GRP78: a multifunctional receptor on the cell surface.

Published

Journal Article (Review)

The 78 kDa glucose-regulated protein (GRP78) is an endoplasmic reticulum chaperone, whose function is generally thought to be restricted to controlling the structural maturation of nascent glycoproteins. However, GRP78 also is expressed on the cell surface where it functions as a receptor for a wide variety of ligands, behaving as an autoantigen for several classes of autoantibodies. GRP78 is a signaling receptor for activated alpha2-macroglobulin, plasminogen kringle 5, and microplasminogen, and it plays a critical role in viral entry of coxsackie B, and dengue fever viruses. GRP78 is also implicated in the regulation of tissue factor procoagulant activity and functions as a receptor for angiogenic peptides via a mechanism independent of the VEGF receptor. Cell surface GRP78 is found associated with such diverse proteins as the voltage-dependent anion channel (VDAC), the major histocompatibility complex class I (MHC-I), the teratocarcinoma-derived growth factor I (Cripto), and the DnaJ-like protein MTJ-1. These associations suggest a unique GRP78 cell surface topography, which appears to be compartmentalized to respond differently to agonists that bind to its N- or C-terminal domains. Here, we discuss the significance of these associations, and the possible mechanisms involved in the transportation of GRP78 from the cytosol to the cell surface.

Full Text

Duke Authors

Cited Authors

  • Gonzalez-Gronow, M; Selim, MA; Papalas, J; Pizzo, SV

Published Date

  • September 2009

Published In

Volume / Issue

  • 11 / 9

Start / End Page

  • 2299 - 2306

PubMed ID

  • 19331544

Pubmed Central ID

  • 19331544

Electronic International Standard Serial Number (EISSN)

  • 1557-7716

Digital Object Identifier (DOI)

  • 10.1089/ARS.2009.2568

Language

  • eng

Conference Location

  • United States