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PMID: 17411420 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

The peptide-binding activity of GRP94 is regulated by calcium.

The Biochemical journal ·Vol. 405 ·No. 2 ·2007-07-15 ·Pages 233-41

Biswas C, Ostrovsky O, Makarewich CA, Wanderling S, Gidalevitz T, Argon Y

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Calcium/physiology Calcium-Binding Proteins/metabolism Cell Line Membrane Glycoproteins/metabolism Mice Peptides/metabolism Spodoptera
Chemicals
Calcium-Binding Proteins Membrane Glycoproteins Peptides endoplasmin Calcium
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Biswas Chhanda
Division of Cell Pathology, Department of Pathology and Laboratory Medicine, Children's Hospital of Philadelphia and University of Pennsylvania, Philadelphia, PA 19104, USA.
Ostrovsky Olga
Makarewich Catherine A
Wanderling Sherry
Gidalevitz Tali
Argon Yair
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
1470-8728
DOI
10.1042/BJ20061867
Published
2007-07-15
Pages
233-41
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1904529
Subset
IM
Grants
NIAID NIH HHS · R01 AI030178 · United States
NHLBI NIH HHS · T32 HL007237 · United States
NIAID NIH HHS · AI-30178 · United States
NHLBI NIH HHS · HL-07237 · United States
External Links
PubMed source DOI: 10.1042/BJ20061867 PMC Full Text View journal details
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