Regulation of AP-3 function by inositides. Identification of phosphatidylinositol 3,4,5-trisphosphate as a potent ligand
about
Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated trafficUNC-11, a Caenorhabditis elegans AP180 homologue, regulates the size and protein composition of synaptic vesiclesIdentification of a novel domain shared by putative components of the endocytic and cytoskeletal machineryPan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosisCalmodulin controls organization of the actin cytoskeleton via regulation of phosphatidylinositol (4,5)-bisphosphate synthesis in Saccharomyces cerevisiaeThe dual phosphatase activity of synaptojanin1 is required for both efficient synaptic vesicle endocytosis and reavailability at nerve terminalsCasein kinase I associates with members of the centaurin-alpha family of phosphatidylinositol 3,4,5-trisphosphate-binding proteinsSynaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysinDevelopmentally regulated alternative splicing in a novel synaptojaninSpecific binding of phosphatidylinositol 4,5-bisphosphate to calcium-dependent activator protein for secretion (CAPS), a potential phosphoinositide effector protein for regulated exocytosisClathrin assembly protein AP180 and CALM differentially control axogenesis and dendrite outgrowth in embryonic hippocampal neuronsPhosphatidylinositol 4-kinase type IIalpha is responsible for the phosphatidylinositol 4-kinase activity associated with synaptic vesiclesAP180 and AP-2 interact directly in a complex that cooperatively assembles clathrinLoss of endocytic clathrin-coated pits upon acute depletion of phosphatidylinositol 4,5-bisphosphate.Clathrin assembly proteins AP180 and CALM in the embryonic rat brain.The inositol 5-phosphatase SHIP2 regulates endocytic clathrin-coated pit dynamicsLipid metabolism and regulation of membrane trafficking.Protein-lipid interactions and phosphoinositide metabolism in membrane traffic: insights from vesicle recycling in nerve terminalsskittles, a Drosophila phosphatidylinositol 4-phosphate 5-kinase, is required for cell viability, germline development and bristle morphology, but not for neurotransmitter releaseThe monomeric clathrin assembly protein, AP180, regulates contractile vacuole size in Dictyostelium discoideumPI-loting membrane traffic.Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits.Mutations in synaptojanin disrupt synaptic vesicle recycling.Diphosphoinositol polyphosphates: what are the mechanisms?A role for an Hsp70 nucleotide exchange factor in the regulation of synaptic vesicle endocytosis.Diphosphoinositol polyphosphates: metabolic messengers?Dynamic interactions between clathrin and locally structured elements in a disordered protein mediate clathrin lattice assemblyU-73122 reduces the cell growth in cultured MG-63 ostesarcoma cell line involving Phosphoinositide-specific Phospholipases C.Picornaviruses.Overexpression of OSBP-related protein 2 (ORP2) induces changes in cellular cholesterol metabolism and enhances endocytosis.Arrestin function in G protein-coupled receptor endocytosis requires phosphoinositide binding.Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling.Phosphorylation of a synaptic vesicle-associated protein by an inositol hexakisphosphate-regulated protein kinase.Membrane bending by protein-protein crowding.Effects of wortmannin and latrunculin A on slow endocytosis at the frog neuromuscular junction.Lipid products of phosphoinositide 3-kinase interact with Rac1 GTPase and stimulate GDP dissociation.Structural and membrane binding analysis of the Phox homology domain of phosphoinositide 3-kinase-C2alpha.
P2860
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P2860
Regulation of AP-3 function by inositides. Identification of phosphatidylinositol 3,4,5-trisphosphate as a potent ligand
description
1997 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի մարտին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1997
@ast
im März 1997 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1997/03/07)
@sk
vědecký článek publikovaný v roce 1997
@cs
wetenschappelijk artikel (gepubliceerd op 1997/03/07)
@nl
наукова стаття, опублікована в березні 1997
@uk
name
Regulation of AP-3 function by ...... isphosphate as a potent ligand
@ast
Regulation of AP-3 function by ...... isphosphate as a potent ligand
@en
Regulation of AP-3 function by ...... isphosphate as a potent ligand
@nl
type
label
Regulation of AP-3 function by ...... isphosphate as a potent ligand
@ast
Regulation of AP-3 function by ...... isphosphate as a potent ligand
@en
Regulation of AP-3 function by ...... isphosphate as a potent ligand
@nl
prefLabel
Regulation of AP-3 function by ...... isphosphate as a potent ligand
@ast
Regulation of AP-3 function by ...... isphosphate as a potent ligand
@en
Regulation of AP-3 function by ...... isphosphate as a potent ligand
@nl
P2093
P2860
P356
P1476
Regulation of AP-3 function by ...... isphosphate as a potent ligand
@en
P2093
E. M. Lafer
G. D. Prestwich
J. R. Falck
K. K. Reddy
S. B. Shears
P2860
P304
P356
10.1074/JBC.272.10.6393
P407
P577
1997-03-07T00:00:00Z