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Membranes 2014, 4(3), 630-641; doi:10.3390/membranes4030630

Calreticulin: Roles in Cell-Surface Protein Expression

1
Department of Molecular Genetics and Microbiology, University Program of Genetics and Genomics, Duke University Medical Center, Durham, NC 27710, USA
2
Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
3
Department of Neurobiology, Duke Institute for Brain Sciences, Duke University Medical Center, Durham, NC 27710, USA
*
Authors to whom correspondence should be addressed.
Received: 10 June 2014 / Revised: 5 September 2014 / Accepted: 9 September 2014 / Published: 16 September 2014
(This article belongs to the Special Issue Trafficking of Membrane Receptors)
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Abstract

In order to perform their designated functions, proteins require precise subcellular localizations. For cell-surface proteins, such as receptors and channels, they are able to transduce signals only when properly targeted to the cell membrane. Calreticulin is a multi-functional chaperone protein involved in protein folding, maturation, and trafficking. However, evidence has been accumulating that calreticulin can also negatively regulate the surface expression of certain receptors and channels. In these instances, depletion of calreticulin enhances cell-surface expression and function. In this review, we discuss the role of calreticulin with a focus on its negative effects on the expression of cell-surface proteins. View Full-Text
Keywords: calreticulin; calreticulin4; calnexin; endoplasmic reticulum; chaperone; trafficking; receptor; channel; retention; vomeronasal; V2R; CFTR calreticulin; calreticulin4; calnexin; endoplasmic reticulum; chaperone; trafficking; receptor; channel; retention; vomeronasal; V2R; CFTR
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This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Jiang, Y.; Dey, S.; Matsunami, H. Calreticulin: Roles in Cell-Surface Protein Expression. Membranes 2014, 4, 630-641.

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