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    RAPH1 Ras association (RalGDS/AF-6) and pleckstrin homology domains 1 [ Homo sapiens (human) ]

    Gene ID: 65059, updated on 6-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Nuclear isoform of RAPH1 interacts with FOXQ1 to promote aggressiveness and radioresistance in breast cancer.

    Nuclear isoform of RAPH1 interacts with FOXQ1 to promote aggressiveness and radioresistance in breast cancer.
    Liu Q, Cao Y, Wei X, Dong H, Cui M, Guan S, Liu B, Wang X, Xing P., Free PMC Article

    01/8/2024
    High RAPH1 expression is correlated with aggressive breast cancer phenotypes and provides independent prognostic value in invasive breast cancer.

    Clinicopathological and prognostic significance of Ras association and pleckstrin homology domains 1 (RAPH1) in breast cancer.
    Kurozumi S, Joseph C, Sonbul S, Aleskandarany MA, Pigera M, Alsaleem M, Alsaeed S, Kariri Y, Nolan CC, Diez-Rodriguez M, Johnston S, Mongan NP, Fujii T, Shirabe K, Martin SG, Ellis IO, Green AR, Rakha EA.

    01/12/2019
    The human RAPH1 gene is the CHE2 locus.

    Association between RAPH1 Gene Haplotypes and CHE2 Locus Phenotypes.
    A De Andrade F, Batistela MS, Amaral Sda C, Dos Santos W, Mikami LR, Chautard-Freire-Maia EA, Furtado-Alle L, Souza RL.

    05/27/2017
    these studies demonstrate an insight into how the Lpd-PH domain regulates cellular signals in a PI(3,4)P2 dependent manner.

    Mechanistic insights into the phosphatidylinositol binding properties of the pleckstrin homology domain of lamellipodin.
    Gorai S, Paul D, Haloi N, Borah R, Santra MK, Manna D.

    12/17/2016
    Disruption of the RIAM/lamellipodin-integrin-talin complex markedly impairs cell migration.

    A RIAM/lamellipodin-talin-integrin complex forms the tip of sticky fingers that guide cell migration.
    Lagarrigue F, Vikas Anekal P, Lee HS, Bachir AI, Ablack JN, Horwitz AF, Ginsberg MH., Free PMC Article

    06/28/2016
    The authors propose that Lpd delivers Ena/VASP proteins to growing barbed ends and increases their actin polymerase activity by tethering them to actin filaments.

    Lamellipodin promotes actin assembly by clustering Ena/VASP proteins and tethering them to actin filaments.
    Hansen SD, Mullins RD., Free PMC Article

    05/14/2016
    These data indicate a possible role for Lpd in the actin-based movement and the cell-to-cell spread of L. monocytogenes.

    Lamellipodin Is Important for Cell-to-Cell Spread and Actin-Based Motility in Listeria monocytogenes.
    Wang J, King JE, Goldrick M, Lowe M, Gertler FB, Roberts IS., Free PMC Article

    11/7/2015
    The results suggest that although the RAPH1 gene was deleted or amplified in all samples, the Lpd does not seem to play a major role in tumorigenesis of mammary carcinomas.

    Amplification and deletion of the RAPH1 gene in breast cancer patients.
    Batistela MS, Boberg DR, Andrade FA, Pecharki M, de S F Ribeiro EM, Cavalli IJ, Lima RS, Urban CA, Furtado-Alle L, Souza RL.

    07/5/2014
    this study suggests a novel mechanism in which Lpd mediates EGFR endocytosis via Mena downstream of endophilin.

    Endophilin, Lamellipodin, and Mena cooperate to regulate F-actin-dependent EGF-receptor endocytosis.
    Vehlow A, Soong D, Vizcay-Barrena G, Bodo C, Law AL, Perera U, Krause M., Free PMC Article

    12/21/2013
    The crystal structure of Lpd cc-RA-PH presents a molecular model of Lpd enhances actin polymerization by oligomerization via two intermolecular contact sites.

    Crystal structure of Lamellipodin implicates diverse functions in actin polymerization and Ras signaling.
    Chang YC, Zhang H, Brennan ML, Wu J., Free PMC Article

    09/7/2013
    results of this study suggested that that PI(3,4)P2, Lpd, and Ena/VASP are involved in the process movement of multipolar migrating cells.

    A phosphatidylinositol lipids system, lamellipodin, and Ena/VASP regulate dynamic morphology of multipolar migrating cells in the developing cerebral cortex.
    Yoshinaga S, Ohkubo T, Sasaki S, Nuriya M, Ogawa Y, Yasui M, Tabata H, Nakajima K., Free PMC Article

    11/24/2012
    Nephrin ligation resulted in abnormal morphology of actin tails in human podocytes when Ship2, Filamin or Lamellipodin were individually knocked down.

    Nephrin regulates lamellipodia formation by assembling a protein complex that includes Ship2, filamin and lamellipodin.
    Venkatareddy M, Cook L, Abuarquob K, Verma R, Garg P., Free PMC Article

    09/1/2012
    Data show that profilin1 negatively regulates lamellipodin targeting to the leading edge; profilin1 depletion increases lamellipodin concentration at the lamellipodial tip (where it binds Ena/VASP), and this mediates the hypermotility.

    Profilin1 regulates PI(3,4)P2 and lamellipodin accumulation at the leading edge thus influencing motility of MDA-MB-231 cells.
    Bae YH, Ding Z, Das T, Wells A, Gertler F, Roy P., Free PMC Article

    05/14/2011
    Consistently, in HeLa cells, lamellipodin was required for EGF-induced proliferation.

    Drosophila pico and its mammalian ortholog lamellipodin activate serum response factor and promote cell proliferation.
    Lyulcheva E, Taylor E, Michael M, Vehlow A, Tan S, Fletcher A, Krause M, Bennett D., Free PMC Article

    01/21/2010
    proline-rich peptides organize the 4 subunits of BChE into a 340 kDa tetramer, by interacting with the C-terminal BChE tetramerization domain

    Lamellipodin proline rich peptides associated with native plasma butyrylcholinesterase tetramers.
    Li H, Schopfer LM, Masson P, Lockridge O.

    01/21/2010
    RMO1 is expressed and deleted in osteosarcoma

    Altered expression and deletion of RMO1 in osteosarcoma.
    Eppert K, Wunder JS, Aneliunas V, Tsui LC, Scherer SW, Andrulis IL.

    01/21/2010
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