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striking isoform-specific consequences of distinct CAAX-signaled posttranslational modifications that contribute to the divergent subcellular localization and activity of RalA and RalB (show Ralb Proteins).
RalA activation was remarkably impaired in rac1-deficient skeletal muscle fibres.
Our results provide the first in vivo characterization of RalA function in the mammalian brain and highlight a novel molecular mechanism for cell polarization.
The constitutively increased RalA activity occludes further increases in RalA activity during induction of long-term depression, causing impaired NMDAR (show GRIN1 Proteins)-long-term depression.
findings show either RALA or RALB (show Ralb Proteins) is sufficient for tumor growth; either RALA or RALB (show Ralb Proteins) is sufficient for cell proliferation; RALA and RALB (show Ralb Proteins) act in a redundant fashion
study reports the identification and characterization of a Ral GAP complex (RG1 (show PPP1R3A Proteins), RGC2) that mediates the activation of RalA downstream of the PI 3 (show PI3 Proteins)-kinase/Akt (show AKT1 Proteins) pathway
A novel regulatory pathway involves RalA and phospholipase D in the production of phosphatidic acid during Fc gamma receptor (show FCGR1A Proteins)-mediated phagocytosis and phagosome formation.
RalA but not RalB (show Ralb Proteins) mediates integrin-dependent membrane raft exocytosis through the exocyst complex. Constitutively active RalA restores membrane raft targeting to promote anchorage-independent growth signaling.
RalA activation elicited by the exchange factor RalGDS (show RALGDS Proteins) in response to a rise in intracellular Ca2 (show CA2 Proteins)+ and cAMP controls hormone release from pancreatic beta-cells
RalA is activated by H-Ras, which along with ARF6, leads to phospholipase D activation
Lowering the level of cellular FLNA caused an elevation in RalA activity and resulted in selective interference with the normal intracellular trafficking and signaling of the D2R and D3R, through GRK2 and beta-arrestins, respectively. Active RalA was found to interact with GRK2 to sequester it from D2R. Knockdown of FLNA or coexpression of active RalA prevented D3R from coupling with G protein.
results suggest that the small GTPase (show RACGAP1 Proteins) RalA plays an important role in promoting invagination and trafficking of caveolae, not by potentiating the association between Cav-1 (show CAV1 Proteins) and FilA but by stimulating PLD2 (show PLD2 Proteins)-mediated generation of phosphatidic acid.
agonist-induced Gbetagamma-mediated conversion of RalA from the GTP (show AK3 Proteins)-bound form to the GDP-bound form could be a mechanism to facilitate agonist-induced internalization of GPCRs.
RCC2 (show RCC2 Proteins) exhibits guanine exchange factor activity, in vitro and in cells, for the small GTPase (show RACGAP1 Proteins) RalA. RCC2 (show RCC2 Proteins) and RalA apparently work together to contribute to the regulation of kinetochore-microtubule interactions in early mitosis.
expression of K-Ras (show HRAS Proteins) and RalB (show Ralb Proteins) and possibly RalA proteins is critical for maintaining low levels of p53 (show TP53 Proteins), and down-regulation of these GTPases reactivates p53 (show TP53 Proteins) by significantly enhancing its stability, contributing to suppression of malignant transformation
These results indicate that MLN8237 treatment may be effective for a subset of patients with PDAC independent of RalA S194 phosphorylation
microRNA-140 targets RALA and regulates chondrogenic differentiation of human mesenchymal stem cells by translational enhancement of SOX9 (show SOX9 Proteins) and ACAN (show ACAN Proteins).
Data show that small GTPase (show RACGAP1 Proteins) RALA regulates formation of a JIP1 (show MAPK8IP1 Proteins) (C-Jun (show JUN Proteins)-amino-terminal-interacting protein 1) scaffold complex to propagate JNK (show MAPK8 Proteins) signaling toward FOXO4 (show FOXO4 Proteins) (forkhead box O transcription factor) in response to reactive oxygen species (ROS (show ROS1 Proteins)).
The product of this gene belongs to the small GTPase superfamily, Ras family of proteins. GTP-binding proteins mediate the transmembrane signaling initiated by the occupancy of certain cell surface receptors. This gene encodes a low molecular mass ras-like GTP-binding protein that shares about 50% similarity with other ras proteins.
RAS-like, family 1
, ral-A protein
, ras-related protein Ral-A
, -ral simian leukemia viral oncogene homolog A (ras related)
, RAS-like protein A
, Ras family small GTP binding protein RALA
, ras related v-ral simian leukemia viral oncogene homolog A