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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Resistance to inhibitors of cholinesterase 8 homolog

Ric-8, RIC8A
Top mentioned proteins: RIC, GEF, Cholinesterase, GPR, CAN
Papers on Ric-8
B Lymphocyte-Specific Loss of Ric-8A Results in a Gα Protein Deficit and Severe Humoral Immunodeficiency.
Kehrl et al., Bethesda, United States. In J Immunol, Oct 2015
Resistance to inhibitors of cholinesterase 8A (Ric-8A) is a highly evolutionarily conserved cytosolic protein initially identified in Caenorhabditis elegans, where it was assigned a regulatory role in asymmetric cell divisions.
Deletion of RIC8A in neural precursor cells leads to altered neurogenesis and neonatal lethality of mouse.
Pooga et al., Tartu, Estonia. In Dev Neurobiol, Sep 2015
RIC8A is a noncanonical guanine nucleotide exchange factor for a subset of Gα subunits.
Activator of G protein signaling 3 forms a complex with resistance to inhibitors of cholinesterase-8A without promoting nucleotide exchange on Gα(i3).
Wong et al., Hong Kong, Hong Kong. In Mol Cell Biochem, Mar 2015
It has recently been demonstrated in reconstitution experiments that the AGS3/Gα(i/o)-GDP complex may act as a substrate of resistance to inhibitors of cholinesterase 8A (Ric-8A), a guanine exchange factor (GEF) for heterotrimeric Gα proteins.
The guanine nucleotide exchange factor Ric-8A induces domain separation and Ras domain plasticity in Gαi1.
Sprang et al., Missoula, United States. In Proc Natl Acad Sci U S A, Mar 2015
Ric-8A is a soluble cytoplasmic protein essential for embryonic development that acts as both a guanine nucleotide exchange factor (GEF) and a chaperone for Gα subunits of the i, q, and 12/13 classes.
The guanine-exchange factor Ric8a binds to the Ca²⁺ sensor NCS-1 to regulate synapse number and neurotransmitter release.
Ferrús et al., Madrid, Spain. In J Cell Sci, 2014
We show here that Drosophila Ric8a (a homolog of mammalian synembryn, which is also known as Ric8a), a receptor-independent activator of G protein complexes, binds to Frq2 but not to the virtually identical homolog Frq1.
Implications of non-canonical G-protein signaling for the immune system.
Kehrl et al., Bethesda, United States. In Cell Signal, 2014
In these pathways the guanine exchange factor (GEF) exerted by a GPCR in the canonical pathway is replaced or supplemented by another protein such as Ric-8A.
Resistance to inhibitors of cholinesterase (Ric)-8A and Gαi contribute to cytokinesis abscission by controlling vacuolar protein-sorting (Vps)34 activity.
Kehrl et al., Bethesda, United States. In Plos One, 2013
Ric-8A, Gαi subunits, and their regulators are localized at the midbody prior to abscission and linked to the final stages of cell division.
Ric-8 regulation of heterotrimeric G proteins.
Tall, Rochester, United States. In J Recept Signal Transduct Res, 2013
Resistance to inhibitors of cholinesterase 8 proteins (Ric-8A and Ric-8B) collectively bind the four classes of heterotrimeric G protein α subunits.
NCAM180 regulates Ric8A membrane localization and potentiates β-adrenergic response.
Rougon et al., Marseille, France. In Plos One, 2011
NCAM180 regulates Ric8A membrane localization and potentiates beta-adrenergic response
G protein-coupled receptors and resistance to inhibitors of cholinesterase-8A (Ric-8A) both regulate the regulator of g protein signaling 14 RGS14·Gαi1 complex in live cells.
Blumer et al., Atlanta, United States. In J Biol Chem, 2011
RGS14 can form complexes with GPCRs in cells that are dependent on Galpha(i/o) and these RGS14.Galpha(i1).GPCR complexes may be substrates for other signaling partners such as Ric-8A
Resistance to inhibitors of cholinesterase-8A (Ric-8A) is critical for growth factor receptor-induced actin cytoskeletal reorganization.
Huang et al., Wuhan, China. In J Biol Chem, 2011
Ric-8A is critical for growth factor receptor-induced actin cytoskeletal reorganization
Activation of the regulator of G protein signaling 14-Gαi1-GDP signaling complex is regulated by resistance to inhibitors of cholinesterase-8A.
Hepler et al., Atlanta, United States. In Biochemistry, 2011
Activation of the Rsg14-Galphai1-GDP signaling complex is regulated by Ric8.
Ric-8 proteins are molecular chaperones that direct nascent G protein α subunit membrane association.
Tall et al., Rochester, United States. In Sci Signal, 2010
data suggest that Ric-8 proteins are molecular chaperones required for the initial association of nascent Galpha subunits with cellular membranes
Novel regulation of adenylyl cyclases by direct protein-protein interactions: insights from snapin and ric8a.
Chern et al., Taipei, Taiwan. In Neurosignals, 2008
Based on recent studies on AC-interacting proteins (particularly Snapin and Ric8a), this review focuses on the importance and possible involvement of AC-interacting proteins in (1) the association of the cAMP signaling pathway with various cellular machineries and (2) the coordination of tightly regulated cAMP signaling by other signaling molecules.
Heterotrimeric G proteins in C. elegans.
Mendel et al., Pasadena, United States. In Wormbook, 2005
The rate of G protein activation can be enhanced by the guanine-nucleotide exchange factor, RIC-8, while the rate of GTP hydrolysis can be enhanced by RGS proteins such as EGL-10 and EAT-16.
Ric-8 controls Drosophila neural progenitor asymmetric division by regulating heterotrimeric G proteins.
Yu et al., Singapore, Singapore. In Nat Cell Biol, 2005
Another key component of this non-canonical G-protein activation mechanism is a non-receptor guanine nucleotide-exchange factor (GEF) for Galpha, RIC-8, which has recently been characterized in C. elegans and in mammals.
Drosophila Ric-8 is essential for plasma-membrane localization of heterotrimeric G proteins.
Knoblich et al., Vienna, Austria. In Nat Cell Biol, 2005
We show here that, in Drosophila, both functions require the Galpha interaction partner Ric-8.
New roles for Galpha and RGS proteins: communication continues despite pulling sisters apart.
Kinch et al., Dallas, United States. In Curr Biol, 2005
Recent studies have led to the discovery of GPCR-independent activation of Galpha subunits by the guanine nucleotide exchange factor RIC-8 in both asymmetric cell division and synaptic vesicle priming in metazoan organisms.
RIC-8 is required for GPR-1/2-dependent Galpha function during asymmetric division of C. elegans embryos.
Gönczy et al., Lausanne, Switzerland. In Cell, 2004
Here, we establish that the evolutionarily conserved protein RIC-8 is required for proper asymmetric division of one-cell stage C. elegans embryos.
RGS-7 completes a receptor-independent heterotrimeric G protein cycle to asymmetrically regulate mitotic spindle positioning in C. elegans.
Koelle et al., New Haven, United States. In Cell, 2004
RGS-7 is localized at the cell cortex, and its effects require two redundant Galphao-related G proteins and their nonreceptor activators RIC-8 and GPR-1/2.
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