ArticleThe EMBO journal2010
Regulation of clathrin adaptor function in endocytosis: novel role for the SAM domain.
Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 44 citations in OpenAlex.
- Fully genetically encoded low-molecular-weight protein tags with defined shapes for direct molecular identification by cryo-electron tomography.bioRxiv : the preprint server for biology · 2026Article
- Competitive binding of actin and SH3 domains at proline-rich regions of Las17/WASP regulates actin polymerisation.Communications biology · 2025Article
- Mechanism of actin capping protein recruitment and turnover during clathrin-mediated endocytosis.The Journal of cell biology · 2024Article
- Review
- Hunting for Novel Routes in Anticancer Drug Discovery: Peptides against Sam-Sam Interactions.International journal of molecular sciences · 2022Review
- Syntaxin 12 and COMMD3 are new factors that function with VPS33B in the biogenesis of platelet α-granules.Blood · 2022Article
- The dynein light chain protein Tda2 functions as a dimerization engine to regulate actin capping protein during endocytosis.Molecular biology of the cell · 2021Article
- Cargo-mediated recruitment of the endocytic adaptor protein Sla1 inJournal of cell science · 2020Article
- Sterile α-motif domain requirement for cellular signaling and survival.The Journal of biological chemistry · 2020Article
- Mechanism of platelet α-granule biogenesis: study of cargo transport and the VPS33B-VPS16B complex in a model system.Blood advances · 2019Article
- Optimizing model representation for integrative structure determination of macromolecular assemblies.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Sla1 adaptor-clathrin interaction regulates coat formation and progression of endocytosis.Traffic (Copenhagen, Denmark) · 2018Article
- Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis.The Journal of cell biology · 2017Article
- Article
- A second Las17 monomeric actin-binding motif functions in Arp2/3-dependent actin polymerization during endocytosis.Traffic (Copenhagen, Denmark) · 2015Article
- Calcineurin regulates the yeast synaptojanin Inp53/Sjl3 during membrane stress.Molecular biology of the cell · 2015Article
- Actin and endocytosis in budding yeast.Genetics · 2015Review
- Article
- Characterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3.BMC structural biology · 2014Article
- Quantifying the dynamic interactions between a clathrin-coated pit and cargo molecules.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
During clathrin-mediated endocytosis, adaptor proteins play central roles in coordinating the assembly of clathrin coats and cargo selection. Here we characterize the binding of the yeast endocytic adaptor Sla1p to clathrin through a variant clathrin-binding motif that is negatively regulated by the Sla1p SHD2 domain. The crystal structure of SHD2 identifies the domain as a sterile alpha-motif (SAM) domain and shows a propensity to oligomerize. By co-immunoprecipitation, Sla1p binds to clathrin and self-associates in vivo. Mutations in the clathrin-binding motif that abolish clathrin binding and structure-based mutations in SHD2 that impede self-association result in endocytosis defects and altered dynamics of Sla1p assembly at the sites of endocytosis. These results define a novel mechanism for negative regulation of clathrin binding by an adaptor and suggest a role for SAM domains in clathrin-mediated endocytosis.
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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.