Heterotrimeric Gαq11 co‐immunoprecipitates with surface‐anchored GRP78 from plasma membranes of α2M*‐stimulated macrophages
Copyright policy )Heterotrimeric Gαq11 co‐immunoprecipitates with surface‐anchored GRP78 from plasma membranes of α2M*‐stimulated macrophages
AbstractWe have previously shown that a fraction of newly expressed GRP78 is translocated to the cell surface in association with the co‐chaperone MTJ‐1. Proteinase and methylamine‐activated α2M (α2M*) bind to cell surface‐associated GRP78 activating phosphoinositide‐specific phospholipase C coupled to a pertussis toxin‐insensitive heterotrimeric G protein, generating IP3/calcium signaling. We have now studied the association of pertussis toxin‐insensitive Gαq11, with GRP78/MTJ‐1 complexes in the plasma membranes of α2M*‐stimulated macrophages. When GRP78 was immunoprecipitated from plasma membranes of macrophages stimulated with α2M*, Gαq11, and MTJ‐1 were co‐precipitated. Likewise Gαq11 and GRP78 co‐immunoprecipitated with MTJ‐1 while GRP78 and MTJ‐1 co‐immunoprecipitated with Gαq11. Silencing GRP78 expression with GRP78 dsRNA or MTJ‐1 with MTJ‐1 dsRNA greatly reduced the levels of Gαq11 co‐precipitated with GRP78 or MTJ‐1. In conclusion, we show here that plasma membrane‐associated GRP78 is coupled to pertussis toxin‐insensitive Gαq11 and forms a ternary signaling complex with MTJ‐1. J. Cell. Biochem. 104: 96–104, 2008. © 2008 Wiley‐Liss, Inc.
- Duke University United States
- Duke University Hospital United States
- Duke Medical Center United States
Macrophages, Cell Membrane, Membrane Proteins, HSP40 Heat-Shock Proteins, Macrophage Activation, Heterotrimeric GTP-Binding Proteins, Mice, Animals, GTP-Binding Protein alpha Subunits, Gq-G11, Immunoprecipitation, Endoplasmic Reticulum Chaperone BiP, Heat-Shock Proteins, Molecular Chaperones, Signal Transduction
Macrophages, Cell Membrane, Membrane Proteins, HSP40 Heat-Shock Proteins, Macrophage Activation, Heterotrimeric GTP-Binding Proteins, Mice, Animals, GTP-Binding Protein alpha Subunits, Gq-G11, Immunoprecipitation, Endoplasmic Reticulum Chaperone BiP, Heat-Shock Proteins, Molecular Chaperones, Signal Transduction
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).29 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 10%
Citations provided by BIP!Popularity provided by BIP!