HSPA8

From Wikipedia, the free encyclopedia

Heat shock 70kDa protein 8

PDB rendering based on 1atr.

Available structures: 1atr, 1ats, 1ba0, 1ba1, 1bup, 1ckr, 1hpm, 1hx1, 1kax, 1kay, 1kaz, 1nga, 1ngb, 1ngc, 1ngd, 1nge, 1ngf, 1ngg, 1ngh, 1ngi, 1ngj, 1qqm, 1qqn, 1qqo, 1ud0, 1yuw, 2bup, 3hsc, 7hsc

Identifiers

Symbol(s)

HSPA8; LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; HSPA10; MGC131511; MGC29929; NIP71

External IDs

OMIM: 600816 MGI: 105384 HomoloGene: 68524

Gene ontology
Molecular Function:	• nucleotide binding • protein binding • ATP binding • ATPase activity, coupled
Cellular Component:	• intracellular • nucleus • cell surface
Biological Process:	• protein folding • response to unfolded protein

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_006597 (mRNA)
NP_006588 (protein)

NM_031165 (mRNA)
NP_112442 (protein)

Location

Chr 11: 122.43 - 122.44 Mb

n/a

Pubmed search

[1]

[2]

Heat shock 70kDa protein 8, also known as HSPA8, is a human gene encoding a heat shock protein.^[1]

The product encoded by this gene belongs to the heat shock protein 70 family which contains both heat-inducible and constitutively expressed members. The latter are called heat-shock cognate proteins. This gene encodes a heat-shock cognate protein. This protein binds to nascent polypeptides to facilitate correct 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 is also called Hsp73. The human gene name is HSPA8. It is in the DnaK heat shock protein family.

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.

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]

[edit] References

^ ^a ^b Entrez Gene: HSPA8 heat shock 70kDa protein 8.
^ 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 U S A 103 (15): 5817–22. doi:10.1073/pnas.0507903103. PMID 16585520.

[edit] 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. 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. 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. 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. 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. PMID 2966179.
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. PMID 3037489.
Rensing SA, Maier UG (1994). "Phylogenetic analysis of the stress-70 protein family.". J. Mol. Evol. 39 (1): 80–6. 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. PMID 7559589.
Benaroudj N, Batelier G, Triniolles F, Ladjimi MM (1995). "Self-association of the molecular chaperone HSC70.". Biochemistry 34 (46): 15282–90. 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. 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 ( Pt 1): 193–9. 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. 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. 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. PMID 8940078.