F-BAR proteins of the syndapin family shape the plasma membrane and are crucial for neuromorphogenesis
about
Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin IIVersatile membrane deformation potential of activated pacsinCooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular recycling endosome biogenesisProper synaptic vesicle formation and neuronal network activity critically rely on syndapin ILet's go bananas: revisiting the endocytic BAR codeCytoskeletal dynamics: a view from the membraneSyndapin--a membrane remodelling and endocytic F-BAR proteinSyndapin promotes pseudocleavage furrow formation by actin organization in the syncytial Drosophila embryo.Rho1- and Pkc1-dependent phosphorylation of the F-BAR protein Syp1 contributes to septin ring assembly.The Actin Nucleator Cobl Is Controlled by Calcium and CalmodulinMolecular basis for SH3 domain regulation of F-BAR-mediated membrane deformationPhosphorylation of syndapin I F-BAR domain at two helix-capping motifs regulates membrane tubulationPACSIN1, a Tau-interacting protein, regulates axonal elongation and branching by facilitating microtubule instabilityThe functions of the actin nucleator Cobl in cellular morphogenesis critically depend on syndapin ICoordinated autoinhibition of F-BAR domain membrane binding and WASp activation by Nervous Wreck.ProSAP1 and membrane nanodomain-associated syndapin I promote postsynapse formation and function.Syndapin 3 modulates fusion pore expansion in mouse neuroendocrine chromaffin cells.The proposed functions of membrane curvatures mediated by the BAR domain superfamily proteins.The F-BAR domains from srGAP1, srGAP2 and srGAP3 regulate membrane deformation differently.Drosophila F-BAR protein Syndapin contributes to coupling the plasma membrane and contractile ring in cytokinesis.Proteomic analysis of glycine receptor β subunit (GlyRβ)-interacting proteins: evidence for syndapin I regulating synaptic glycine receptors.The cytoplasmic protein Pacsin 2 in kidney development and injury repair.Identification of neuronal substrates implicates Pak5 in synaptic vesicle trafficking.The F-BAR domain of SRGP-1 facilitates cell-cell adhesion during C. elegans morphogenesisCasein kinase 2 phosphorylation of protein kinase C and casein kinase 2 substrate in neurons (PACSIN) 1 protein regulates neuronal spine formationTranscription factor Sp4 regulates expression of nervous wreck 2 to control NMDAR1 levels and dendrite patterning.Dynamin-2 regulates fusion pore expansion and quantal release through a mechanism that involves actin dynamics in neuroendocrine chromaffin cellsBAR proteins in cancer and blood disordersActivity-dependent fusion pore expansion regulated by a calcineurin-dependent dynamin-syndapin pathway in mouse adrenal chromaffin cells.FBAR syndapin 1 recognizes and stabilizes highly curved tubular membranes in a concentration dependent mannerThe actin cytoskeleton in presynaptic assembly.Syndapin/SDPN-1 is required for endocytic recycling and endosomal actin association in the C. elegans intestine.BAR domain competition during directional cellular migration.Barfly: sculpting membranes at the Drosophila neuromuscular junction.Membrane shaping by the Bin/amphiphysin/Rvs (BAR) domain protein superfamily.Lessons from yeast for clathrin-mediated endocytosis.Bridging membrane and cytoskeleton dynamics in the secretory and endocytic pathways.Dynamin-2 function and dysfunction along the secretory pathway.Dynamic shaping of cellular membranes by phospholipids and membrane-deforming proteins.Beyond the cytoskeleton: The emerging role of organelles and membrane remodeling in the regulation of axon collateral branches.
P2860
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P2860
F-BAR proteins of the syndapin family shape the plasma membrane and are crucial for neuromorphogenesis
description
2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2009
@ast
im Oktober 2009 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2009/10/21)
@sk
vědecký článek publikovaný v roce 2009
@cs
wetenschappelijk artikel (gepubliceerd op 2009/10/21)
@nl
наукова стаття, опублікована в жовтні 2009
@uk
مقالة علمية (نشرت في 21-10-2009)
@ar
name
F-BAR proteins of the syndapin ...... crucial for neuromorphogenesis
@ast
F-BAR proteins of the syndapin ...... crucial for neuromorphogenesis
@en
F-BAR proteins of the syndapin ...... crucial for neuromorphogenesis
@nl
type
label
F-BAR proteins of the syndapin ...... crucial for neuromorphogenesis
@ast
F-BAR proteins of the syndapin ...... crucial for neuromorphogenesis
@en
F-BAR proteins of the syndapin ...... crucial for neuromorphogenesis
@nl
prefLabel
F-BAR proteins of the syndapin ...... crucial for neuromorphogenesis
@ast
F-BAR proteins of the syndapin ...... crucial for neuromorphogenesis
@en
F-BAR proteins of the syndapin ...... crucial for neuromorphogenesis
@nl
P2093
P3181
P1476
F-BAR proteins of the syndapin ...... crucial for neuromorphogenesis
@en
P2093
Akvile Haeckel
Dennis Koch
Elavarasi Dharmalingam
Lukas Schwintzer
Michael Manfred Kessels
P304
13315-13327
P3181
P356
10.1523/JNEUROSCI.3973-09.2009
P407
P577
2009-10-01T00:00:00Z