HSPA8
Heat shock 70 kDa protein 8 also known as heat shock cognate 71 kDa protein or Hsc70 or Hsp73 is a heat shock protein that in humans is encoded by the HSPA8 gene.[1]
Function
The heat shock protein 70 (Hsp70) family contains both heat-inducible and constitutively expressed members. The latter are called heat-shock cognate (Hsc) proteins. The heat shock 70 kDa protein 8 also known as Hsc70 belongs to the heat-shock cognate subgroup. This protein binds to nascent polypeptides to facilitate correct protein folding. It also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Two alternatively spliced variants have been characterized to date.[1]
HSPA8 is ATPase that works with auxilin to remove clathrin coated vesicles. In neurons, synaptojanin is also an important protein involved in vesicle uncoating.
Hsc70 vs Hsp70 comparison
Human Hsc70 has 85% identity with human Hsp70 (SDSC workbench, blosom26 default analysis). The scientific community has long assumed that Hsp70 and Hsc70 have similar cellular roles, but this assumption proved erroneous.[2]
Unlike canonical heat shock proteins, Hsc70 is constitutively expressed and performs functions related to normal cellular processes. Hsc70 was placed in the heat shock protein family due to homology with other heat shock proteins.
Interactions
HSPA8 has been shown to interact with STUB1,[3] BAG3,[4] BAG4,[5] Parkin (ligase),[6] BAG2,[4] HSPBP1,[7][8] CDC5L,[9] BAG1,[4][10] DNAJA3[11] and CITED1.[12]
References
- ^ a b "Entrez Gene: HSPA8 heat shock 70kDa protein 8". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3312.
- ^ Goldfarb S, Kashlan O, Watkins J, Suaud L, Yan W, Kleyman T, Rubenstein R (2006). "Differential effects of Hsc70 and Hsp70 on the intracellular trafficking and functional expression of epithelial sodium channels". Proc Natl Acad Sci USA 103 (15): 5817–22. doi:10.1073/pnas.0507903103. PMC 1458656. PMID 16585520. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1458656.
- ^ Ballinger, C A; Connell P, Wu Y, Hu Z, Thompson L J, Yin L Y, Patterson C (Jun. 1999). "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions". Mol. Cell. Biol. (UNITED STATES) 19 (6): 4535–45. ISSN 0270-7306. PMC 104411. PMID 10330192. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=104411.
- ^ a b c Takayama, S; Xie Z, Reed J C (Jan. 1999). "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators". J. Biol. Chem. (UNITED STATES) 274 (2): 781–6. doi:10.1074/jbc.274.2.781. ISSN 0021-9258. PMID 9873016.
- ^ Miki, Kiyoshi; Eddy Edward M (Apr. 2002). "Tumor necrosis factor receptor 1 is an ATPase regulated by silencer of death domain". Mol. Cell. Biol. (United States) 22 (8): 2536–43. doi:10.1128/MCB.22.8.2536-2543.2002. ISSN 0270-7306. PMC 133739. PMID 11909948. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=133739.
- ^ Imai, Yuzuru; Soda Mariko, Hatakeyama Shigetsugu, Akagi Takumi, Hashikawa Tsutomu, Nakayama Kei Ichi, Takahashi Ryosuke (Jul. 2002). "CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity". Mol. Cell (United States) 10 (1): 55–67. doi:10.1016/S1097-2765(02)00583-X. ISSN 1097-2765. PMID 12150907.
- ^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- ^ Stelzl, Ulrich; Worm Uwe, Lalowski Maciej, Haenig Christian, Brembeck Felix H, Goehler Heike, Stroedicke Martin, Zenkner Martina, Schoenherr Anke, Koeppen Susanne, Timm Jan, Mintzlaff Sascha, Abraham Claudia, Bock Nicole, Kietzmann Silvia, Goedde Astrid, Toksöz Engin, Droege Anja, Krobitsch Sylvia, Korn Bernhard, Birchmeier Walter, Lehrach Hans, Wanker Erich E (Sep. 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell (United States) 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. ISSN 0092-8674. PMID 16169070.
- ^ Ajuh, P; Kuster B, Panov K, Zomerdijk J C, Mann M, Lamond A I (Dec. 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". EMBO J. (ENGLAND) 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. ISSN 0261-4189. PMC 305846. PMID 11101529. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=305846.
- ^ Takayama, S; Bimston D N, Matsuzawa S, Freeman B C, Aime-Sempe C, Xie Z, Morimoto R I, Reed J C (Aug. 1997). "BAG-1 modulates the chaperone activity of Hsp70/Hsc70". EMBO J. (ENGLAND) 16 (16): 4887–96. doi:10.1093/emboj/16.16.4887. ISSN 0261-4189. PMC 1170124. PMID 9305631. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170124.
- ^ Sarkar, S; Pollack B P, Lin K T, Kotenko S V, Cook J R, Lewis A, Pestka S (Dec. 2001). "hTid-1, a human DnaJ protein, modulates the interferon signaling pathway". J. Biol. Chem. (United States) 276 (52): 49034–42. doi:10.1074/jbc.M103683200. ISSN 0021-9258. PMID 11679576.
- ^ Yahata, T; de Caestecker M P, Lechleider R J, Andriole S, Roberts A B, Isselbacher K J, Shioda T (Mar. 2000). "The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors". J. Biol. Chem. (UNITED STATES) 275 (12): 8825–34. doi:10.1074/jbc.275.12.8825. ISSN 0021-9258. PMID 10722728.
Further reading
- Kiang JG (2005). "Inducible heat shock protein 70 kD and inducible nitric oxide synthase in hemorrhage/resuscitation-induced injury". Cell Res. 14 (6): 450–9. doi:10.1038/sj.cr.7290247. PMID 15625011.
- Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667.
- Hattori H, Liu YC, Tohnai I, et al. (1992). "Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells". Cell Struct. Funct. 17 (1): 77–86. doi:10.1247/csf.17.77. PMID 1586970.
- DeLuca-Flaherty C, McKay DB, Parham P, Hill BL (1990). "Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis". Cell 62 (5): 875–87. doi:10.1016/0092-8674(90)90263-E. PMID 1975516.
- Lim MY, Davis N, Zhang JY, Bose HR (1990). "The v-rel oncogene product is complexed with cellular proteins including its proto-oncogene product and heat shock protein 70". Virology 175 (1): 149–60. doi:10.1016/0042-6822(90)90195-W. PMID 2155506.
- Welch WJ, Mizzen LA (1988). "Characterization of the thermotolerant cell. II. Effects on the intracellular distribution of heat-shock protein 70, intermediate filaments, and small nuclear ribonucleoprotein complexes". J. Cell Biol. 106 (4): 1117–30. doi:10.1083/jcb.106.4.1117. PMC 2115010. PMID 2966179. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2115010.
- Dworniczak B, Mirault ME (1987). "Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein". Nucleic Acids Res. 15 (13): 5181–97. doi:10.1093/nar/15.13.5181. PMC 305955. PMID 3037489. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=305955.
- Rensing SA, Maier UG (1994). "Phylogenetic analysis of the stress-70 protein family". J. Mol. Evol. 39 (1): 80–6. doi:10.1007/BF00178252. PMID 7545947.
- Lain B, Iriarte A, Mattingly JR, et al. (1995). "Structural features of the precursor to mitochondrial aspartate aminotransferase responsible for binding to hsp70". J. Biol. Chem. 270 (42): 24732–9. doi:10.1074/jbc.270.42.24732. PMID 7559589.
- Benaroudj N, Batelier G, Triniolles F, Ladjimi MM (1995). "Self-association of the molecular chaperone HSC70". Biochemistry 34 (46): 15282–90. doi:10.1021/bi00046a037. PMID 7578144.
- Nunes SL, Calderwood SK (1995). "Heat shock factor-1 and the heat shock cognate 70 protein associate in high molecular weight complexes in the cytoplasm of NIH-3T3 cells". Biochem. Biophys. Res. Commun. 213 (1): 1–6. doi:10.1006/bbrc.1995.2090. PMID 7639722.
- Inoue A, Torigoe T, Sogahata K, et al. (1995). "70-kDa heat shock cognate protein interacts directly with the N-terminal region of the retinoblastoma gene product pRb. Identification of a novel region of pRb-mediating protein interaction". J. Biol. Chem. 270 (38): 22571–6. doi:10.1074/jbc.270.38.22571. PMID 7673249.
- Abe T, Konishi T, Hirano T, et al. (1995). "Possible correlation between DNA damage induced by hydrogen peroxide and translocation of heat shock 70 protein into the nucleus". Biochem. Biophys. Res. Commun. 206 (2): 548–55. doi:10.1006/bbrc.1995.1078. PMID 7826371.
- Furlini G, Vignoli M, Re MC, et al. (1994). "Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein". J. Gen. Virol. 75 (1): 193–9. doi:10.1099/0022-1317-75-1-193. PMID 7906708.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Tavaria M, Gabriele T, Anderson RL, et al. (1996). "Localization of the gene encoding the human heat shock cognate protein, HSP73, to chromosome 11". Genomics 29 (1): 266–8. doi:10.1006/geno.1995.1242. PMID 8530083.
- Gao B, Eisenberg E, Greene L (1996). "Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate". J. Biol. Chem. 271 (28): 16792–7. doi:10.1074/jbc.271.28.16792. PMID 8663341.
- Egerton M, Moritz RL, Druker B, et al. (1996). "Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes". Biochem. Biophys. Res. Commun. 224 (3): 666–74. doi:10.1006/bbrc.1996.1082. PMID 8713105.
- Lamian V, Small GM, Feldherr CM (1996). "Evidence for the existence of a novel mechanism for the nuclear import of Hsc70". Exp. Cell Res. 228 (1): 84–91. doi:10.1006/excr.1996.0302. PMID 8892974.
- Hansen S, Midgley CA, Lane DP, et al. (1997). "Modification of two distinct COOH-terminal domains is required for murine p53 activation by bacterial Hsp70". J. Biol. Chem. 271 (48): 30922–8. doi:10.1074/jbc.271.48.30922. PMID 8940078.
External links
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PDB gallery
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1atr: THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS
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1ats: THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS
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1ba0: HEAT-SHOCK COGNATE 70KD PROTEIN 44KD ATPASE N-TERMINAL 1NGE 3
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1ba1: HEAT-SHOCK COGNATE 70KD PROTEIN 44KD ATPASE N-TERMINAL MUTANT WITH CYS 17 REPLACED BY LYS
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1bup: T13S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN
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1ckr: HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES
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1hpm: HOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS SPECIFICALLY IN THE ATPASE ACTIVE SITE
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1hx1: CRYSTAL STRUCTURE OF A BAG DOMAIN IN COMPLEX WITH THE HSC70 ATPASE DOMAIN
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1kax: 70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71M MUTANT
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1kay: 70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71A MUTANT
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1kaz: 70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71E MUTANT
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1nga: STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
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1ngb: STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
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1ngc: STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
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1ngd: STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
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1nge: STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
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1ngf: STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
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1ngg: STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
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1ngh: STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
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1ngi: STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
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1ngj: STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
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1qqm: D199S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN
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1qqn: D206S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN
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1qqo: E175S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN
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1ud0: CRYSTAL STRUCTURE OF THE C-TERMINAL 10-kDA SUBDOMAIN OF HSC70
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1yuw: crystal structure of bovine hsc70(aa1-554)E213A/D214A mutant
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2bup: T13G MUTANT OF THE ATPASE FRAGMENT OF BOVINE HSC70
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3hsc: THREE-DIMENSIONAL STRUCTURE OF THE ATPASE FRAGMENT OF A 70K HEAT-SHOCK COGNATE PROTEIN
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7hsc: HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES
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Chaperones/
protein folding |
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Hsp10/GroES (Early pregnancy factor) · Hsp27 · Hsp47 · HSP60/GroEL
Hsp40/DnaJ (A1, A2, A3, B1, B2, B11, B4, B6, B9, C1, C3, C5, C6, C7, C10, C11, C13, C14, C19)
Hsp70 (1A, 1B, 1L, 2, 4, 4L, 5, 6, 7, 8, 9, 12A, 14)
Hsp90 ( α1, α2, β, ER, TRAP1)
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Other
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| Protein targeting |
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| Ubiquitin |
E1 Ubiquitin-activating enzyme (UBA1, UBA2, UBA3, UBA5, UBA6, UBA7, ATG7, NAE1, SAE1)
E2 Ubiquitin-conjugating enzyme (A • B • C • D1, D2, D3 • E1, E2, E3 • G1, G2 • H • I • J1, J2 • K • L1, L2, L3, L4, L6 • M • N • O • Q1, Q2 • R1 (CDC34), R2 • S • V1, V2 • Z)
E3 Ubiquitin ligase (VHL, Cullin, CBL, MDM2, FANCL, UBR1)
Deubiquitinating enzyme: Ataxin 3 • USP6 • CYLD
ATG3 • BIRC6 • UFC1
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| Other |
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see also posttranslational modification disorders
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)
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