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Data indicate that Ric-8 binds to Galpha12/13 subunit, Concertina (Cta (show PCYT1A Proteins)) 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 (show NLRP2 Proteins) 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 (show GPSM1 Proteins)) and guanine nucleotide exchange factor (show ARHGEF12 Proteins) RIC-8 act during food deprivation in a mutually dependent fashion to activate G protein Galpha(o (show GNAO1 Proteins)).
Data suggest a mechanism in which RIC-8 favors generation of Galpha (show SUCLG1 Proteins) 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 (show GNAS Proteins)) 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 (show GNAS Proteins)) pathway in a functional state.
RIC-8 directly modulates Galpha (show SUCLG1 Proteins) activity and that Galpha (show SUCLG1 Proteins)-GTP (show AK3 Proteins) 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 (show SUCLG1 Proteins) proteins and GPR-1/2
found that RIC8A plays an important role in the organisation and remodelling of actin cytoskeleton and cell-extracellular matrix association
Results suggest that RIC8A has an essential role in the development of mammalian nervous system by maintaining the integrity of pial basement membrane and modulating cell division
Data show that the localization of maternally expressed RIC8 protein is highly dynamic and is dependent on the stage of folliculogenesis, oogenesis and cleavage, and imply that it may have a regulatory function in mammalian gametogenesis.
Data show that disrupting resistance to inhibitors of cholinesterase 8A (Ric-8A) expression in hematopoietic cells results in a loss of GTP-binding protein (show DRG1 Proteins) alpha subunits Galphai2 (show GNAI2 Proteins), Galphai3 (show GNAI3 Proteins), and Galphaq (show GNAQ Proteins).
The activity of RIC8A in neurons is essential for survival and its deficiency causes a severe neuromuscular phenotype.
Ric-8 proteins support G protein levels by serving as molecular chaperones that promote Galpha (show SUCLG1 Proteins) subunit biosynthesis
These data indicate a dynamic interaction between GPR (show ALDH18A1 Proteins) proteins, Galpha (show SUCLG1 Proteins)(i1) and Ric-8A, in the cell that influences subcellular localization of the three proteins and regulates complex formation.
The results of this study revealed a novel role of Ric-8a in modulating Bergmann glia-basement membrane adhesion during foliation.
NCAM180 regulates Ric8A membrane localization and potentiates beta-adrenergic response
data suggest that Ric-8 proteins are molecular chaperones required for the initial association of nascent Galpha (show SUCLG1 Proteins) subunits with cellular membranes
Human NCS-1 (show NCS1 Proteins) and Ric8a reproduce the binding and maintain the structural requirements at these key positions. Drosophila Ric8a and Galphas (show GNAS Proteins) 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 (show SUCLG1 Proteins)(i)-induced suppression of adenylyl cyclase, suggesting that it may not serve as a guanine exchange factor for AGS3 (show GPSM1 Proteins)/Galpha (show SUCLG1 Proteins)(i/o)-GDP complex in a cellular environment.
Ric-8A co-localized with Vps34 (show PIK3C3 Proteins) at the midbody.
The ubiquitination of Galphai2 (show GNAI2 Proteins) and Galphaq (show GNAQ Proteins) is suppressed by expression of Ric-8A. The suppression likely requires Ric-8A interaction with these Galpha (show SUCLG1 Proteins) proteins; the C-terminal truncation of Galphaq (show GNAQ Proteins) and Galphai2 (show GNAI2 Proteins) completely abrogates their interaction with Ric-8A.
RGS14 (show RGS14 Proteins) can form complexes with GPCRs in cells that are dependent on Galpha (show SUCLG1 Proteins)(i/o) and these RGS14 (show RGS14 Proteins).Galpha (show SUCLG1 Proteins)(i1).GPCR (show NMUR1 Proteins) 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