The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module
about
Epsin 3 is a novel extracellular matrix-induced transcript specific to wounded epitheliaClathrin- and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteinsThe epsin family of endocytic adaptors promotes fibrosarcoma migration and invasionUbiquitylation of leptin receptor OB-Ra regulates its clathrin-mediated endocytosisA novel GTPase-activating protein for ARF6 directly interacts with clathrin and regulates clathrin-dependent endocytosis.The Phox homology (PX) domain, a new player in phosphoinositide signallingIdentification of a family of endocytic proteins that define a new alpha-adaptin ear-binding motifEpsinR: an ENTH domain-containing protein that interacts with AP-1.Gamma subunit of the AP-1 adaptor complex binds clathrin: implications for cooperative binding in coated vesicle assemblyEpsin 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 (PLZStonin 2: an adaptor-like protein that interacts with components of the endocytic machineryEnthoprotin: a novel clathrin-associated protein identified through subcellular proteomicsEpsinR: an AP1/clathrin interacting protein involved in vesicle traffickingStructure and ubiquitin binding of the ubiquitin-interacting motifPhosphatidic Acid Sequesters Sec18p from cis-SNARE Complexes to Inhibit PrimingPurification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p.Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sitesA role for epsin N-terminal homology/AP180 N-terminal homology (ENTH/ANTH) domains in tubulin bindingThe ENTH domainIdentification and characterization of a synaptojanin 2 splice isoform predominantly expressed in nerve terminalsThe epsin protein family: coordinators of endocytosis and signalingPhosphoproteomic analysis of the developing mouse brainEpsin Family of Endocytic Adaptor Proteins as Oncogenic Regulators of Cancer ProgressionDisruption of the endocytic protein HIP1 results in neurological deficits and decreased AMPA receptor traffickingSelective high-level expression of epsin 3 in gastric parietal cells, where it is localized at endocytic sites of apical canaliculiDisabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2Embryonic arrest at midgestation and disruption of Notch signaling produced by the absence of both epsin 1 and epsin 2 in miceUnusual structural organization of the endocytic proteins AP180 and epsin 1Association of Endophilin B1 with Cytoplasmic Vesicles.Intersectin 2, a new multimodular protein involved in clathrin-mediated endocytosis.Requirement for Golgi-localized PI(4)P in fusion of COPII vesicles with Golgi compartmentsEpsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus.The yeast endocytic protein Epsin 2 functions in a cell-division signaling pathway.Spatial Control of Epsin-induced Clathrin Assembly by Membrane CurvatureInteraction of Sla2p's ANTH domain with PtdIns(4,5)P2 is important for actin-dependent endocytic internalizationThe endocytic activity of the flagellar pocket in Trypanosoma brucei is regulated by an adjacent phosphatidylinositol phosphate kinase.A phosphotyrosine switch for cargo sequestration at clathrin-coated buds.The association of epsin with ubiquitinated cargo along the endocytic pathway is negatively regulated by its interaction with clathrin.A mammalian mirtron miR-1224 promotes tube-formation of human primary endothelial cells by targeting anti-angiogenic factor epsin2In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation.
P2860
Q24291242-9A94C43A-E19D-4FA2-A15A-169E9A8A8A64Q24291738-31A94FB2-0794-4284-9357-62206BB53CE1Q24295295-F79F7EAD-E6A5-44D3-8E10-9A76A69096D2Q24304963-B3D7C1A8-F13C-425C-BD34-8C1EC15046D3Q24521340-E3FA5C3B-13AB-4812-AA99-7866C3B85B82Q24533547-A8B28473-ABA9-4FC1-946B-2EE1E7359570Q24536065-3BA8A334-B2BE-424A-BC12-BF903E255BEEQ24550798-BA3AC48B-DE85-45BC-8413-5F6DF7053F4FQ24555711-2F47EBAA-82DA-4014-8EAF-90A04F7CA216Q24669673-6B55B372-B8D6-4D0A-876F-05540FA5A821Q24670373-36ED9516-8ACD-4474-A5F6-4FCBF7185A93Q24673739-8A5FA436-97C7-46F0-A8EF-17BED705843BQ24675918-44E8104B-E1F9-4EB9-9D0D-275D61C6367EQ27641265-E11B95F7-A286-4A9A-9AEE-F841DC5A2FC9Q27933545-C3F16DB2-D4FF-4597-B6AE-BF7B1D892399Q27935373-64DDF6C3-9F28-4F59-8835-DB30338AAF12Q28140776-A4E73AAA-908F-45E6-9847-8CFE1DA73CFBQ28204419-364A1E03-D59C-4B79-AC11-21301C3B508BQ28209625-1C995ADF-4CE7-4BD1-A176-7BB33AB68D9CQ28212156-8D4B7B16-2FE2-40D2-B6D5-434C58336925Q28274114-F1D789B7-BF67-4EC7-977A-71FFF85CFFDEQ28280338-55195210-810E-4726-9F23-271E24B9287FQ28307353-DE62C522-7C6B-4EF8-A0EE-AB7FEA5612E2Q28510810-E18D70F3-32EF-41B9-894E-001B80B778DFQ28511738-C053D396-D1B7-4A2C-A652-654806D113F8Q28511801-8CD5D11F-7929-4932-B9D2-2844485DDB17Q28586389-C8E8C655-7736-4674-8D1F-935CA5EC38F3Q28909703-7509DDAC-055F-4DB1-A1F4-55C32029754BQ30008877-E1FC1DF7-A973-4A86-AB66-FCE9693810EDQ30168860-6782A65D-C5EE-4D27-8858-0C0996401EBDQ30432882-2F8009E5-DB2B-47D5-9053-B6C74DB2DFD7Q30483002-C08B639E-2962-404B-9A65-1AF65E0744BEQ30488557-477201B1-CD55-4440-B813-B92253F15487Q30657973-E50512FA-9202-4E6D-8435-654BA917B4A5Q30854661-B71ECC2C-DDA2-4EEC-9043-197D62AACAA9Q33613389-624073AF-FA6A-4FB4-81E6-855BF268FE4BQ33792902-416C2617-52DD-499D-97E0-9D43959D803BQ33864158-EDB8E4F8-32DE-42A1-A9D8-B14696DBB486Q33912279-A6FF3464-D20E-4BD2-BFC9-C2DC1A0A76B2Q33948575-9D1088CF-A898-4F43-9E1B-89D75AF79E08
P2860
The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module
description
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1999
@ast
im November 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1999/11/26)
@sk
vědecký článek publikovaný v roce 1999
@cs
wetenschappelijk artikel (gepubliceerd op 1999/11/26)
@nl
наукова стаття, опублікована в листопаді 1999
@uk
name
The epsins define a family of ...... d contain a new protein module
@ast
The epsins define a family of ...... d contain a new protein module
@en
The epsins define a family of ...... d contain a new protein module
@nl
type
label
The epsins define a family of ...... d contain a new protein module
@ast
The epsins define a family of ...... d contain a new protein module
@en
The epsins define a family of ...... d contain a new protein module
@nl
prefLabel
The epsins define a family of ...... d contain a new protein module
@ast
The epsins define a family of ...... d contain a new protein module
@en
The epsins define a family of ...... d contain a new protein module
@nl
P2093
P2860
P356
P1476
The epsins define a family of ...... d contain a new protein module
@en
P2093
J A Rosenthal
L Pellegrini
P De Camilli
P P Di Fiore
V I Slepnev
P2860
P304
33959-33965
P356
10.1074/JBC.274.48.33959
P407
P577
1999-11-01T00:00:00Z