
87146911995Modulation of actin dynamics during stress and physiological stimulation by a signaling pathway involving p38 MAP kinase and heat-shock protein 27.Landry J et al
162642672005Heat shock protein 27 interacts with vimentin and prevents insolubilization of vimentin subunits induced by cadmium.Lee JS et al
147021792004HSP 27 as possible prognostic factor in patients with oral squamous cell carcinoma.Lo Muzio L et al
183838922008Stress proteins HSP27 and HSP70i predict survival in non-small cell lung carcinoma.Malusecka E et al
171081352006Up-regulation of heat shock protein 27 induces resistance to 17-allylamino-demethoxygeldanamycin through a glutathione-mediated mechanism.McCollum AK et al
147702992004Alexander disease: putative mechanisms of an astrocytic encephalopathy.Mignot C et al
179826612007Proteomics finding heat shock protein 27 as a biomarker for resistance of pancreatic cancer cells to gemcitabine.Mori-Iwamoto S et al
123806842002Actin cytoskeleton and small heat shock proteins: how do they interact?Mounier N et al
180898082007Hsp27 modulates p53 signaling and suppresses cellular senescence.O'Callaghan-Sunol C et al
120607162002Amyotrophic lateral sclerosis: a proposed mechanism.Okado-Matsumoto A et al
170814992006Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation.Outeiro TF et al
166411992006HSP27 favors ubiquitination and proteasomal degradation of p27Kip1 and helps S-phase re-entry in stressed cells.Parcellier A et al
117848582002Hsp27 as a negative regulator of cytochrome C release.Paul C et al
168145282006Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis.Rakhit R et al
127403622003Heat shock protein 27 controls apoptosis by regulating Akt activation.Rane MJ et al
103833931999Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation.Rogalla T et al
181546392007The expression of HSP27 is associated with poor clinical outcome in intrahepatic cholangiocarcinoma.Romani AA et al
185792102008Small heat shock proteins in smooth muscle.Salinthone S et al
152741192004Expression of heat shock protein 27 in human renal cell carcinoma.Sarto C et al
155426042005Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme.Shashidharamurthy R et al
124937732003Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function.Shin BK et al
128385492003Heat shock protein 27 gene: chromosomal and molecular location and relationship to Williams syndrome.Stock AD et al
106256512000Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation.Sugiyama Y et al
159437972005The small heat shock proteins and their role in human disease.Sun Y et al
160877582005Mutation analysis of the small heat shock protein 27 gene in chinese patients with Charcot-Marie-Tooth disease.Tang B et al
156824602005Characterization of heat shock protein 27 phosphorylation sites in renal cell carcinoma.Tremolada L et al
182637062008HSP27 regulates p53 transcriptional activity in doxorubicin-treated fibroblasts and cardiac H9c2 cells: p21 upregulation and G2/M phase cell cycle arrest.Venkatakrishnan CD et al
124307132002Upregulation of HSP27 in a transgenic model of ALS.Vleminckx V et al
188002382009The level of Hsp27 in lymphocytes is negatively associated with a higher risk of lung cancer.Wang F et al
165999412006Specific association of small heat shock proteins with the pathological hallmarks of Alzheimer's disease brains.Wilhelmus MM et al
119787722002Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin.Wyttenbach A et al
127006312003Interferon-gamma downregulates Hsp27 expression and suppresses the negative regulation of cell death in oral squamous cell carcinoma lines.Yonekura N et al
180665882008Proteomic identification of heat shock protein 27 as a differentiation and prognostic marker in neuroblastoma but not in Ewing's sarcoma.Zanini C et al
16187901992Heat shock protein 27 and alpha B-crystallin can form a complex, which dissociates by heat shock.Zantema A et al
178816522007Disruption of neurofilament network with aggregation of light neurofilament protein: a common pathway leading to motor neuron degeneration due to Charcot-Marie-Tooth disease-linked mutations in NFL and HSPB1.Zhai J et al
175030812007Differential proteomic analysis of human colorectal carcinoma cell lines metastasis-associated proteins.Zhao L et al
150096452004HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells.Zourlidou A et al

Other Information

Locus ID:

NCBI: 3315
MIM: 602195
HGNC: 5246
Ensembl: ENSG00000106211

Variants:

dbSNP: 3315
ClinVar: 3315
TCGA: ENSG00000106211
COSMIC: HSPB1

RNA/Proteins

Gene IDTranscript IDUniprot
ENSG00000106211ENST00000248553P04792
ENSG00000106211ENST00000248553V9HW43
ENSG00000106211ENST00000429938C9J3N8
ENSG00000106211ENST00000447574F8WE04

Expression (GTEx)

0
500
1000
1500
2000
2500
3000
3500
4000
4500

Pathways

PathwaySourceExternal ID
MAPK signaling pathwayKEGGko04010
VEGF signaling pathwayKEGGko04370
MAPK signaling pathwayKEGGhsa04010
VEGF signaling pathwayKEGGhsa04370
AmoebiasisKEGGko05146
AmoebiasisKEGGhsa05146
Epstein-Barr virus infectionKEGGhsa05169
Epstein-Barr virus infectionKEGGko05169
Signal TransductionREACTOMER-HSA-162582
Signaling by VEGFREACTOMER-HSA-194138
VEGFA-VEGFR2 PathwayREACTOMER-HSA-4420097
MAPK family signaling cascadesREACTOMER-HSA-5683057
MAPK6/MAPK4 signalingREACTOMER-HSA-5687128
Gene ExpressionREACTOMER-HSA-74160
Regulation of mRNA stability by proteins that bind AU-rich elementsREACTOMER-HSA-450531
AUF1 (hnRNP D0) binds and destabilizes mRNAREACTOMER-HSA-450408

Protein levels (Protein atlas)

Not detected
Low
Medium
High

References

Pubmed IDYearTitleCitations
383101322024Mechanical activation and expression of HSP27 in epithelial ovarian cancer.0
384297422024HSPB1 as an RNA-binding protein mediates the pathological process of osteoarthritis.0
385074802024Reactive astrocytes secrete the chaperone HSPB1 to mediate neuroprotection.1
385533062024HSP27 promotes vasculogenic mimicry formation in human salivary adenoid cystic carcinoma via the AKT-MMP-2/9 pathway.0
383101322024Mechanical activation and expression of HSP27 in epithelial ovarian cancer.0
384297422024HSPB1 as an RNA-binding protein mediates the pathological process of osteoarthritis.0
385074802024Reactive astrocytes secrete the chaperone HSPB1 to mediate neuroprotection.1
385533062024HSP27 promotes vasculogenic mimicry formation in human salivary adenoid cystic carcinoma via the AKT-MMP-2/9 pathway.0
362509962023High frequency of heat shock protein 27 overexpression is a highly effective, high-coverage marker for minimal residual disease detection in children with B-cell acute lymphoblastic leukemia.0
365393202023Pathogenic variants in three families with distal muscle involvement.0
366721592023Heat Shock Protein 27 Is Involved in the Bioactive Glass Induced Osteogenic Response of Human Mesenchymal Stem Cells.2
367389812023Untangling the complexity of heat shock protein 27 in cancer and metastasis.2
372119492023FHOD1 is upregulated in glioma cells and attenuates ferroptosis of glioma cells by targeting HSPB1 signaling.3
372490952023Clinical features of a family with late-onset distal hereditary motor neuropathy harboring p.Pro39Leu variant of HSPB1.0
372689252023High HSPB1 expression predicts poor clinical outcomes and correlates with breast cancer metastasis.4

Citation

Ewa Laskowska ; Dorota Kuczyńska-Wiśnik ; Ewelina Matuszewska

HSPB1 (Heat-Shock 27 kDa Protein 1)

Atlas Genet Cytogenet Oncol Haematol. 2009-03-01

Online version: http://atlasgeneticsoncology.org/gene/40880/js/css/lib/bootstrap.min.css