Document Detail


Beyond the endoplasmic reticulum: atypical GRP78 in cell viability, signalling and therapeutic targeting.
MedLine Citation:
PMID:  21309747     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
GRP78 (glucose-regulated protein of 78 kDa) is traditionally regarded as a major ER (endoplasmic reticulum) chaperone facilitating protein folding and assembly, protein quality control, Ca(2+) binding and regulating ER stress signalling. It is a potent anti-apoptotic protein and plays a critical role in tumour cell survival, tumour progression and angiogenesis, metastasis and resistance to therapy. Recent evidence shows that GRP78 can also exist outside the ER. The finding that GRP78 is present on the surface of cancer but not normal cells in vivo represents a paradigm shift on how GRP78 controls cell homoeostasis and provides an opportunity for cancer-specific targeting. Cell-surface GRP78 has emerged as an important regulator of tumour cell signalling and viability as it forms complexes with a rapidly expanding repertoire of cell-surface protein partners, regulating proliferation, PI3K (phosphoinositide 3-kinase)/Akt signalling and cell viability. Evidence is also emerging that GRP78 serves as a receptor for viral entry into host cells. Additionally, a novel cytosolic form of GRP78 has been discovered prominently in leukaemia cells. These, coupled with reports of nucleus- and mitochondria-localized forms of GRP78, point to the previously unanticipated role of GRP78 beyond the ER that may be critical for cell viability and therapeutic targeting.
Authors:
Min Ni; Yi Zhang; Amy S Lee
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Review    
Journal Detail:
Title:  The Biochemical journal     Volume:  434     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2011 Mar 
Date Detail:
Created Date:  2011-02-11     Completed Date:  2011-04-19     Revised Date:  2012-05-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  181-8     Citation Subset:  IM    
Copyright Information:
© The Authors Journal compilation © 2011 Biochemical Society
Affiliation:
Department of Biochemistry and Molecular Biology, University of Southern California Keck School of Medicine, USC Norris Comprehensive Cancer Center, 1441 Eastlake Avenue, Los Angeles, CA 90089-9176, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Membrane / metabolism
Cell Nucleus / metabolism
Cell Survival
Cytosol / metabolism
Endoplasmic Reticulum / metabolism*
Heat-Shock Proteins / metabolism*
Humans
Models, Biological
Neoplasms / drug therapy
Signal Transduction*
Grant Support
ID/Acronym/Agency:
CA027607/CA/NCI NIH HHS; CA111700/CA/NCI NIH HHS; DK079999/DK/NIDDK NIH HHS; R01 CA027607/CA/NCI NIH HHS; R01 CA111700/CA/NCI NIH HHS; R01 DK079999/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Heat-Shock Proteins; 0/molecular chaperone GRP78

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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