Biology:HSPA1B

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Short description: Human gene


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example


Human gene HSPA1B is an intron-less gene which encodes for the heat shock protein HSP70-2, a member of the Hsp70 family of proteins.[1] The gene is located in the major histocompatibility complex, on the short arm of chromosome 6, in a cluster with two paralogous genes, HSPA1A and HSPA1L.[2][3][4] HSPA1A and HSPA1B produce nearly identical proteins because the few differences in their DNA sequences are almost exclusively synonymous substitutions or in the three prime untranslated region, heat shock 70kDa protein 1A, from HSPA1A, and heat shock 70kDa protein 1B, from HSPA1B.[2] A third, more modified paralog to these genes exists in the same region, HSPA1L, which shares a 90% homology with the other two.[4]

Function

Heat shock 70kDa protein 1B is a chaperone protein, cooperating with other heat shock proteins and chaperone systems to maintain proteostasis by stabilizing the structural conformation of other proteins in the cell and protecting against stress-induced aggregation.[5] Hsp70s have also been shown to bind and stabilize mRNA rich in adenine and uracil bases, independent of the occupational states of its other binding sites.[6] This protein is deactivated by binding ATP, and activated by its dephosphorylation to ADP, which requires a potassium ion to facilitate the hydrolysis, or ATP-ADP exchange.[7]

Hsp70-2 specifically is developmentally expressed in male germ line cells during meiosis, where it is necessary for the formation of the complex between CDC2 and cyclin B1.[8] It later becomes incorporated into the CatSper complex, a specialized calcium ion channel that enables spermatozoa motility.[9]

Clinical significance

Infertility has been observed in mice when HSA1B expression is disrupted, as CDC2 in unable to form the required heterodimer with cyclin B1 for the meiotic cell cycle to progress beyond S phase.[10]

Expression of heat shock protein 70kDa protein 2 in transformed tumor cells has been implicated in the rapid proliferation, metastasis, and inhibition of apoptosis in ovarian, bladder urothelial, and breast cancers.[11][12][13] Patients with chronic hepatitis B or hepatitis C virus infection who harbor a HSPA1B-1267 single nucleotide polymorphism have a higher risk for developing hepatocellular carcinoma.[14]

Interactions

Interactions have been characterized between Hsp70-2 and the following proteins:


See also

  • Heat shock proteins
  • Hsp70

References

  1. ↑ "Structure and expression of the three MHC-linked HSP70 genes". Immunogenetics 32 (4): 242–251. 1990. doi:10.1007/BF00187095. PMID 1700760. 
  2. ↑ 2.0 2.1 "Entrez Gene: HSPA1A heat shock 70kDa protein 1B". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3304. 
  3. ↑ "Genomic structure of the spermatid-specific hsp70 homolog gene located in the class III region of the major histocompatibility complex of mouse and man". Journal of Biochemistry 124 (2): 347–353. August 1998. doi:10.1093/oxfordjournals.jbchem.a022118. PMID 9685725. 
  4. ↑ 4.0 4.1 "Human major histocompatibility complex contains genes for the major heat shock protein HSP70". Proceedings of the National Academy of Sciences of the United States of America 86 (6): 1968–1972. March 1989. doi:10.1073/pnas.86.6.1968. PMID 2538825. Bibcode: 1989PNAS...86.1968S. 
  5. ↑ "The Hsp70 chaperone network". Nature Reviews. Molecular Cell Biology 20 (11): 665–680. November 2019. doi:10.1038/s41580-019-0133-3. PMID 31253954. 
  6. ↑ "Hsp70's RNA-binding and mRNA-stabilizing activities are independent of its protein chaperone functions" (in English). The Journal of Biological Chemistry 292 (34): 14122–14133. August 2017. doi:10.1074/jbc.M117.785394. PMID 28679534. 
  7. ↑ "Biochemical and structural studies on the high affinity of Hsp70 for ADP". Protein Science 20 (8): 1367–1379. August 2011. doi:10.1002/pro.663. PMID 21608060. 
  8. ↑ "Role of heat shock protein HSP70-2 in spermatogenesis". Reviews of Reproduction 4 (1): 23–30. January 1999. doi:10.1530/ror.0.0040023. PMID 10051099. 
  9. ↑ "CatSperbeta, a novel transmembrane protein in the CatSper channel complex" (in English). The Journal of Biological Chemistry 282 (26): 18945–18952. June 2007. doi:10.1074/jbc.M701083200. PMID 17478420. 
  10. ↑ "Role of heat shock protein HSP70-2 in spermatogenesis". Reviews of Reproduction 4 (1): 23–30. January 1999. doi:10.1530/ror.0.0040023. PMID 10051099. 
  11. ↑ "Heat shock protein 70-2 (HSP70-2) a novel cancer testis antigen that promotes growth of ovarian cancer". American Journal of Cancer Research 7 (6): 1252–1269. 2017. PMID 28670489. 
  12. ↑ "Heat-shock protein 70-2 (HSP70-2) expression in bladder urothelial carcinoma is associated with tumour progression and promotes migration and invasion". European Journal of Cancer 46 (1): 207–215. January 2010. doi:10.1016/j.ejca.2009.10.020. PMID 19914824. 
  13. ↑ "Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms". Genes & Development 19 (5): 570–582. March 2005. doi:10.1101/gad.305405. PMID 15741319. 
  14. ↑ "Heat shock protein A1B 1267 polymorphism is highly associated with risk and prognosis of hepatocellular carcinoma: a case-control study". Medicine 87 (2): 87–98. March 2008. doi:10.1097/MD.0b013e31816be95c. PMID 18344806. 
  15. ↑ "Nucleophosmin (NPM1/B23) interacts with activating transcription factor 5 (ATF5) protein and promotes proteasome- and caspase-dependent ATF5 degradation in hepatocellular carcinoma cells". The Journal of Biological Chemistry 287 (23): 19599–19609. June 2012. doi:10.1074/jbc.M112.363622. PMID 22528486. 
  16. ↑ "Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro". The Journal of Biological Chemistry 289 (3): 1402–1414. January 2014. doi:10.1074/jbc.M113.521997. PMID 24318877. 
  17. ↑ "Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro". The Journal of Biological Chemistry 289 (3): 1402–1414. January 2014. doi:10.1074/jbc.M113.521997. PMID 24318877. 
  18. ↑ "Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro". The Journal of Biological Chemistry 289 (3): 1402–1414. January 2014. doi:10.1074/jbc.M113.521997. PMID 24318877. 
  19. ↑ "CatSperbeta, a novel transmembrane protein in the CatSper channel complex" (in English). The Journal of Biological Chemistry 282 (26): 18945–18952. June 2007. doi:10.1074/jbc.M701083200. PMID 17478420. 
  20. ↑ "HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes". Development 124 (15): 3007–3014. August 1997. doi:10.1242/dev.124.15.3007. PMID 9247342. https://pubmed.ncbi.nlm.nih.gov/9247342/. 
  21. ↑ "ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function" (in English). The Journal of Biological Chemistry 286 (4): 2918–2932. January 2011. doi:10.1074/jbc.M110.171975. PMID 21081504. 
  22. ↑ "Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system". The EMBO Journal 22 (14): 3613–3623. July 2003. doi:10.1093/emboj/cdg362. PMID 12853476. 
  23. ↑ "Role of the cochaperone Tpr2 in Hsp90 chaperoning". Biochemistry 47 (31): 8203–8213. August 2008. doi:10.1021/bi800770g. PMID 18620420. 
  24. ↑ "A novel nuclear DnaJ protein, DNAJC8, can suppress the formation of spinocerebellar ataxia 3 polyglutamine aggregation in a J-domain independent manner". Biochemical and Biophysical Research Communications 474 (4): 626–633. June 2016. doi:10.1016/j.bbrc.2016.03.152. PMID 27133716. 
  25. ↑ "HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain". Biochemical and Biophysical Research Communications 353 (2): 280–285. February 2007. doi:10.1016/j.bbrc.2006.12.013. PMID 17182002. 
  26. ↑ "DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network". Molecular Cell 81 (12): 2533–2548.e9. June 2021. doi:10.1016/j.molcel.2021.03.041. PMID 33857403. 
  27. ↑ "The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3". Immunity 39 (2): 272–285. August 2013. doi:10.1016/j.immuni.2013.08.006. PMID 23973223. 
  28. ↑ "ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation". Nature Communications 7: 12882. October 2016. doi:10.1038/ncomms12882. PMID 27708256. Bibcode: 2016NatCo...712882S. 
  29. ↑ "ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation". Nature Communications 7: 12882. October 2016. doi:10.1038/ncomms12882. PMID 27708256. Bibcode: 2016NatCo...712882S. 
  30. ↑ "ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation". Nature Communications 7: 12882. October 2016. doi:10.1038/ncomms12882. PMID 27708256. Bibcode: 2016NatCo...712882S. 
  31. ↑ "ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation". Nature Communications 7: 12882. October 2016. doi:10.1038/ncomms12882. PMID 27708256. Bibcode: 2016NatCo...712882S. 
  32. ↑ "Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro". The Journal of Biological Chemistry 289 (3): 1402–1414. January 2014. doi:10.1074/jbc.M113.521997. PMID 24318877. 
  33. ↑ "The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family". DNA and Cell Biology 25 (12): 704–714. December 2006. doi:10.1089/dna.2006.25.704. PMID 17233114. 
  34. ↑ "Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation". The Journal of Biological Chemistry 288 (39): 27752–27763. September 2013. doi:10.1074/jbc.M113.483248. PMID 23921388. 
  35. ↑ "ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation". Nature Communications 7: 12882. October 2016. doi:10.1038/ncomms12882. PMID 27708256. Bibcode: 2016NatCo...712882S. 
  36. ↑ "HSP70 regulates the function of mitotic centrosomes". Cellular and Molecular Life Sciences 73 (20): 3949–3960. October 2016. doi:10.1007/s00018-016-2236-8. PMID 27137183. 
  37. ↑ "The molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn disease". The Journal of Biological Chemistry 289 (27): 18987–18998. July 2014. doi:10.1074/jbc.M114.557686. PMID 24790089. 
  38. ↑ "Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole". The Biochemical Journal 385 (Pt 1): 45–56. January 2005. doi:10.1042/BJ20040690. PMID 15383005. 
  39. ↑ "High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy". Nature 504 (7479): 291–295. December 2013. doi:10.1038/nature12748. PMID 24270810. Bibcode: 2013Natur.504..291H. 
  40. ↑ "Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1". Biochemical and Biophysical Research Communications 446 (1): 387–392. March 2014. doi:10.1016/j.bbrc.2014.02.124. PMID 24613385. 
  41. ↑ "ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation". Nature Communications 7: 12882. October 2016. doi:10.1038/ncomms12882. PMID 27708256. Bibcode: 2016NatCo...712882S. 
  42. ↑ "Stable association of hsp90 and p23, but Not hsp70, with active human telomerase". The Journal of Biological Chemistry 276 (19): 15571–15574. May 2001. doi:10.1074/jbc.C100055200. PMID 11274138. 
  43. ↑ "Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha". The Journal of Biological Chemistry 285 (10): 7827–7837. March 2010. doi:10.1074/jbc.M109.040618. PMID 20053985. 
  44. ↑ "Phosphorylation and binding partner analysis of the TSC1-TSC2 complex". Biochemical and Biophysical Research Communications 333 (3): 818–826. August 2005. doi:10.1016/j.bbrc.2005.05.175. PMID 15963462. 

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.





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