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    RALA RAS like proto-oncogene A [ Homo sapiens (human) ]

    Gene ID: 5898, updated on 17-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Obesity causes mitochondrial fragmentation and dysfunction in white adipocytes due to RalA activation.

    Obesity causes mitochondrial fragmentation and dysfunction in white adipocytes due to RalA activation.
    Xia W, Veeragandham P, Cao Y, Xu Y, Rhyne TE, Qian J, Hung CW, Zhao P, Jones Y, Gao H, Liddle C, Yu RT, Downes M, Evans RM, Rydén M, Wabitsch M, Wang Z, Hakozaki H, Schöneberg J, Reilly SM, Huang J, Saltiel AR., Free PMC Article

    05/24/2024
    Ral GTPase promotes metastasis of pancreatic ductal adenocarcinoma via elevation of TGF-beta1 production.

    Ral GTPase promotes metastasis of pancreatic ductal adenocarcinoma via elevation of TGF-β1 production.
    Cao M, Li X, Trinh DA, Yoshimachi S, Goto K, Sakata N, Ishida M, Ohtsuka H, Unno M, Wang Y, Shirakawa R, Horiuchi H., Free PMC Article

    07/3/2023
    Identification of RALA as a Therapeutic Target and Prognostic Predictor of Osteosarcoma.

    Identification of RALA as a Therapeutic Target and Prognostic Predictor of Osteosarcoma.
    Fan G, Zhu Y, Zhu H, Yu L, Wang Z, Zhai C, Zhou G, Zhao J, Wang Y., Free PMC Article

    03/1/2023
    Dysregulation of RalA signaling through dual regulatory mechanisms exerts its oncogenic functions in hepatocellular carcinoma.

    Dysregulation of RalA signaling through dual regulatory mechanisms exerts its oncogenic functions in hepatocellular carcinoma.
    Tian L, Zhao L, Sze KM, Kam CS, Ming VS, Wang X, Zhang VX, Ho DW, Cheung TT, Chan LK, Ng IO., Free PMC Article

    06/25/2022
    RalA and PLD1 promote lipid droplet growth in response to nutrient withdrawal.

    RalA and PLD1 promote lipid droplet growth in response to nutrient withdrawal.
    Hussain SS, Tran TM, Ware TB, Luse MA, Prevost CT, Ferguson AN, Kashatus JA, Hsu KL, Kashatus DF., Free PMC Article

    02/12/2022
    The small G-protein RalA promotes progression and metastasis of triple-negative breast cancer.

    The small G-protein RalA promotes progression and metastasis of triple-negative breast cancer.
    Thies KA, Cole MW, Schafer RE, Spehar JM, Richardson DS, Steck SA, Das M, Lian AW, Ray A, Shakya R, Knoblaugh SE, Timmers CD, Ostrowski MC, Chakravarti A, Sizemore GM, Sizemore ST., Free PMC Article

    01/1/2022
    RAL GTPases mediate EGFR-driven intestinal stem cell proliferation and tumourigenesis.

    RAL GTPases mediate EGFR-driven intestinal stem cell proliferation and tumourigenesis.
    Nászai M, Bellec K, Yu Y, Román-Fernández A, Sandilands E, Johansson J, Campbell AD, Norman JC, Sansom OJ, Bryant DM, Cordero JB., Free PMC Article

    10/23/2021
    Ral GTPase-activating protein regulates the malignancy of pancreatic ductal adenocarcinoma.

    Ral GTPase-activating protein regulates the malignancy of pancreatic ductal adenocarcinoma.
    Yoshimachi S, Shirakawa R, Cao M, Trinh DA, Gao P, Sakata N, Miyazaki K, Goto K, Miura T, Ariake K, Maeda S, Masuda K, Ishida M, Ohtsuka H, Unno M, Horiuchi H., Free PMC Article

    08/21/2021
    RAL GTPases mediate multiple myeloma cell survival and are activated independently of oncogenic RAS.

    RAL GTPases mediate multiple myeloma cell survival and are activated independently of oncogenic RAS.
    Seibold M, Stühmer T, Kremer N, Mottok A, Scholz CJ, Schlosser A, Leich E, Holzgrabe U, Brünnert D, Barrio S, Kortüm MK, Solimando AG, Chatterjee M, Einsele H, Rosenwald A, Bargou RC, Steinbrunn T., Free PMC Article

    05/1/2021
    RalA and RalB both relocalize to mitochondria following depolarization in a process dependent on clathrin-mediated endocytosis. Furthermore, both genetic and pharmacologic inhibition of RalA and RalB leads to an increase in the activity of the atypical IkappaB kinase TBK1 both basally and in response to mitochondrial depolarization.

    RalA and RalB relocalization to depolarized mitochondria depends on clathrin-mediated endocytosis and facilitates TBK1 activation.
    Pollock SR, Schinlever AR, Rohani A, Kashatus JA, Kashatus DF., Free PMC Article

    01/4/2020
    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.

    De novo mutations in the GTP/GDP-binding region of RALA, a RAS-like small GTPase, cause intellectual disability and developmental delay.
    Hiatt SM, Neu MB, Ramaker RC, Hardigan AA, Prokop JW, Hancarova M, Prchalova D, Havlovicova M, Prchal J, Stranecky V, Yim DKC, Powis Z, Keren B, Nava C, Mignot C, Rio M, Revah-Politi A, Hemati P, Stong N, Iglesias AD, Suchy SF, Willaert R, Wentzensen IM, Wheeler PG, Brick L, Kozenko M, Hurst ACE, Wheless JW, Lacassie Y, Myers RM, Barsh GS, Sedlacek Z, Cooper GM., Free PMC Article

    02/9/2019
    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

    RalGPS2 is involved in tunneling nanotubes formation in 5637 bladder cancer cells.
    D'Aloia A, Berruti G, Costa B, Schiller C, Ambrosini R, Pastori V, Martegani E, Ceriani M.

    10/6/2018
    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.

    Subcellular localization of aquaporin 3 in prostate cancer is regulated by RalA.
    Chen Q, Zhu L, Zong H, Song X, Wang L, Wang X, Yang D, Wang J.

    09/1/2018
    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.

    Ral A, via activating the mitotic checkpoint, sensitizes cells lacking a functional Nf1 to apoptosis in the absence of protein kinase C.
    Ganapathy S, Fagman JB, Shen L, Yu T, Zhou X, Dai W, Makriyannis A, Chen C., Free PMC Article

    03/10/2018
    High RalA expression is associated with chronic myelogenous leukemia.

    RalA, a GTPase targeted by miR-181a, promotes transformation and progression by activating the Ras-related signaling pathway in chronic myelogenous leukemia.
    Gu C, Feng M, Yin Z, Luo X, Yang J, Li Y, Li T, Wang R, Fei J., Free PMC Article

    01/27/2018
    This study demonstrated that RalA is overactivated in medulloblastoma.

    RalA is overactivated in medulloblastoma.
    Ginn KF, Fangman B, Terai K, Wise A, Ziazadeh D, Shah K, Gartrell R, Ricke B, Kimura K, Mathur S, Borrego-Diaz E, Farassati F.

    01/6/2018
    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.

    Evaluation and characterization of anti-RalA autoantibody as a potential serum biomarker in human prostate cancer.
    Li J, Dai L, Lei N, Xing M, Li P, Luo C, Casiano CA, Zhang JY., Free PMC Article

    12/30/2017
    This study identifies a novel regulatory crosstalk between Ral and Arf6 that controls Ral function in cells.

    Ral-Arf6 crosstalk regulates Ral dependent exocyst trafficking and anchorage independent growth signalling.
    Pawar A, Meier JA, Dasgupta A, Diwanji N, Deshpande N, Saxena K, Buwa N, Inchanalkar S, Schwartz MA, Balasubramanian N., Free PMC Article

    12/2/2017
    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.

    RalA employs GRK2 and β-arrestins for the filamin A-mediated regulation of trafficking and signaling of dopamine D2 and D3 receptor.
    Zheng M, Zhang X, Sun N, Min C, Zhang X, Kim KM.

    10/28/2017
    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.

    Phosphatidic Acid Produced by RalA-activated PLD2 Stimulates Caveolae-mediated Endocytosis and Trafficking in Endothelial Cells.
    Jiang Y, Sverdlov MS, Toth PT, Huang LS, Du G, Liu Y, Natarajan V, Minshall RD., Free PMC Article

    05/20/2017
    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.

    Agonist-induced changes in RalA activities allows the prediction of the endocytosis of G protein-coupled receptors.
    Zheng M, Zhang X, Guo S, Zhang X, Min C, Cheon SH, Oak MH, Kim YR, Kim KM.

    04/30/2016
    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.

    TD-60 links RalA GTPase function to the CPC in mitosis.
    Papini D, Langemeyer L, Abad MA, Kerr A, Samejima I, Eyers PA, Jeyaprakash AA, Higgins JM, Barr FA, Earnshaw WC., Free PMC Article

    04/23/2016
    striking isoform-specific consequences of distinct CAAX-signaled posttranslational modifications that contribute to the divergent subcellular localization and activity of RalA and RalB.

    Divergent roles of CAAX motif-signaled posttranslational modifications in the regulation and subcellular localization of Ral GTPases.
    Gentry LR, Nishimura A, Cox AD, Martin TD, Tsygankov D, Nishida M, Elston TC, Der CJ., Free PMC Article

    12/5/2015
    RalA activation was remarkably impaired in rac1-deficient skeletal muscle fibres.

    Role for RalA downstream of Rac1 in skeletal muscle insulin signalling.
    Takenaka N, Sumi Y, Matsuda K, Fujita J, Hosooka T, Noguchi T, Aiba A, Satoh T.

    11/14/2015
    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

    Ral GTPase down-regulation stabilizes and reactivates p53 to inhibit malignant transformation.
    Tecleab A, Zhang X, Sebti SM., Free PMC Article

    01/24/2015
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