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the small molecule stabilizes a mobile C-terminal helix inside a hydrophobic crevice of NCS-1 to impede Ric8a interaction.
Data indicate that Ric-8 binds to Galpha12/13 subunit, Concertina (Cta) through an interface of conserved residues.
Ric-8, which belongs to a family of guanine nucleotide-exchange factors for Galphai, regulates cortical localization of the subunits Galphai and Gbeta13F.
both receptor-dependent and receptor-independent G-protein functions are executed at the plasma membrane and require the Ric-8 protein.
Ric-8 homologue is required for asymmetric division of both NBs and pl cells.Ric-8 is necessary for membrane targeting of Galphai, Pins and Gbeta13F
New studies show that targeting of G-protein subunits to membrane requires Ric-8, pointing to possible novel roles for this protein in both receptor-dependent and independent pathways.
Data suggest that Ric-8A plays essential roles during the migration of cranial neural crest (NC) cells, possibly by regulating cell adhesion and spreading.
Genetic epistasis experiments show that activator of G protein signaling (AGS-3) and guanine nucleotide exchange factor RIC-8 act during food deprivation in a mutually dependent fashion to activate G protein Galpha(o).
Data suggest a mechanism in which RIC-8 favors generation of Galpha free from Gbetagamma and enables GPR-1/2 to mediate asymmetric cell division.
ric-8 (synembryn) paralysis can be rescued by neuronal G alpha(s) pathway activation.
Analysis of a ric-8 mutant suggests that it is required to maintain both the G alpha(q) vesicle priming pathway and the neuronal G alpha(s) pathway in a functional state.
RIC-8 directly modulates Galpha activity and that Galpha-GTP is the signaling molecule regulating spindle positioning in the early embryo
requirement toward GPA-16 is distinct from the known function of RIC-8 in enabling interaction between Galpha proteins and GPR-1/2
Human NCS-1 and Ric8a reproduce the binding and maintain the structural requirements at these key positions. Drosophila Ric8a and Galphas regulate synapse number and neurotransmitter release, and both are functionally linked to Frq2.
Results confirmed that Ric-8A can directly bind to AGS3S but failed to facilitate Galpha(i)-induced suppression of adenylyl cyclase, suggesting that it may not serve as a guanine exchange factor for AGS3/Galpha(i/o)-GDP complex in a cellular environment.
Ric-8A co-localized with Vps34 at the midbody.
The ubiquitination of Galphai2 and Galphaq is suppressed by expression of Ric-8A. The suppression likely requires Ric-8A interaction with these Galpha proteins; the C-terminal truncation of Galphaq and Galphai2 completely abrogates their interaction with Ric-8A.
NCAM180 regulates Ric8A membrane localization and potentiates beta-adrenergic response
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
Ric-8A is critical for growth factor receptor-induced actin cytoskeletal reorganization
Ric-8A signaling leads to assembly of a cortical signaling complex that functions to orient the mitotic spindle.
Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex (By similarity). Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation.
, resistance to inhibitors of cholinesterase 8 homolog A
, resistance to inhibitors of cholinesterase 8 homolog A a
, resistance to inhibitors of cholinesterase 8 homolog A (C. elegans)
, heterotrimeric G protein guanine nucleotide exchange factor Ric-8A
, resistance to inhibitors of cholinesterase 8A
, likely ortholog of mouse synembryn
, synembryn A
, Protein Ric-8A
, resistance to inhibitors of cholinesterase 8 homolog A b