Heat shock protein 90kDa alpha (cytosolic), member A1

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Heat shock protein 90kDa alpha (cytosolic), class A member 1
Protein HSP90AA1 PDB 1byq.png
PDB rendering based on 1byq.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols HSP90AA1 ; EL52; HSP86; HSP89A; HSP90A; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; Hsp89; Hsp90; LAP-2; LAP2
External IDs OMIM140571 MGI96250 HomoloGene68464 ChEMBL: 3880 GeneCards: HSP90AA1 Gene
RNA expression pattern
PBB GE HSP90AA1 211969 at tn.png
PBB GE HSP90AA1 210211 s at tn.png
PBB GE HSP90AA1 211968 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3320 15519
Ensembl ENSG00000080824 ENSMUSG00000021270
UniProt P07900 P07901
RefSeq (mRNA) NM_001017963 NM_010480
RefSeq (protein) NP_001017963 NP_034610
Location (UCSC) Chr 14:
102.55 – 102.61 Mb
Chr 12:
110.69 – 110.7 Mb
PubMed search [1] [2]

Heat shock protein HSP 90-alpha is a protein that in humans is encoded by the HSP90AA1 gene.[1][2]


Interactions[edit]

Heat shock protein 90kDa alpha (cytosolic), member A1 has been shown to interact with:

References[edit]

  1. ^ Hickey E, Brandon SE, Smale G, Lloyd D, Weber LA (September 1989). "Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein". Mol Cell Biol 9 (6): 2615–26. PMC 362334. PMID 2527334. 
  2. ^ Chen B, Piel WH, Gui L, Bruford E, Monteiro A (December 2005). "The HSP90 family of genes in the human genome: insights into their divergence and evolution". Genomics 86 (6): 627–37. doi:10.1016/j.ygeno.2005.08.012. PMID 16269234. 
  3. ^ Panaretou B, Siligardi G, Meyer P, Maloney A, Sullivan JK, Singh S, Millson SH, Clarke PA, Naaby-Hansen S, Stein R, Cramer R, Mollapour M, Workman P, Piper PW, Pearl LH, Prodromou C (2002). "Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1". Mol. Cell 10 (6): 1307–18. doi:10.1016/S1097-2765(02)00785-2. PMID 12504007. 
  4. ^ a b Haendeler J, Hoffmann J, Rahman S, Zeiher AM, Dimmeler S (2003). "Regulation of telomerase activity and anti-apoptotic function by protein-protein interaction and phosphorylation". FEBS Lett. 536 (1-3): 180–6. doi:10.1016/S0014-5793(03)00058-9. PMID 12586360. 
  5. ^ a b Kawauchi K, Ihjima K, Yamada O (2005). "IL-2 increases human telomerase reverse transcriptase activity transcriptionally and posttranslationally through phosphatidylinositol 3'-kinase/Akt, heat shock protein 90, and mammalian target of rapamycin in transformed NK cells". J. Immunol. 174 (9): 5261–9. doi:10.4049/jimmunol.174.9.5261. PMID 15843522. 
  6. ^ Sato S, Fujita N, Tsuruo T (2000). "Modulation of Akt kinase activity by binding to Hsp90". Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10832–7. doi:10.1073/pnas.170276797. PMC 27109. PMID 10995457. 
  7. ^ Veldscholte J, Berrevoets CA, Brinkmann AO, Grootegoed JA, Mulder E (1992). "Anti-androgens and the mutated androgen receptor of LNCaP cells: differential effects on binding affinity, heat-shock protein interaction, and transcription activation". Biochemistry 31 (8): 2393–9. doi:10.1021/bi00123a026. PMID 1540595. 
  8. ^ Nemoto T, Ohara-Nemoto Y, Ota M (1992). "Association of the 90-kDa heat shock protein does not affect the ligand-binding ability of androgen receptor". J. Steroid Biochem. Mol. Biol. 42 (8): 803–12. doi:10.1016/0960-0760(92)90088-Z. PMID 1525041. 
  9. ^ Stancato LF, Chow YH, Hutchison KA, Perdew GH, Jove R, Pratt WB (1993). "Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system". J. Biol. Chem. 268 (29): 21711–6. PMID 8408024. 
  10. ^ Dogan T, Harms GS, Hekman M, Karreman C, Oberoi TK, Alnemri ES, Rapp UR, Rajalingam K (2008). "X-linked and cellular IAPs modulate the stability of C-RAF kinase and cell motility". Nat. Cell Biol. 10 (12): 1447–55. doi:10.1038/ncb1804. PMID 19011619. 
  11. ^ Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH (2004). "The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)". Cell 116 (1): 87–98. doi:10.1016/S0092-8674(03)01027-4. PMID 14718169. 
  12. ^ Silverstein AM, Grammatikakis N, Cochran BH, Chinkers M, Pratt WB (1998). "p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site". J. Biol. Chem. 273 (32): 20090–5. doi:10.1074/jbc.273.32.20090. PMID 9685350. 
  13. ^ a b Hulkko SM, Wakui H, Zilliacus J (2000). "The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function". Biochem. J. 349 (3): 885–93. PMC 1221218. PMID 10903152. 
  14. ^ Kang J, Kim T, Ko YG, Rho SB, Park SG, Kim MJ, Kwon HJ, Kim S (2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases". J. Biol. Chem. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. PMID 10913161. 
  15. ^ Marcu MG, Doyle M, Bertolotti A, Ron D, Hendershot L, Neckers L (2002). "Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha". Mol. Cell. Biol. 22 (24): 8506–13. doi:10.1128/MCB.22.24.8506-8513.2002. PMC 139892. PMID 12446770. 
  16. ^ a b Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF (1996). "A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor". Cell Stress Chaperones 1 (4): 237–50. doi:10.1379/1466-1268(1996)001<0237:APOMCI>2.3.CO;2. PMC 376461. PMID 9222609. 
  17. ^ Lee MO, Kim EO, Kwon HJ, Kim YM, Kang HJ, Kang H, Lee JE (2002). "Radicicol represses the transcriptional function of the estrogen receptor by suppressing the stabilization of the receptor by heat shock protein 90". Mol. Cell. Endocrinol. 188 (1-2): 47–54. doi:10.1016/S0303-7207(01)00753-5. PMID 11911945. 
  18. ^ Nair SC, Rimerman RA, Toran EJ, Chen S, Prapapanich V, Butts RN, Smith DF (1997). "Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor". Mol. Cell. Biol. 17 (2): 594–603. PMC 231784. PMID 9001212. 
  19. ^ Vaiskunaite R, Kozasa T, Voyno-Yasenetskaya TA (2001). "Interaction between the G alpha subunit of heterotrimeric G(12) protein and Hsp90 is required for G alpha(12) signaling". J. Biol. Chem. 276 (49): 46088–93. doi:10.1074/jbc.M108711200. PMID 11598136. 
  20. ^ a b Venema RC, Venema VJ, Ju H, Harris MB, Snead C, Jilling T, Dimitropoulou C, Maragoudakis ME, Catravas JD (2003). "Novel complexes of guanylate cyclase with heat shock protein 90 and nitric oxide synthase". Am. J. Physiol. Heart Circ. Physiol. 285 (2): H669–78. doi:10.1152/ajpheart.01025.2002. PMID 12676772. 
  21. ^ Xu W, Mimnaugh E, Rosser MF, Nicchitta C, Marcu M, Yarden Y, Neckers L (2001). "Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90". J. Biol. Chem. 276 (5): 3702–8. doi:10.1074/jbc.M006864200. PMID 11071886. 
  22. ^ Jeong JH, An JY, Kwon YT, Li LY, Lee YJ (2008). "Quercetin-induced ubiquitination and down-regulation of Her-2/neu". J. Cell. Biochem. 105 (2): 585–95. doi:10.1002/jcb.21859. PMC 2575035. PMID 18655187. 
  23. ^ Hu Y, Mivechi NF (2003). "HSF-1 interacts with Ral-binding protein 1 in a stress-responsive, multiprotein complex with HSP90 in vivo". J. Biol. Chem. 278 (19): 17299–306. doi:10.1074/jbc.M300788200. PMID 12621024. 
  24. ^ Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I (2000). "Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine". Cell 101 (2): 199–210. doi:10.1016/S0092-8674(00)80830-2. PMID 10786835. 
  25. ^ Johnson BD, Schumacher RJ, Ross ED, Toft DO (1998). "Hop modulates Hsp70/Hsp90 interactions in protein folding". J. Biol. Chem. 273 (6): 3679–86. doi:10.1074/jbc.273.6.3679. PMID 9452498. 
  26. ^ Harris MB, Ju H, Venema VJ, Blackstone M, Venema RC (2000). "Role of heat shock protein 90 in bradykinin-stimulated endothelial nitric oxide release". Gen. Pharmacol. 35 (3): 165–70. doi:10.1016/S0306-3623(01)00104-5. PMID 11744239. 
  27. ^ Stepp DW, Ou J, Ackerman AW, Welak S, Klick D, Pritchard KA (2002). "Native LDL and minimally oxidized LDL differentially regulate superoxide anion in vascular endothelium in situ". Am. J. Physiol. Heart Circ. Physiol. 283 (2): H750–9. doi:10.1152/ajpheart.00029.2002. PMID 12124224. 
  28. ^ Jibard N, Meng X, Leclerc P, Rajkowski K, Fortin D, Schweizer-Groyer G, Catelli MG, Baulieu EE, Cadepond F (1999). "Delimitation of two regions in the 90-kDa heat shock protein (Hsp90) able to interact with the glucocorticosteroid receptor (GR)". Exp. Cell Res. 247 (2): 461–74. doi:10.1006/excr.1998.4375. PMID 10066374. 
  29. ^ Kanelakis KC, Shewach DS, Pratt WB (2002). "Nucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assembly". J. Biol. Chem. 277 (37): 33698–703. doi:10.1074/jbc.M204164200. PMID 12093808. 
  30. ^ Hecht K, Carlstedt-Duke J, Stierna P, Gustafsson J, Brönnegârd M, Wikström AC (1997). "Evidence that the beta-isoform of the human glucocorticoid receptor does not act as a physiologically significant repressor". J. Biol. Chem. 272 (42): 26659–64. doi:10.1074/jbc.272.42.26659. PMID 9334248. 
  31. ^ de Castro M, Elliot S, Kino T, Bamberger C, Karl M, Webster E, Chrousos GP (1996). "The non-ligand binding beta-isoform of the human glucocorticoid receptor (hGR beta): tissue levels, mechanism of action, and potential physiologic role". Mol. Med. 2 (5): 597–607. PMC 2230188. PMID 8898375. 
  32. ^ van den Berg JD, Smets LA, van Rooij H (1996). "Agonist-free transformation of the glucocorticoid receptor in human B-lymphoma cells". J. Steroid Biochem. Mol. Biol. 57 (3-4): 239–49. doi:10.1016/0960-0760(95)00271-5. PMID 8645634. 
  33. ^ Stancato LF, Silverstein AM, Gitler C, Groner B, Pratt WB (1996). "Use of the thiol-specific derivatizing agent N-iodoacetyl-3-[125I]iodotyrosine to demonstrate conformational differences between the unbound and hsp90-bound glucocorticoid receptor hormone binding domain". J. Biol. Chem. 271 (15): 8831–6. doi:10.1074/jbc.271.15.8831. PMID 8621522. 
  34. ^ Wang C, Chen J (2003). "Phosphorylation and hsp90 binding mediate heat shock stabilization of p53". J. Biol. Chem. 278 (3): 2066–71. doi:10.1074/jbc.M206697200. PMID 12427754. 
  35. ^ Akakura S, Yoshida M, Yoneda Y, Horinouchi S (2001). "A role for Hsc70 in regulating nucleocytoplasmic transport of a temperature-sensitive p53 (p53Val-135)". J. Biol. Chem. 276 (18): 14649–57. doi:10.1074/jbc.M100200200. PMID 11297531. 
  36. ^ Peng Y, Chen L, Li C, Lu W, Chen J (2001). "Inhibition of MDM2 by hsp90 contributes to mutant p53 stabilization". J. Biol. Chem. 276 (44): 40583–90. doi:10.1074/jbc.M102817200. PMID 11507088. 
  37. ^ Mizuno K, Shirogane T, Shinohara A, Iwamatsu A, Hibi M, Hirano T (2001). "Regulation of Pim-1 by Hsp90". Biochem. Biophys. Res. Commun. 281 (3): 663–9. doi:10.1006/bbrc.2001.4405. PMID 11237709. 
  38. ^ Sumanasekera WK, Tien ES, Turpey R, Vanden Heuvel JP, Perdew GH (2003). "Evidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2". J. Biol. Chem. 278 (7): 4467–73. doi:10.1074/jbc.M211261200. PMID 12482853. 
  39. ^ Hamamoto R, Furukawa Y, Morita M, Iimura Y, Silva FP, Li M, Yagyu R, Nakamura Y (2004). "SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells". Nat. Cell Biol. 6 (8): 731–40. doi:10.1038/ncb1151. PMID 15235609. 
  40. ^ Boudeau J, Deak M, Lawlor MA, Morrice NA, Alessi DR (2003). "Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability". Biochem. J. 370 (Pt 3): 849–57. doi:10.1042/BJ20021813. PMC 1223241. PMID 12489981. 
  41. ^ a b Wrighton KH, Lin X, Feng XH (2008). "Critical regulation of TGFbeta signaling by Hsp90". Proc. Natl. Acad. Sci. U.S.A. 105 (27): 9244–9. doi:10.1073/pnas.0800163105. PMC 2453700. PMID 18591668. 

Further reading[edit]