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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
In conditional Ric8a knockout mice the absence of RIC8A severely affected the attachment and positioning of radial glial processes, Cajal-Retzius' cells, and the arachnoid trabeculae, and these mice displayed additional defects in the lens, skeletal muscles, and heart development. All the discovered defects might be linked to aberrancies in cell adhesion and migration.
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 alpha subunits Galphai2, Galphai3, and Galphaq.
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 subunit biosynthesis
These data indicate a dynamic interaction between GPR proteins, Galpha(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 subunits with cellular membranes
Ric-8A is critical for growth factor receptor-induced actin cytoskeletal reorganization
Activation of the Rsg14-Galphai1-GDP signaling complex is regulated by Ric8.
Study reveals that the activity of RIC-8 protein is irreplaceable for the correct gastrulation of mouse embryo.
Here we show that during the early development in mice (E9.5-E12.0) ric-8 (synembryn) is expressed in the developing nervous system
Based on these results we can conclude the importance of ric-8 in the regulation of memory and emotional behavior.
These results suggested that Ric-8A potentiates Gq-mediated signal transduction by acting as a novel-type regulator in intact cells.
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.
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 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