Eps15 is constitutively oligomerized due to homophilic interaction of its coiled-coil region.
about
The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15.Molecular cloning and characterization of MT-ACT48, a novel mitochondrial acyl-CoA thioesteraseA novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTPase Rab5Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificityCharacterization of the EFC/F-BAR domain protein, FCHO2Stonin 2: an adaptor-like protein that interacts with components of the endocytic machineryAP-2/Eps15 interaction is required for receptor-mediated endocytosisPan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosisHrs-2 regulates receptor-mediated endocytosis via interactions with Eps15Association of insulin-like growth factor 1 receptor with EHD1 and SNAP29An Eps homology (EH) domain protein that binds to the Ral-GTPase target, RalBP1Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)Intersectin (ITSN) family of scaffolds function as molecular hubs in protein interaction networksEps15R is a tyrosine kinase substrate with characteristics of a docking protein possibly involved in coated pits-mediated internalizationCharacterization of EHD4, an EH domain-containing protein expressed in the extracellular matrix.Differential nucleocytoplasmic trafficking between the related endocytic proteins Eps15 and Eps15R.Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain.UIM domain-dependent recruitment of the endocytic adaptor protein Eps15 to ubiquitin-enriched endosomes.Parallel dimers and anti-parallel tetramers formed by epidermal growth factor receptor pathway substrate clone 15.EH and UIM: endocytosis and more.Eps15 mediates vesicle trafficking from the trans-Golgi network via an interaction with the clathrin adaptor AP-1.The endocytic adaptor proteins of pathogenic fungi: charting new and familiar pathways.An endosomally localized isoform of Eps15 interacts with Hrs to mediate degradation of epidermal growth factor receptor.Evolutionary Changes on the Way to Clathrin-Mediated Endocytosis in Animals.A ubiquitin-interacting motif (UIM) is essential for Eps15 and Eps15R ubiquitination.Assembly of clathrin coats disrupts the association between Eps15 and AP-2 adaptors.Synaptic Vesicle Endocytosis
P2860
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P2860
Eps15 is constitutively oligomerized due to homophilic interaction of its coiled-coil region.
description
1997 nî lūn-bûn
@nan
1997 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Eps15 is constitutively oligom ...... ion of its coiled-coil region.
@ast
Eps15 is constitutively oligom ...... ion of its coiled-coil region.
@en
type
label
Eps15 is constitutively oligom ...... ion of its coiled-coil region.
@ast
Eps15 is constitutively oligom ...... ion of its coiled-coil region.
@en
prefLabel
Eps15 is constitutively oligom ...... ion of its coiled-coil region.
@ast
Eps15 is constitutively oligom ...... ion of its coiled-coil region.
@en
P2093
P2860
P356
P1476
Eps15 is constitutively oligom ...... ion of its coiled-coil region.
@en
P2093
Confalonieri S
Di Fiore PP
P2860
P304
15413-15418
P356
10.1074/JBC.272.24.15413
P407
P577
1997-06-01T00:00:00Z