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Article

Inhibition of clathrin-coated pit assembly by an Eps15 mutant.

Journal of cell science - 1 May 1999

Benmerah A, Bayrou M, Cerf-Bensussan N, Dautry-Varsat A

Abstract excerpt

Recent data have shown that Eps15, a newly identified component of clathrin-coated pits constitutively associated with the AP-2 complex, is required for receptor-mediated endocytosis. However, its precise function remains unknown. Interestingly, Eps15 contains three EH (Eps15-Homology) domains al...

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Source

Identifiers

PMID: 10194409
DOI: 10.1242/jcs.112.9.1303

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-10194409-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

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Inhibition of clathrin-coated pit assembly by an Eps15 mutant.PMID 10194409Read ↗

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A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15.Semantic proximity Read ↗

Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis.Semantic proximity Read ↗

The Eps15 C. elegans homologue EHS-1 is implicated in synaptic vesicle recycling.Semantic proximity Read ↗

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The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein ModuleSemantic proximity Read ↗

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