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anti-Mouse (Murine) rala Antibodies:
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Platelet Ral GTPases primarily control P-selectin surface expression, in turn regulating platelet-leukocyte interaction.
RalA plays a crucial role in glucose transport in adipose tissue in vivo.
This study identifies a novel regulatory crosstalk between Ral and Arf6 that controls Ral function in cells.
striking isoform-specific consequences of distinct CAAX-signaled posttranslational modifications that contribute to the divergent subcellular localization and activity of RalA and RalB.
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-long-term depression.
findings show either RALA or RALB is sufficient for tumor growth; either RALA or RALB is sufficient for cell proliferation; RALA and RALB act in a redundant fashion
study reports the identification and characterization of a Ral GAP complex (RG1, RGC2) that mediates the activation of RalA downstream of the PI 3-kinase/Akt pathway
A novel regulatory pathway involves RalA and phospholipase D in the production of phosphatidic acid during Fc gamma receptor-mediated phagocytosis and phagosome formation.
RalA but not RalB 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 in response to a rise in intracellular Ca2+ and cAMP controls hormone release from pancreatic beta-cells
RalA is activated by H-Ras, which along with ARF6, leads to phospholipase D activation
Activation of Rala is required for insulin-stimulated Glut4 trafficking to the plasma membrane via the exocyst and Myo1c protein.
RalA is a critical component in biphasic insulin release from pancreatic beta cells
Silencing Ral or inhibiting it with a dominant-negative Ral (Ral S28N) caused a significant reduction in proliferation, invasiveness, and in vivo tumorigenicity of malignant peripheral nerve sheath tumors.
Exocytosis pathway seems to be particularly important for M-induced nanotube formation, because interfering with the RalA.
These results show the power of data sharing for the interpretation and analysis of rare variation, expand the spectrum of molecular causes of developmental disability to include RALA, and provide additional insight into the pathogenesis of human disease caused by mutations in small GTPases.
In fact the overexpression of RalGPS2 or of its PH-domain increased markedly the number and the length of nanotubes, while the knock-down of RalGPS2 caused a strong reduction of these structures. Moreover, using a series of RalA mutants impaired in the interaction with different downstream components (Sec5, Exo84, RalBP1) we demonstrated that the interaction of RalA with Sec5 is required for TNTs formation
Study explored the function of RalA in regulating the localization of AQP3 in androgenindependent prostate cancer and demonstrated that depletion of RalA led to the redistribution of AQP3 into the plasma membrane.
Data show that ras related GTP binding protein A (Ral A) is necessary for 1-O-Hexadecyl-2-O-methyl-rac-glycerol (HMG)-mediated M phase arrest and induction of apoptosis in Nf1-deficient cells.
High RalA expression is associated with chronic myelogenous leukemia.
This study demonstrated that RalA is overactivated in medulloblastoma.
Study shows the additional benefits of anti-RalA autoantibody as a potential serological biomarker for prostate cancer (PCa), particularly in patients with normal PSA, and further demonstrate the utility of biomarker combinations in the immunodiagnosis of PCa.
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 RalA plays an important role in promoting invagination and trafficking of caveolae, not by potentiating the association between Cav-1 and FilA but by stimulating PLD2-mediated generation of phosphatidic acid.
agonist-induced Gbetagamma-mediated conversion of RalA from the GTP-bound form to the GDP-bound form could be a mechanism to facilitate agonist-induced internalization of GPCRs.
RCC2 exhibits guanine exchange factor activity, in vitro and in cells, for the small GTPase RalA. RCC2 and RalA apparently work together to contribute to the regulation of kinetochore-microtubule interactions in early mitosis.
expression of K-Ras and RalB and possibly RalA proteins is critical for maintaining low levels of p53, and down-regulation of these GTPases reactivates p53 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 and ACAN.
Data show that small GTPase RALA regulates formation of a JIP1 (C-Jun-amino-terminal-interacting protein 1) scaffold complex to propagate JNK signaling toward FOXO4 (forkhead box O transcription factor) in response to reactive oxygen species (ROS).
RalA and RalB exhibit both distinct and redundant roles in tumorigenesis (Review).
Targeted interference of EP2/EP4 signal to RalA.GTP may provide benefit to patients diagnosed with advanced kidney cancer.
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