The interaction of epsin and Eps15 with the clathrin adaptor AP-2 is inhibited by mitotic phosphorylation and enhanced by stimulation-dependent dephosphorylation in nerve terminals
about
Eps15 homology domain-NPF motif interactions regulate clathrin coat assembly during synaptic vesicle recyclingAccumulation of rab4GTP in the cytoplasm and association with the peptidyl-prolyl isomerase pin1 during mitosisThe AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with a casein kinase Ialpha-like isoformEvolving nature of the AP2 alpha-appendage hub during clathrin-coated vesicle endocytosisRegulation of synaptojanin 1 by cyclin-dependent kinase 5 at synapsesUnlocking the mysteries of Na+-K+-ATPase endocytosis: phosphorylation is the keyEpsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZCrystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assemblyIdentification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosisTroyer syndrome protein spartin is mono-ubiquitinated and functions in EGF receptor traffickingThe conserved Pkh-Ypk kinase cascade is required for endocytosis in yeast.Epsins: adaptors in endocytosis?The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions.Amphiphysin 1 binds the cyclin-dependent kinase (cdk) 5 regulatory subunit p35 and is phosphorylated by cdk5 and cdc2A role for epsin N-terminal homology/AP180 N-terminal homology (ENTH/ANTH) domains in tubulin bindingRLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosisThe ENTH domainDual engagement regulation of protein interactions with the AP-2 adaptor alpha appendageThe epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein modulePhosphorylation of dynamin I on Ser-795 by protein kinase C blocks its association with phospholipids.Regulation of Hip1r by epsin controls the temporal and spatial coupling of actin filaments to clathrin-coated pitsCdc28-Cln3 phosphorylation of Sla1 regulates actin patch dynamics in different modes of fungal growthConvergent evolution with combinatorial peptides.The association of epsin with ubiquitinated cargo along the endocytic pathway is negatively regulated by its interaction with clathrin.Regulation of complex formation of POB1/epsin/adaptor protein complex 2 by mitotic phosphorylation.Regulation of AMPA receptor endocytosis by a signaling mechanism shared with LTD.In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation.Epsin deficiency impairs endocytosis by stalling the actin-dependent invagination of endocytic clathrin-coated pits.Endocytosis and signaling cascades: a close encounter.Rapid Ca2+-dependent decrease of protein ubiquitination at synapses.The endocytic adaptor Eps15 controls marginal zone B cell numbersNegative regulation of the endocytic adaptor disabled-2 (Dab2) in mitosis.Vesicular protein transport.Synaptophysin regulates clathrin-independent endocytosis of synaptic vesiclesCargo- and compartment-selective endocytic scaffold proteins.Clathrin-mediated endocytosis is inhibited during mitosisRegulation of the interaction between PIPKI gamma and talin by proline-directed protein kinases.G protein-coupled receptor/arrestin3 modulation of the endocytic machineryA requirement for epsin in mitotic membrane and spindle organization.Molecular Mechanisms for the Coupling of Endocytosis to Exocytosis in Neurons.
P2860
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P2860
The interaction of epsin and Eps15 with the clathrin adaptor AP-2 is inhibited by mitotic phosphorylation and enhanced by stimulation-dependent dephosphorylation in nerve terminals
description
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1999
@ast
im Februar 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1999/02/05)
@sk
vědecký článek publikovaný v roce 1999
@cs
wetenschappelijk artikel (gepubliceerd op 1999/02/05)
@nl
наукова стаття, опублікована в лютому 1999
@uk
name
The interaction of epsin and E ...... phorylation in nerve terminals
@ast
The interaction of epsin and E ...... phorylation in nerve terminals
@en
The interaction of epsin and E ...... phorylation in nerve terminals
@nl
type
label
The interaction of epsin and E ...... phorylation in nerve terminals
@ast
The interaction of epsin and E ...... phorylation in nerve terminals
@en
The interaction of epsin and E ...... phorylation in nerve terminals
@nl
prefLabel
The interaction of epsin and E ...... phorylation in nerve terminals
@ast
The interaction of epsin and E ...... phorylation in nerve terminals
@en
The interaction of epsin and E ...... phorylation in nerve terminals
@nl
P2093
P2860
P356
P1476
The interaction of epsin and E ...... phorylation in nerve terminals
@en
P2093
P. De Camilli
P. P. Di Fiore
V. I. Slepnev
P2860
P304
P356
10.1074/JBC.274.6.3257
P407
P577
1999-02-05T00:00:00Z