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Journal article
The peptide-binding activity of GRP94 is regulated by calcium
Biochemical journal, v 405(Pt 2), pp 233-241
27 Jun 2007
PMID: 17411420
Featured in Collection : UN Sustainable Development Goals @ Drexel
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 Ca
2+
regulates the ability of GRP94 to bind peptides. This effect is due to a Ca
2+
-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 Ca
2+
storage.
Metrics
Details
- Title
- The peptide-binding activity of GRP94 is regulated by calcium
- Creators
- Chhanda Biswas - Children's Hospital of PhiladelphiaOlga Ostrovsky - Children's Hospital of PhiladelphiaCatherine A. Makarewich - University of PennsylvaniaSherry Wanderling - University of ChicagoTali Gidalevitz - University of ChicagoYair Argon - University of Chicago
- Publication Details
- Biochemical journal, v 405(Pt 2), pp 233-241
- Publisher
- Portland Press Ltd
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biology; College of Arts and Sciences; Drexel University
- Web of Science ID
- WOS:000248158600003
- Scopus ID
- 2-s2.0-34447132178
- Other Identifier
- 991020100077204721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology