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    ARHGAP1 Rho GTPase activating protein 1 [ Homo sapiens (human) ]

    Gene ID: 392, updated on 3-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Cdc42GAP deficiency contributes to the Alzheimer's disease phenotype.

    Cdc42GAP deficiency contributes to the Alzheimer's disease phenotype.
    Zhu M, Xiao B, Xue T, Qin S, Ding J, Wu Y, Tang Q, Huang M, Zhao N, Ye Y, Zhang Y, Zhang B, Li J, Guo F, Jiang Y, Zhang L, Zhang L.

    10/11/2023
    The Role of ARHGAP1 in Rho GTPase Inactivation during Metastasizing of Breast Cancer Cell Line MCF-7 after Treatment with Doxorubicin.

    The Role of ARHGAP1 in Rho GTPase Inactivation during Metastasizing of Breast Cancer Cell Line MCF-7 after Treatment with Doxorubicin.
    Géci I, Bober P, Filová E, Amler E, Sabo J., Free PMC Article

    08/7/2023
    circRNA RPPH1 Facilitates the Aggravation of Breast Cancer Development by Regulating miR-542-3p/ARHGAP1 Pathway.

    circRNA RPPH1 Facilitates the Aggravation of Breast Cancer Development by Regulating miR-542-3p/ARHGAP1 Pathway.
    Qi L, Sun B, Yang B, Lu S.

    10/29/2022
    Exosome miR-134-5p restrains breast cancer progression via regulating PI3K/AKT pathway by targeting ARHGAP1.

    Exosome miR-134-5p restrains breast cancer progression via regulating PI3K/AKT pathway by targeting ARHGAP1.
    Yang C, Zhang G, Zhang Y, Zhang S, Li J, Liu Y.

    11/27/2021
    Angio-associated migratory cell protein (AAMP) interacts with cell division cycle 42 (CDC42) and enhances migration and invasion in human non-small cell lung cancer cells.

    Angio-associated migratory cell protein (AAMP) interacts with cell division cycle 42 (CDC42) and enhances migration and invasion in human non-small cell lung cancer cells.
    Yao S, Shi F, Mu N, Li X, Ma G, Wang Y, Sun X, Liu X, Su L.

    08/7/2021
    identified ARHGAP1, which is a negative regulator of CDC42, as a novel, direct target of miR-130b

    miR-130b directly targets ARHGAP1 to drive activation of a metastatic CDC42-PAK1-AP1 positive feedback loop in Ewing sarcoma.
    Satterfield L, Shuck R, Kurenbekova L, Allen-Rhoades W, Edwards D, Huang S, Rajapakshe K, Coarfa C, Donehower LA, Yustein JT., Free PMC Article

    10/28/2017
    to complete invasion of the endothelium, staphylococci reorient recycling endocytic vesicles to recruit Cdc42GAP.

    Staphylococcus aureus recruits Cdc42GAP through recycling endosomes and the exocyst to invade human endothelial cells.
    Rauch L, Hennings K, Trasak C, Röder A, Schröder B, Koch-Nolte F, Rivera-Molina F, Toomre D, Aepfelbacher M., Free PMC Article

    08/5/2017
    we identified novel associations in WLS , ARHGAP1 , and 5' of MEF2C ( P- values < 8x10 - 5 ; false discovery rate (FDR) q-values < 0.01) that were much more strongly associated with BMD compared to the GWAS SNPs.

    Targeted sequencing of genome wide significant loci associated with bone mineral density (BMD) reveals significant novel and rare variants: the Cohorts for Heart and Aging Research in Genomic Epidemiology (CHARGE) targeted sequencing study.
    Hsu YH, Li G, Liu CT, Brody JA, Karasik D, Chou WC, Demissie S, Nandakumar K, Zhou Y, Cheng CH, Gill R, Gibbs RA, Muzny D, Santibanez J, Estrada K, Rivadeneira F, Harris T, Gudnason V, Uitterlinden A, Psaty BM, Robbins JA, Adrienne Cupples L, Kiel DP., Free PMC Article

    07/29/2017
    study shows that HMHA1 acts as a RhoGAP to regulate GTPase activity, cytoskeletal remodeling and cell spreading, which are crucial functions in normal hematopoietic and cancer cells

    The human minor histocompatibility antigen 1 is a RhoGAP.
    de Kreuk BJ, Schaefer A, Anthony EC, Tol S, Fernandez-Borja M, Geerts D, Pool J, Hambach L, Goulmy E, Hordijk PL., Free PMC Article

    07/19/2014
    The interaction of RhoGap protein stabilizes the tetrameric conformation of p53 and enhances its DNA-binding activity, thereby inducing cell-cycle arrest and apoptosis.

    RhoGAPs attenuate cell proliferation by direct interaction with p53 tetramerization domain.
    Xu J, Zhou X, Wang J, Li Z, Kong X, Qian J, Hu Y, Fang JY.

    12/21/2013
    In PC3 cells, ARHGAP21 presented GAP activity for RhoA and RhoC and induced changes in cell morphology. Moreover, its silencing altered the expression of genes involved in cell proliferation and cytoskeleton organization

    ARHGAP21 is a RhoGAP for RhoA and RhoC with a role in proliferation and migration of prostate adenocarcinoma cells.
    Lazarini M, Traina F, Machado-Neto JA, Barcellos KS, Moreira YB, Brandão MM, Verjovski-Almeida S, Ridley AJ, Saad ST.

    03/16/2013
    RhoGAP Stard13 temporally and spatially regulates Rho activity in the developing pancreas to ensure that morphogenesis and establishment of tissue architecture are coordinated with organ growth.

    Rho signalling restriction by the RhoGAP Stard13 integrates growth and morphogenesis in the pancreas.
    Petzold KM, Naumann H, Spagnoli FM.

    02/2/2013
    Observational study of gene-disease association. (HuGE Navigator)

    Mutation of ARHGAP9 in patients with coronary spastic angina.
    Takefuji M, Asano H, Mori K, Amano M, Kato K, Watanabe T, Morita Y, Katsumi A, Itoh T, Takenawa T, Hirashiki A, Izawa H, Nagata K, Hirayama H, Takatsu F, Naoe T, Yokota M, Kaibuchi K.

    01/20/2010
    CDC42GAP was identified as a counter-regulatory mediator for tubule formation.

    Differential gene expression analysis of tubule forming and non-tubule forming endothelial cells: CDC42GAP as a counter-regulator in tubule formation.
    Engelse MA, Laurens N, Verloop RE, Koolwijk P, van Hinsbergh VW.

    01/21/2010
    two potential interaction partners of Prx6: the calcium-activated cysteine endopeptidase calpain and the p50RhoGAP protein of the family of Sec14-like proteins.

    [Search for protein-protein interaction partners of peroxiredoxin 6 with the yeast two-hybrid system].
    Budanova EN, Bystrova MF.

    01/21/2010
    Mutation of three residues of CDC42GAP involved in specific interactions of CDC42GAP with switch domain residues of Cdc42, as well as individual mutations of each of these residues, yields GAPs that are defective in stimulating GTP hydrolysis.

    Understanding the catalytic mechanism of GTPase-activating proteins: demonstration of the importance of switch domain stabilization in the stimulation of GTP hydrolysis.
    Fidyk NJ, Cerione RA.

    01/21/2010
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