G Protein Activation without Subunit Dissociation Depends on a Gαi-specific Region*
نویسندگان
چکیده
منابع مشابه
High glucose condition down-regulates the inhibitory G-protein subunit, Gαi, in pheochromocytoma PC12 cells
Introduction: G-proteins have an important role in the cell signaling of numerous receptors. The situation of G-proteins in health and disease and their critical role in the development of diabetic side effects is an interested scientific field. Here, the changes in the expression of G-protein subunits (Gαi, Gαs and Gβ) were evaluated in hyperglycemic situation of PC12 cells as...
متن کاملhigh glucose condition down-regulates the inhibitory g-protein subunit, gαi, in pheochromocytoma pc12 cells
introduction: g-proteins have an important role in the cell signaling of numerous receptors. the situation of g-proteins in health and disease and their critical role in the development of diabetic side effects is an interested scientific field. here, the changes in the expression of g-protein subunits (gαi, gαs and gβ) were evaluated in hyperglycemic situation of pc12 cells as a cellular model...
متن کاملG-protein subunit dissociation is not an integral part of G-protein action.
The concept that a guanosine triphosphate (GTP) binding protein (or G protein) is a transducer of receptor-to-effector signal transduction was formulated in the 1970s for hormonedependent adenylyl cyclase. It has been shown that binding of the hormone to the receptor triggers exchange of guanosine diphosphate (GDP) for GTP on the G protein, thereby converting the G protein from the inactive con...
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Animal heterotrimeric G proteins are activated by guanine nucleotide exchange factors (GEF), typically seven transmembrane receptors that trigger GDP release and subsequent GTP binding. In contrast, the Arabidopsis thaliana G protein (AtGPA1) rapidly activates itself without a GEF and is instead regulated by a seven transmembrane Regulator of G protein Signaling (7TM-RGS) protein that promotes ...
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Quality control of defective mRNAs relies on their translation to detect the lesion. Aberrant proteins are therefore an obligate byproduct of mRNA surveillance and must be degraded to avoid disrupting protein homeostasis. These defective translation products are thought to be ubiquitinated at the ribosome, but the mechanism of ubiquitin ligase selectivity for these ribosomes is not clear. Here,...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2005
ISSN: 0021-9258
DOI: 10.1074/jbc.m414630200