78 kD glucose-regulated protein; GRP 78; heat shock 70 kD protein 5; immunoglobulin heavy chain-binding protein; BiP; endoplasmic reticulum lumenal Ca(2+)-binding protein grp78 (HSPA5, GRP78)
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Function
- molecular chaperone that associates with newly synthesized proteins usually in the form of aggregates
- stress increases association of proteins with GRP78
- any unfolded protein that can bind GRP78 can induce the unfolded protein response pathway
- probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER
- interacts with DNAJC1 (via J domain) (putative)
- component of an EIF2 complex at least composed of CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 & HSPA5
- part a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGT1A1 & very small amounts of ERP29, but not, or at very low levels, CALR nor CANX
- interacts with TMEM132A
Structure
belongs to the heat shock protein 70 family
Compartment
Expression
- glucose regulated protein, induced by glucose starvation
Pathology
- seizure-related protein
- autoantigen in rheumatoid arthritis
- role in transmission of Covid-19
Comparative biology
- up-regulated after environmental enrichment in mice[3]
More general terms
References
- ↑ Ou WJ et al Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364:771 1993 PMID: https://www.ncbi.nlm.nih.gov/pubmed/8102790
- ↑ Arlan Richardson, AGE meeting Oct 3-6, 1990 New York, NY
- ↑ 3.0 3.1 Rampon C, Jiang CH, Dong H, Tang YP, Lockhart DJ, Schultz PG, Tsien JZ, Hu Y. Effects of environmental enrichment on gene expression in the brain. Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12880-4. PMID: https://www.ncbi.nlm.nih.gov/pubmed/11070096
- ↑ Abrams Z New drug shows promise for fighting both COVID-19 and cancer. Keck School of Medicine USC. Keck School News. Nov 14, 2022 https://keck.usc.edu/new-drug-shows-promise-for-fighting-both-covid-19-and-cancer/
Shin WJ, Ha DP, Machida K, Lee AS The stress-inducible ER chaperone GRP78/BiP is upregulated during SARS-CoV-2 infection and acts as a pro-viral protein. Nature Communications. 2022. 13:6551. Nov 14 PMID: https://www.ncbi.nlm.nih.gov/pubmed/36376289 PMCID: PMC9663498 Free PMC article. https://www.nature.com/articles/s41467-022-34065-3