Unknown

Dataset Information

0

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


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.

SUBMITTER: Biswas C 

PROVIDER: S-EPMC1904529 | biostudies-other | 2007 Jul

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1221965 | biostudies-other
| S-EPMC3717329 | biostudies-literature
| S-EPMC4906247 | biostudies-literature
| S-EPMC2679901 | biostudies-literature
| S-EPMC2710619 | biostudies-literature
| S-EPMC15323 | biostudies-literature
| S-EPMC5897183 | biostudies-literature
| S-EPMC6167357 | biostudies-literature
| S-EPMC6324581 | biostudies-literature
| S-EPMC3904872 | biostudies-literature