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Article

Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis.

Molecular biology of the cell - 1 Aug 2007

Barker Sarah L, Lee Linda, Pierce B Daniel, Maldonado-Báez Lymarie, Drubin David G, Wendland Beverly

Abstract excerpt

The yeast endocytic scaffold Pan1 contains an uncharacterized proline-rich domain (PRD) at its carboxy (C)-terminus. We report that the pan1-20 temperature-sensitive allele has a disrupted PRD due to a frame-shift mutation in the open reading frame of the domain. To reveal redundantly masked functions of the PRD, synthetic genetic array screens with a pan1DeltaPRD strain found genetic interactions with alleles of...

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Identifiers

PMID: 17522383
DOI: 10.1091/mbc.e07-05-0436
PMCID: PMC1949359

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis.PMID 17522383Read ↗

Negative regulation of yeast Eps15-like Arp2/3 complex activator, Pan1p, by the Hip1R-related protein, Sla2p, during endocytosis.Semantic proximity Read ↗

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