Eps15 homology domain-NPF motif interactions regulate clathrin coat assembly during synaptic vesicle recycling (Q24305171)

GOA release 2020-03-11

clathrin coat assembly

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GOA release 2020-03-11

author name string

Jennifer R Morgan

1

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Kondury Prasad

2

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Suping Jin

3

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George J Augustine

4

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Eileen M Lafer

Journal of Biological Chemistry

5

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language of work or name

English

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publication date

29 August 2003

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published in

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volume

278

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issue

35

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page(s)

33583-92

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cites work

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Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain

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Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis

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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

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Curvature of clathrin-coated pits driven by epsin

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Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module

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The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps 15 protein

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The tyrosine kinase substrate eps15 is constitutively associated with the plasma membrane adaptor AP-2

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Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly

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A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain

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The Eps15 C. elegans homologue EHS-1 is implicated in synaptic vesicle recycling.

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Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits

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AP-2/Eps15 interaction is required for receptor-mediated endocytosis

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Uncoating of clathrin-coated vesicles in presynaptic terminals: roles for Hsc70 and auxilin

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A functional role for GTP-binding proteins in synaptic vesicle cycling.

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Assembly polypeptides from coated vesicles mediate reassembly of unique clathrin coats

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Assembly of clathrin coats disrupts the association between Eps15 and AP-2 adaptors

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Bacterially expressed F1‐20/AP‐3 assembles clathrin into cages with a narrow size distribution: Implications for the regulation of quantal size during neurotransmission

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Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic

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AP180 and AP-2 interact directly in a complex that cooperatively assembles clathrin

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Solution structure of the Reps1 EH domain and characterization of its binding to NPF target sequences

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Endocytosis: EH domains lend a hand

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Unusual structural organization of the endocytic proteins AP180 and epsin 1

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Essential role of phosphoinositide metabolism in synaptic vesicle recycling

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EHSH1/intersectin, a protein that contains EH and SH3 domains and binds to dynamin and SNAP-25. A protein connection between exocytosis and endocytosis?

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Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery

21 January 2018

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Yeast Eps15-like endocytic protein, Pan1p, activates the Arp2/3 complex

21 January 2018

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Molecular characterization of the AP180 coated vesicle assembly protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304346200

A role for the clathrin assembly domain of AP180 in synaptic vesicle endocytosis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304346200

inferred from DOI database lookup

7 January 2021

based on heuristic

A conserved clathrin assembly motif essential for synaptic vesicle endocytosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304346200