HSPA8
4125086
224267538
2008-07-08T02:06:13Z
ProteinBoxBot
3991663
Replaced protein Box Template with PBB Template for easy viewing.
{{PBB|geneid=3312}}
'''Heat shock 70kDa protein 8''', also known as '''HSPA8''', is a human [[gene]] encoding a [[heat shock protein]].<ref name="entrez">{{cite web | title = Entrez Gene: HSPA8 heat shock 70kDa protein 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3312| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: HSPA8 heat shock 70kDa protein 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3312| accessdate = }}</ref>
}}
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.<ref>{{cite journal |author=Goldfarb S, Kashlan O, Watkins J, Suaud L, Yan W, Kleyman T, Rubenstein R |title=Differential effects of Hsc70 and Hsp70 on the intracellular trafficking and functional expression of epithelial sodium channels |journal=Proc Natl Acad Sci U S A |volume=103 |issue=15 |pages=5817–22 |year=2006 |pmid=16585520 |doi=10.1073/pnas.0507903103}}</ref>
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kiang JG |title=Inducible heat shock protein 70 kD and inducible nitric oxide synthase in hemorrhage/resuscitation-induced injury. |journal=Cell Res. |volume=14 |issue= 6 |pages= 450–9 |year= 2005 |pmid= 15625011 |doi= 10.1038/sj.cr.7290247 }}
*{{cite journal | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960–9 |year= 1993 |pmid= 1286667 |doi= }}
*{{cite journal | author=Hattori H, Liu YC, Tohnai I, ''et al.'' |title=Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells. |journal=Cell Struct. Funct. |volume=17 |issue= 1 |pages= 77–86 |year= 1992 |pmid= 1586970 |doi= }}
*{{cite journal | author=DeLuca-Flaherty C, McKay DB, Parham P, Hill BL |title=Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis. |journal=Cell |volume=62 |issue= 5 |pages= 875–87 |year= 1990 |pmid= 1975516 |doi= }}
*{{cite journal | author=Lim MY, Davis N, Zhang JY, Bose HR |title=The v-rel oncogene product is complexed with cellular proteins including its proto-oncogene product and heat shock protein 70. |journal=Virology |volume=175 |issue= 1 |pages= 149–60 |year= 1990 |pmid= 2155506 |doi= }}
*{{cite journal | author=Welch WJ, Mizzen LA |title=Characterization of the thermotolerant cell. II. Effects on the intracellular distribution of heat-shock protein 70, intermediate filaments, and small nuclear ribonucleoprotein complexes. |journal=J. Cell Biol. |volume=106 |issue= 4 |pages= 1117–30 |year= 1988 |pmid= 2966179 |doi= }}
*{{cite journal | author=Dworniczak B, Mirault ME |title=Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein. |journal=Nucleic Acids Res. |volume=15 |issue= 13 |pages= 5181–97 |year= 1987 |pmid= 3037489 |doi= }}
*{{cite journal | author=Rensing SA, Maier UG |title=Phylogenetic analysis of the stress-70 protein family. |journal=J. Mol. Evol. |volume=39 |issue= 1 |pages= 80–6 |year= 1994 |pmid= 7545947 |doi= }}
*{{cite journal | author=Lain B, Iriarte A, Mattingly JR, ''et al.'' |title=Structural features of the precursor to mitochondrial aspartate aminotransferase responsible for binding to hsp70. |journal=J. Biol. Chem. |volume=270 |issue= 42 |pages= 24732–9 |year= 1995 |pmid= 7559589 |doi= }}
*{{cite journal | author=Benaroudj N, Batelier G, Triniolles F, Ladjimi MM |title=Self-association of the molecular chaperone HSC70. |journal=Biochemistry |volume=34 |issue= 46 |pages= 15282–90 |year= 1995 |pmid= 7578144 |doi= }}
*{{cite journal | author=Nunes SL, Calderwood SK |title=Heat shock factor-1 and the heat shock cognate 70 protein associate in high molecular weight complexes in the cytoplasm of NIH-3T3 cells. |journal=Biochem. Biophys. Res. Commun. |volume=213 |issue= 1 |pages= 1–6 |year= 1995 |pmid= 7639722 |doi= 10.1006/bbrc.1995.2090 }}
*{{cite journal | author=Inoue A, Torigoe T, Sogahata K, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=270 |issue= 38 |pages= 22571–6 |year= 1995 |pmid= 7673249 |doi= }}
*{{cite journal | author=Abe T, Konishi T, Hirano T, ''et al.'' |title=Possible correlation between DNA damage induced by hydrogen peroxide and translocation of heat shock 70 protein into the nucleus. |journal=Biochem. Biophys. Res. Commun. |volume=206 |issue= 2 |pages= 548–55 |year= 1995 |pmid= 7826371 |doi= 10.1006/bbrc.1995.1078 }}
*{{cite journal | author=Furlini G, Vignoli M, Re MC, ''et al.'' |title=Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein. |journal=J. Gen. Virol. |volume=75 ( Pt 1) |issue= |pages= 193–9 |year= 1994 |pmid= 7906708 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Tavaria M, Gabriele T, Anderson RL, ''et al.'' |title=Localization of the gene encoding the human heat shock cognate protein, HSP73, to chromosome 11. |journal=Genomics |volume=29 |issue= 1 |pages= 266–8 |year= 1996 |pmid= 8530083 |doi= 10.1006/geno.1995.1242 }}
*{{cite journal | author=Gao B, Eisenberg E, Greene L |title=Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate. |journal=J. Biol. Chem. |volume=271 |issue= 28 |pages= 16792–7 |year= 1996 |pmid= 8663341 |doi= }}
*{{cite journal | author=Egerton M, Moritz RL, Druker B, ''et al.'' |title=Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes. |journal=Biochem. Biophys. Res. Commun. |volume=224 |issue= 3 |pages= 666–74 |year= 1996 |pmid= 8713105 |doi= 10.1006/bbrc.1996.1082 }}
*{{cite journal | author=Lamian V, Small GM, Feldherr CM |title=Evidence for the existence of a novel mechanism for the nuclear import of Hsc70. |journal=Exp. Cell Res. |volume=228 |issue= 1 |pages= 84–91 |year= 1996 |pmid= 8892974 |doi= 10.1006/excr.1996.0302 }}
*{{cite journal | author=Hansen S, Midgley CA, Lane DP, ''et al.'' |title=Modification of two distinct COOH-terminal domains is required for murine p53 activation by bacterial Hsp70. |journal=J. Biol. Chem. |volume=271 |issue= 48 |pages= 30922–8 |year= 1997 |pmid= 8940078 |doi= }}
}}
{{refend}}
==External links==
* {{MeshName|Hsc70+Protein}}
{{gene-11-stub}}
{{Chaperones}}
[[Category: Heat shock proteins]]
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}