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    ARL2BP ARF like GTPase 2 binding protein [ Homo sapiens (human) ]

    Gene ID: 23568, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    ARL3 activation requires the co-GEF BART and effector-mediated turnover.

    ARL3 activation requires the co-GEF BART and effector-mediated turnover.
    ElMaghloob Y, Sot B, McIlwraith MJ, Garcia E, Yelland T, Ismail S., Free PMC Article

    01/29/2022
    Epstein-Barr Virus miR-BART1-3p Regulates the miR-17-92 Cluster by Targeting E2F3.

    Epstein-Barr Virus miR-BART1-3p Regulates the miR-17-92 Cluster by Targeting E2F3.
    Park MC, Kim H, Choi H, Chang MS, Lee SK., Free PMC Article

    12/18/2021
    Study identified multiple ciliopathy phenotypes associated with mutations in ARL2BP in human patients and in a mouse knockout model. Spermiogenesis is impaired, resulting in abnormally shaped heads, shortened and mis-assembled sperm tails, and loss of axonemal doublets. ARL2BP is required for the structural maintenance of cilia as well as of the sperm flagellum, and that its deficiency leads to syndromic ciliopathy.

    Mutations in ARL2BP, a protein required for ciliary microtubule structure, cause syndromic male infertility in humans and mice.
    Moye AR, Bedoni N, Cunningham JG, Sanzhaeva U, Tucker ES, Mathers P, Peter VG, Quinodoz M, Paris LP, Coutinho-Santos L, Camacho P, Purcell MG, Winkelmann AC, Foster JA, Pugacheva EN, Rivolta C, Ramamurthy V., Free PMC Article

    01/11/2020
    This study identified two homozygous variants in ARL2BP as a rare cause of autosomal recessive retinitis pigmentosa. Further studies are required to define the underlying disease mechanism causing retinal degeneration as a result of mutations in ARL2BP and any phenotype-genotype correlation associated with residual levels of the wild-type transcript.

    Novel homozygous splicing mutations in ARL2BP cause autosomal recessive retinitis pigmentosa.
    Fiorentino A, Yu J, Arno G, Pontikos N, Halford S, Broadgate S, Michaelides M, Carss KJ, Raymond FL, Cheetham ME, Webster AR, Downes SM, Hardcastle AJ, NIHR-BioResource Rare Diseases Consortium, U.K. Inherited Retinal Dystrophy Consortium., Free PMC Article

    11/17/2018
    Subsequent analysis of 844 index cases did not reveal further pathogenic chances in ARL2BP indicating that mutations in ARL2B are a rare cause of arRCD (about 0.1%) in a large cohort of French patients.

    ARL2BP mutations account for 0.1% of autosomal recessive rod-cone dystrophies with the report of a novel splice variant.
    Audo I, El Shamieh S, Méjécase C, Michiels C, Demontant V, Antonio A, Condroyer C, Boyard F, Letexier M, Saraiva JP, Blanchard S, Mohand-Saïd S, Sahel JA, Zeitz C.

    03/17/2018
    Alteration of EBV encoded miR-BART1 expression results in an increase in migration and invasion of nasopharyngeal carcinoma in vitro and causes metastasis in vivo. EBV-miR-BART1 directly targets the cellular tumour suppressor PTEN.

    Epstein-Barr virus-encoded microRNA BART1 induces tumour metastasis by regulating PTEN-dependent pathways in nasopharyngeal carcinoma.
    Cai L, Ye Y, Jiang Q, Chen Y, Lyu X, Li J, Wang S, Liu T, Cai H, Yao K, Li JL, Li X., Free PMC Article

    04/16/2016
    EBV also downregulates two immediate early genes by miR-BART20-5p.

    MicroRNA miR-BART20-5p stabilizes Epstein-Barr virus latency by directly targeting BZLF1 and BRLF1.
    Jung YJ, Choi H, Kim H, Lee SK., Free PMC Article

    09/27/2014
    Mutations in ARL2BP cause autosomal-recessive retinitis pigmentosa.

    Mutations in ARL2BP, encoding ADP-ribosylation-factor-like 2 binding protein, cause autosomal-recessive retinitis pigmentosa.
    Davidson AE, Schwarz N, Zelinger L, Stern-Schneider G, Shoemark A, Spitzbarth B, Gross M, Laxer U, Sosna J, Sergouniotis PI, Waseem NH, Wilson R, Kahn RA, Plagnol V, Wolfrum U, Banin E, Hardcastle AJ, Cheetham ME, Sharon D, Webster AR., Free PMC Article

    12/21/2013
    EBV-miR-BART1 could influence the expression of metabolism-associated genes and might be involved in cancer metabolism in nasopharyngeal carcinoma

    EBV-miR-BART1 is involved in regulating metabolism-associated genes in nasopharyngeal carcinoma.
    Ye Y, Zhou Y, Zhang L, Chen Y, Lyu X, Cai L, Lu Y, Deng Y, Wang J, Yao K, Fang W, Cai H, Li X.

    08/31/2013
    Our results imply that BART regulates actin-cytoskeleton rearrangements at membrane ruffles through modulation of the activity of Rac1, which, in turn, inhibits pancreatic cancer cell invasion.

    BART inhibits pancreatic cancer cell invasion by Rac1 inactivation through direct binding to active Rac1.
    Taniuchi K, Yokotani K, Saibara T., Free PMC Article

    11/17/2012
    These results imply that BART contributes to regulating PKCalpha activity through binding to ANX7, thereby affecting the invasiveness of pancreatic cancer cells.

    BART inhibits pancreatic cancer cell invasion by PKCα inactivation through binding to ANX7.
    Taniuchi K, Yokotani K, Saibara T., Free PMC Article

    08/4/2012
    We identify a subset of BART miRNAs that are restricted to Latency III in normal infection but are up regulated in tumors that express Latency I and II.

    A novel persistence associated EBV miRNA expression profile is disrupted in neoplasia.
    Qiu J, Cosmopoulos K, Pegtel M, Hopmans E, Murray P, Middeldorp J, Shapiro M, Thorley-Lawson DA., Free PMC Article

    01/21/2012
    Our results imply that BART increases active RhoA by inhibiting ARL2 function, which in turn inhibits invasiveness of cancer cells.

    BART inhibits pancreatic cancer cell invasion by inhibiting ARL2-mediated RhoA inactivation.
    Taniuchi K, Iwasaki S, Saibara T.

    01/14/2012
    overexpression of the amino (N)-terminal region of G3BP, including the binding region for BART mRNA, dominant-negatively inhibits formation of the complex between endogenous G3BP and BART mRNA, and increases the expression of BART.

    The N-terminal domain of G3BP enhances cell motility and invasion by posttranscriptional regulation of BART.
    Taniuchi K, Nishimori I, Hollingsworth MA.

    11/19/2011
    Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition and binding mode of small GTPase with effector.

    Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition and binding mode of small GTPase with effector.
    Zhang T, Li S, Zhang Y, Zhong C, Lai Z, Ding J.

    01/21/2010
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