Calreticulin: Roles in Cell-Surface Protein Expression

Membranes

Yue Jiang²  Sandeepa Dey¹ 

[1] Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA; E-Mail:;Department of Molecular Genetics and Microbiology, University Program of Genetics and Genomics, Duke University Medical Center, Durham, NC 27710, USA

关键词: calreticulin;    calreticulin4;    calnexin;    endoplasmic reticulum;    chaperone;    trafficking;    receptor;    channel;    retention;    vomeronasal;    V2R;    CFTR;   

DOI  :  10.3390/membranes4030630

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.