Lipid modifications of trimeric G proteins.
Reads0
Chats0
TLDR
This work has shown how different lipid modifications of different G protein subunits affect specific protein-protein interactions and localization to specific cellular sites and regulation of these modifications, particularly palmitoylation, can provide new ways to regulate signals transmitted by G proteins.About:
This article is published in Journal of Biological Chemistry.The article was published on 1995-01-13 and is currently open access. It has received 459 citations till now. The article focuses on the topics: G protein & Palmitoylation.read more
Citations
More filters
Journal ArticleDOI
GTPase-Activating Proteins for Heterotrimeric G Proteins: Regulators of G Protein Signaling (RGS) and RGS-Like Proteins
Elliott M. Ross,Thomas M. Wilkie +1 more
TL;DR: GAP activity can sharpen the termination of a signal upon removal of stimulus, attenuate a signal either as a feedback inhibitor or in response to a second input, promote regulatory association of other proteins, or redirect signaling within a G protein signaling network.
Journal ArticleDOI
G PROTEIN MECHANISMS: Insights from Structural Analysis
TL;DR: This review is concerned with the structures and mechanisms of a superfamily of regulatory GTP hydrolases (G proteins), which include Ras and its close homologs, translation elongation factors, and heterotrimeric G proteins.
Journal ArticleDOI
Nitric oxide synthases: which, where, how, and why?
Thomas Michel,Olivier Feron +1 more
TL;DR: eNOS, the last of the three mammalian NOS isoforms to be isolated, was originally purified and cloned from vascular endothelium, but has since been discovered in cardiac myocytes, blood platelets, brain (hippocampus), and elsewhere.
Journal ArticleDOI
LAT Palmitoylation: Its Essential Role in Membrane Microdomain Targeting and Tyrosine Phosphorylation during T Cell Activation
TL;DR: It is demonstrated that human LAT is palmitoylated and that palMIToylated LAT predominantly localizes into glycolipid-enriched microdomains (GEMs).
Journal ArticleDOI
Protein lipidation in cell signaling
TL;DR: The ability of cells to communicate with and respond to their external environment is critical for their continued existence as mentioned in this paper, and a universal feature of this communication is that the external signal must in some way penetrate the lipid bilayer surrounding the cell.
References
More filters
Journal ArticleDOI
Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
TL;DR: It is proposed that caveolin could function as a transmembrane adaptor molecule that couples luminal G PI-linked proteins with cytoplasmically oriented signaling molecules during GPI- Membrane trafficking or GPI -mediated signal transduction events.
Journal ArticleDOI
Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: implications for human disease.
Michael P. Lisanti,Philipp E. Scherer,Jolanta Vidugiriene,ZhaoLan Tang,Anne Hermanowski-Vosatka,Ya Huei Tu,Richard F. Cook,Massimo Sargiacomo +7 more
TL;DR: Characterization of these complexes by micro-sequencing and immuno- blotting reveals known receptors for modified forms of LDL, multiple GPI-linked proteins, an anion transporter, cytoskeletal elements, and cytoplasmic signaling molecules--including Src-like kinases, hetero- trimeric G-proteins, and three members of the Rap family of small GTPases.
Journal ArticleDOI
Binding of acylated peptides and fatty acids to phospholipid vesicles : pertinence to myristoylated proteins
TL;DR: The interaction of myristoylated proteins with membranes are likely to be important and may cause reversible translocation of these proteins to the membrane.
Journal ArticleDOI
Inhibition of adenylyl cyclase by Gi alpha
TL;DR: Concentration-dependent inhibition of adenylyl cyclases by purified Gi alpha subunits is described, and analysis indicates that these concentrations may be relevant and reasonable.
Journal ArticleDOI
Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae.
TL;DR: Mapping of the requirement for partitioning into Caveolae demonstrated that the amino-terminal sequence Met-Gly-Cys is both necessary and sufficient within the context of a Src family PTK to confer localization into caveolae.