Journal
BIOCHEMICAL JOURNAL
Volume 405, Issue -, Pages 233-241Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20061867
Keywords
calcium store; chaperone; endoplasmic reticulum (ER); glucose-regulated protein of 94 kDa (GRP94); heat-shock protein (HSP)
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Funding
- NHLBI NIH HHS [HL-07237, T32 HL007237] Funding Source: Medline
- NIAID NIH HHS [R01 AI030178, AI-30178] Funding Source: Medline
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GRP94 (glucose-regulated protein of 94 kDa) is a major luminal constituent of the endoplasmic reticulum with known high capacity for calcium in vivo and a peptide-binding activity in vitro. In the present study, we show that Ca2+ regulates the ability of GRP94 to bind peptides. This effect is due to a Ca2+-binding site located in the charged linker domain of GRP94, which, when occupied. enhances the association of peptides with the peptide-binding site in the N-terminal domain of the protein. We further show that grp94(-/-) cells are hypersensitive to perturbation of intracellular calcium and thus GRP94 is important for cellular Ca2+ storage.
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