U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    FHOD1 formin homology 2 domain containing 1 [ Homo sapiens (human) ]

    Gene ID: 29109, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    FHOD1 is upregulated in glioma cells and attenuates ferroptosis of glioma cells by targeting HSPB1 signaling.

    FHOD1 is upregulated in glioma cells and attenuates ferroptosis of glioma cells by targeting HSPB1 signaling.
    Zhang F, Wu L, Feng S, Zhao Z, Zhang K, Thakur A, Xu Z, Liang Q, Liu Y, Liu W, Yan Y., Free PMC Article

    11/27/2023
    Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins.

    Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins.
    Lim SM, Cruz VE, Antoku S, Gundersen GG, Schwartz TU., Free PMC Article

    01/15/2022
    Multiple formin proteins participate in glioblastoma migration.

    Multiple formin proteins participate in glioblastoma migration.
    Heuser VD, Kiviniemi A, Lehtinen L, Munthe S, Kristensen BW, Posti JP, Sipilä JOT, Vuorinen V, Carpén O, Gardberg M., Free PMC Article

    02/6/2021
    FHOD1 plays a critical role in the spatial and temporal coordination of cellular stress fiber dynamics without disrupting the formation of stress fiber networks.

    Active FHOD1 promotes the formation of functional actin stress fibers.
    Shi X, Zhao S, Cai J, Wong G, Jiu Y.

    07/18/2020
    The functional integrity of lamin and nesprin-1 is thus required to modulate the FHOD1 activity and the inside-out mechanical coupling that tunes the cell internal stiffness to match that of its soft, physiological-like environment.

    Lamins and nesprin-1 mediate inside-out mechanical coupling in muscle cell precursors through FHOD1.
    Schwartz C, Fischer M, Mamchaoui K, Bigot A, Lok T, Verdier C, Duperray A, Michel R, Holt I, Voit T, Quijano-Roy S, Bonne G, Coirault C., Free PMC Article

    09/8/2018
    results suggest that FHOD1 participates in key cellular processes that are dysregulated in malignancy

    FHOD1 formin is upregulated in melanomas and modifies proliferation and tumor growth.
    Peippo M, Gardberg M, Lamminen T, Kaipio K, Carpén O, Heuser VD.

    06/3/2017
    FHOD1 and INF2 are novel regulators of inter- and intra-structural contractility of podosomes.

    The formins FHOD1 and INF2 regulate inter- and intra-structural contractility of podosomes.
    Panzer L, Trübe L, Klose M, Joosten B, Slotman J, Cambi A, Linder S.

    12/17/2016
    Immunostaining of sections of hearts with both anti-FHOD1 antibodies confirmed the presence of FHOD1 in intercalated discs and double immunostaining demonstrated its colocalisation with cadherin, plakoglobin and shifted localization to connexin43.

    Distribution of formins in cardiac muscle: FHOD1 is a component of intercalated discs and costameres.
    Al Haj A, Mazur AJ, Radaszkiewicz K, Radaszkiewicz T, Makowiecka A, Stopschinski BE, Schönichen A, Geyer M, Mannherz HG.

    08/29/2015
    Report FODH1 expression in cardiomyocytes and increased expression in dilated cardiommyopathy.

    The formin FHOD1 in cardiomyocytes.
    Dwyer J, Pluess M, Iskratsch T, Dos Remedios CG, Ehler E.

    04/25/2015
    FHOD1 promotes formation of short actin filaments and transiently associates with transverse arcs providing tight temporal and spatial control of the formation and turnover of transverse arcs into mature ventral stress fibers during dynamic cell behavior.

    FHOD1 regulates stress fiber organization by controlling the dynamics of transverse arcs and dorsal fibers.
    Schulze N, Graessl M, Blancke Soares A, Geyer M, Dehmelt L, Nalbant P.

    04/11/2015
    the diaphanous formin FHOD1 as an interaction partner of N2G

    FHOD1 interaction with nesprin-2G mediates TAN line formation and nuclear movement.
    Kutscheidt S, Zhu R, Antoku S, Luxton GW, Stagljar I, Fackler OT, Gundersen GG., Free PMC Article

    09/6/2014
    FHOD1 participates in cytoskeletal changes in epithelial-mesenchymal transition.

    FHOD1, a formin upregulated in epithelial-mesenchymal transition, participates in cancer cell migration and invasion.
    Gardberg M, Kaipio K, Lehtinen L, Mikkonen P, Heuser VD, Talvinen K, Iljin K, Kampf C, Uhlen M, Grénman R, Koivisto M, Carpén O., Free PMC Article

    08/9/2014
    Cdh1 contributes to spatiotemporal organization of AurB activity, and organization of FHOD1 activity by AurB contributes to daughter cell spreading after mitosis.

    Spatiotemporal organization of Aurora-B by APC/CCdh1 after mitosis coordinates cell spreading through FHOD1.
    Floyd S, Whiffin N, Gavilan MP, Kutscheidt S, De Luca M, Marcozzi C, Min M, Watkins J, Chung K, Fackler OT, Lindon C., Free PMC Article

    01/18/2014
    FHOD1 stabilizes actin filaments by protecting barbed ends from depolymerization with its dimeric FH2 domain, whereas the region N-terminal to the FH1 domain mediates F-actin bundling by simultaneously binding to the sides of adjacent F-actin filaments.

    FHOD1 is a combined actin filament capping and bundling factor that selectively associates with actin arcs and stress fibers.
    Schönichen A, Mannherz HG, Behrmann E, Mazur AJ, Kühn S, Silván U, Schoenenberger CA, Fackler OT, Raunser S, Dehmelt L, Geyer M.

    11/2/2013
    SIRPalpha/CD172a and FHOD1 are unique markers of littoral cells, a recently evolved major cell population of red pulp of human spleen.

    SIRPα/CD172a and FHOD1 are unique markers of littoral cells, a recently evolved major cell population of red pulp of human spleen.
    Ogembo JG, Milner DA Jr, Mansfield KG, Rodig SJ, Murphy GF, Kutok JL, Pinkus GS, Fingeroth JD., Free PMC Article

    06/16/2012
    FHOD1 and PPM1F (direct regulators of the actin cytoskeleton) were identified as novel targets of miR-200c. Expression levels of FHOD1 and PPM1F were inversely correlated with miR-200c level in breast cancer cell lines and breast cancer patient samples.

    MicroRNA-200c represses migration and invasion of breast cancer cells by targeting actin-regulatory proteins FHOD1 and PPM1F.
    Jurmeister S, Baumann M, Balwierz A, Keklikoglou I, Ward A, Uhlmann S, Zhang JD, Wiemann S, Sahin Ö., Free PMC Article

    03/17/2012
    Letter: G-protein coupled and ITAM receptor regulation of the formin FHOD1 through Rho kinase in platelets.

    G-protein coupled and ITAM receptor regulation of the formin FHOD1 through Rho kinase in platelets.
    Thomas SG, Calaminus SD, Machesky LM, Alberts AS, Watson SP.

    02/4/2012
    FHOD1 is a critical regulator of smooth muscle cell phenotype and is regulated by ROCK-dependent phosphorylation.

    Formin homology domain-containing protein 1 regulates smooth muscle cell phenotype.
    Staus DP, Blaker AL, Medlin MD, Taylor JM, Mack CP., Free PMC Article

    03/19/2011
    The Diaphanous-related Formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing.

    The Diaphanous-related Formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing.
    Hannemann S, Madrid R, Stastna J, Kitzing T, Gasteier J, Schönichen A, Bouchet J, Jimenez A, Geyer M, Grosse R, Benichou S, Fackler OT.

    01/21/2010
    Mutation of one residue in the predicted DAD-interaction surface efficiently activates FHOD1 in cells.

    The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation.
    Schulte A, Stolp B, Schönichen A, Pylypenko O, Rak A, Fackler OT, Geyer M.

    01/21/2010
    FHOD1 is activated through phosphorylation by rho-dependent protein kinase (ROCK)and has an important function in stress fibre formation in vascular endothelial cells

    The mammalian formin FHOD1 is activated through phosphorylation by ROCK and mediates thrombin-induced stress fibre formation in endothelial cells.
    Takeya R, Taniguchi K, Narumiya S, Sumimoto H., Free PMC Article

    01/21/2010
    In this study, the N-terminal region (residues 1-339) of the human formin homology domain-containing protein 1 (FHOD1) was purified and crystallized.

    Purification, crystallization and preliminary structural characterization of the N-terminal region of the human formin-homology protein FHOD1.
    Schulte A, Rak A, Pylypenko O, Ludwig D, Geyer M., Free PMC Article

    01/21/2010
    This study demonstrates FHOD1 is cleaved by caspase-3 at the SVPD(616) site during apoptosis and the C-terminal FHOD1 cleavage product has the ability to inhibit RNA polymerase I transcription.

    Caspase-3 cleaves the formin-homology-domain-containing protein FHOD1 during apoptosis to generate a C-terminal fragment that is targeted to the nucleolus.
    Ménard I, Gervais FG, Nicholson DW, Roy S.

    01/21/2010
    These novel data demonstrate that FHOD1-ERK MAP kinase interaction regulates key aspects of FHOD1 biology.

    The mammalian formin FHOD1 interacts with the ERK MAP kinase pathway.
    Boehm MB, Milius TJ, Zhou Y, Westendorf JJ, Koka S.

    01/21/2010
    Fhos directly binds to F-actin via the N-terminal region, forms a homotypic complex via the FH2 domain to organize actin cytoskeleton

    Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation.
    Takeya R, Sumimoto H.

    01/21/2010
    firstprevious page of 2 nextlast