ArticleTraffic (Copenhagen, Denmark)2014
Targeted disruption of an EH-domain protein endocytic complex, Pan1-End3.
Article in Traffic (Copenhagen, Denmark), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Recovery of plasma membrane tension after a hyperosmotic shock.Molecular biology of the cell · 2025Article
- Candida albicansMicrobiology spectrum · 2022Article
- Candida albicansmSphere · 2021Article
- The Role of Secretory Pathways inJournal of fungi (Basel, Switzerland) · 2020Review
- Plasma membrane tension regulates eisosome structure and function.Molecular biology of the cell · 2020Article
- A Targeted Mutation Identified through pKa Measurements Indicates a Postrecruitment Role for Fis1 in Yeast Mitochondrial Fission.The Journal of biological chemistry · 2016Article
- A Pan1/End3/Sla1 complex links Arp2/3-mediated actin assembly to sites of clathrin-mediated endocytosis.Molecular biology of the cell · 2015Article
- Pan1 regulates transitions between stages of clathrin-mediated endocytosis.Molecular biology of the cell · 2015Article
- Actin and endocytosis in budding yeast.Genetics · 2015Review
- Quantification of cytosolic interactions identifies Ede1 oligomers as key organizers of endocytosis.Molecular systems biology · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Pan1 is a multi-domain scaffold that enables dynamic interactions with both structural and regulatory components of the endocytic pathway. Pan1 is composed of Eps15 Homology (EH) domains which interact with adaptor proteins, a central region that is responsible for its oligomerization and C-terminal binding sites for Arp2/3, F-actin, and type-I myosin motors. In this study, we have characterized the binding sites between Pan1 and its constitutive binding partner End3, another EH domain containing endocytic protein. The C-terminal End3 Repeats of End3 associate with the N-terminal part of Pan1's central coiled-coil region. These repeats appear to act independently of one another as tandem, redundant binding sites for Pan1. The end3-1 allele was sequenced, and corresponds to a C-terminal truncation lacking the End3 Repeats. Mutations of the End3 Repeats highlight that those residues which are identical between these repeats serve as contact sites for the interaction with Pan1.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.