Publication: GRP78, A chaperone with diverse roles beyond the endoplasmic reticulum
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Date
2008
Authors
Quinones, Quintin J. ; Ridder, Gustaaf G. de ; Pizzo, Salvatore V.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Glucose-regulated protein 78 (GRP78) is a
well-characterized molecular chaperone that is
ubiquitously expressed in mammalian cells. GRP78 is
best known for binding to hydrophobic patches on
nascent polypeptides within the endoplasmic reticulum
(ER) and for its role in signaling the unfolded protein
response. Structurally, GRP78 is highly conserved across
species. The presence of GRP78 or a homologue in
nearly every organism from bacteria to man, reflects the
central roles it plays in cell survival. While the principal
role of GRP78 as a molecular chaperone is a matter of
continuing study, independent work demonstrates that
like many other proteins with ancient origins, GRP78
plays more roles than originally appreciated. Studies
have shown that GRP78 is expressed on the cell surface
in many tissue types both in vitro and in vivo. Cell
surface GRP78 is involved in transducing signals from
ligands as disparate as activated a2-macroglobulin and
antibodies. Plasmalemmar GRP78 also plays a role in
viral entry of Coxsackie B, and Dengue Fever viruses.
GRP78 disregulation is also implicated in
atherosclerotic, thrombotic, and auto-immune disease. It
is challenging to posit a hypothesis as to why an ER
molecular chaperone, such as GRP78, plays such a
variety of roles in cellular processes. An ancient and highly conserved protein such as GRP78, whose primary
function is to bind to misfolded polypeptides, could be
uniquely suited to bind a wide variety of ligands and
thus, over time, could assume the wide variety of roles it
now plays.
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