BiP (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum.
BiP is a constitutively-expressed resident protein of the endoplasmic reticulum (ER) of all eucaryotic cells, and belongs to the highly conserved hsp70 protein family. In the ER, BiP is involved in polypeptide translocation, protein folding and presumably protein degradation as well. These functions are essential to cell viability, as has been shown for yeast. In this review, I will summarize the structural features of hsp70 proteins and focus on those experiments which revealed the biological function of BiP.
Haas
I G
IG
Institut für Biochemie, Universität Heidelberg, Germany.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins / Q000502:physiology*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D000091342:Endoplasmic Reticulum Chaperone BiP; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry*; D006360:Heat-Shock Proteins; D006801:Humans; D007143:Immunoglobulin Heavy Chains / Q000502:physiology*; D018832:Molecular Chaperones / Q000502:physiology*; D010766:Phosphorylation; D017510:Protein Folding
D002352:Carrier Proteins; D000091342:Endoplasmic Reticulum Chaperone BiP; D018840:HSP70 Heat-Shock Proteins; C000717247:HSPA5 protein, human; D006360:Heat-Shock Proteins; D007143:Immunoglobulin Heavy Chains; D018832:Molecular Chaperones; D000255:Adenosine Triphosphate