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    Rph3a rabphilin 3A [ Rattus norvegicus (Norway rat) ]

    Gene ID: 171039, updated on 9-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Rabphilin 3A binds the N-peptide of SNAP-25 to promote SNARE complex assembly in exocytosis.

    Rabphilin 3A binds the N-peptide of SNAP-25 to promote SNARE complex assembly in exocytosis.
    Li T, Cheng Q, Wang S, Ma C., Free PMC Article

    10/8/2022
    Rabphilin-3A Drives Structural Modifications of Dendritic Spines Induced by Long-Term Potentiation.

    Rabphilin-3A Drives Structural Modifications of Dendritic Spines Induced by Long-Term Potentiation.
    Franchini L, Stanic J, Barzasi M, Zianni E, Mauceri D, Diluca M, Gardoni F., Free PMC Article

    06/11/2022
    Findings indicate that Rph3A activity is linked to the aberrant synaptic localization of GluN2A-expressing NMDARs characterizing levodopa-induced dyskinesias; suggest that Rph3A/GluN2A complex could represent an innovative therapeutic target for those pathological conditions where NMDAR composition is significantly altered.

    Rabphilin 3A: A novel target for the treatment of levodopa-induced dyskinesias.
    Stanic J, Mellone M, Napolitano F, Racca C, Zianni E, Minocci D, Ghiglieri V, Thiolat ML, Li Q, Longhi A, De Rosa A, Picconi B, Bezard E, Calabresi P, Di Luca M, Usiello A, Gardoni F.

    07/28/2018
    Rph3A interacts with GluN2A and PSD-95 forming a complex that regulates NMDARs stabilization at postsynaptic membranes.

    Rabphilin 3A retains NMDA receptors at synaptic sites through interaction with GluN2A/PSD-95 complex.
    Stanic J, Carta M, Eberini I, Pelucchi S, Marcello E, Genazzani AA, Racca C, Mulle C, Di Luca M, Gardoni F., Free PMC Article

    05/21/2016
    Binding of rabphilin to SNAP-25 regulates exocytosis of synaptic vesicles after the readily releasable pool has either been physiologically exhausted by use-dependent depression, or has been artificially depleted by deletion of synaptobrevin.

    Rabphilin regulates SNARE-dependent re-priming of synaptic vesicles for fusion.
    Deák F, Shin OH, Tang J, Hanson P, Ubach J, Jahn R, Rizo J, Kavalali ET, Südhof TC., Free PMC Article

    01/21/2010
    Interactions of SNAP25A and RPH3A take place at cell surface during stimulated exocytosis.

    In-depth fluorescence lifetime imaging analysis revealing SNAP25A-Rabphilin 3A interactions.
    Lee JD, Huang PC, Lin YC, Kao LS, Huang CC, Kao FJ, Lin CC, Yang DM.

    01/21/2010
    Structural determinants for Ca2+ and phosphatidylinositol 4,5-bisphosphate binding by the C2A domain of rabphilin-3A.

    Structural determinants for Ca2+ and phosphatidylinositol 4,5-bisphosphate binding by the C2A domain of rabphilin-3A.
    Coudevylle N, Montaville P, Leonov A, Zweckstetter M, Becker S.

    01/21/2010
    different PIP2 headgroup recognition modes suggest that PIP2 is a target of the C2A domain of rabphilin-3A while this phospholipid is an effector of the C2B domain

    The PIP2 binding mode of the C2 domains of rabphilin-3A.
    Montaville P, Coudevylle N, Radhakrishnan A, Leonov A, Zweckstetter M, Becker S., Free PMC Article

    01/21/2010
    Three Rab3/27 effectors, Granuphilin, Noc2, and Rabphilin, in PC12 cells using fluorescence recovery after photobleaching of EGFP-tagged proteins.

    The Rab27 effector Rabphilin, unlike Granuphilin and Noc2, rapidly exchanges between secretory granules and cytosol in PC12 cells.
    Handley MT, Burgoyne RD.

    01/21/2010
    rabphilin, by interacting with alpha-actinin, organizes the cell cytoskeleton to facilitate granule localization within F-actin-rich regions

    Rabphilin localizes with the cell actin cytoskeleton and stimulates association of granules with F-actin cross-linked by {alpha}-actinin.
    Baldini G, Martelli AM, Tabellini G, Horn C, Machaca K, Narducci P, Baldini G.

    01/21/2010
    Rabphilin and Noc2 are recruited to dense-core vesicles through specific interaction with Rab27A in rat cells

    Rabphilin and Noc2 are recruited to dense-core vesicles through specific interaction with Rab27A in PC12 cells.
    Fukuda M, Kanno E, Yamamoto A.

    01/21/2010
    These results indicate that the polybasic sequence in the rabphilin C2B domain functions as an effector domain for SNAP-25 and controls the number of 'releasable' vesicles docked to the plasma membrane.

    The polybasic sequence in the C2B domain of rabphilin is required for the vesicle docking step in PC12 cells.
    Tsuboi T, Kanno E, Fukuda M.

    01/21/2010
    The crystal structure of the Ca2+-free C2A domain adopts the classical C2-domain fold consisting of an eight-stranded antiparallel beta-sandwich with type I topology, and contains conserved acidic residues responsible for calcium binding.

    Structure of the C2A domain of rabphilin-3A.
    Biadene M, Montaville P, Sheldrick GM, Becker S.

    01/21/2010
    Rabphilin-3A and Rab3A are present in normal mouse, rat, and human kidneys, with an exclusively glomerular expression and a comma-like pattern of positivity along the glomerular capillary wall, suggestive for podocyte staining.

    Glomerular podocytes possess the synaptic vesicle molecule Rab3A and its specific effector rabphilin-3a.
    Rastaldi MP, Armelloni S, Berra S, Li M, Pesaresi M, Poczewski H, Langer B, Kerjaschki D, Henger A, Blattner SM, Kretzler M, Wanke R, D'Amico G., Free PMC Article

    01/21/2010
    the rabphilin C2B domain interacts directly with the N-terminus of annexin A4 and mediates the co-complexing of these two proteins which co-localise at the plasma membrane annexin; A4 may play a role in synaptic exocytosis.

    Identification of a novel protein complex containing annexin A4, rabphilin and synaptotagmin.
    Willshaw A, Grant K, Yan J, Rockliffe N, Ambavarapu S, Burdyga G, Varro A, Fukuoka S, Gawler D.

    01/21/2010
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