ArticleProceedings of the National Academy of Sciences of the United States of America2006
Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed, 116 citations in OpenAlex.
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- Septin organization is regulated by the Gpa1 ubiquitination domain and endocytic machinery during the yeast pheromone response.Molecular biology of the cell · 2025Article
- Subtleties in Clathrin heavy chain binding boxes provide selectivity among adaptor proteins of budding yeast.Nature communications · 2024Article
- Actin- and microtubule-based motors contribute to clathrin-independent endocytosis in yeast.Molecular biology of the cell · 2023Article
- Article
- Chaperone-Dependent Degradation of Cdc42 Promotes Cell Polarity and Shields the Protein from Aggregation.Molecular and cellular biology · 2023Article
- Regulation of Cdc42 protein turnover modulates the filamentous growth MAPK pathway.The Journal of cell biology · 2022Article
- Genome doubling enabled the expansion of yeast vesicle traffic pathways.Scientific reports · 2022Article
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- Gene Signatures Induced by Ionizing Radiation as Prognostic Tools in an In Vitro Experimental Breast Cancer Model.Cancers · 2021Review
- Eng2, a new player involved in feedback loop regulation of Cdc42 activity in fission yeast.Scientific reports · 2021Article
- Essential role of the endocytic site-associated protein Ecm25 in stress-induced cell elongation.Cell reports · 2021Article
- Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis.Nature communications · 2021Article
- Crystal Structure of the Epo1-Bem3 Complex for Bud Growth.International journal of molecular sciences · 2021Article
- Epsins in vascular development, function and disease.Cellular and molecular life sciences : CMLS · 2021Review
- Complimentary action of structured and unstructured domains of epsin supports clathrin-mediated endocytosis at high tension.Communications biology · 2020Article
- Murine Epsins Play an Integral Role in Podocyte Function.Journal of the American Society of Nephrology : JASN · 2020Article
- Review
- Endocytic Adaptor Proteins in Health and Disease: Lessons from Model Organisms and Human Mutations.Cells · 2019Review
9 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
Epsins are endocytic proteins with a structured epsin N-terminal homology (ENTH) domain that binds phosphoinositides and a poorly structured C-terminal region that interacts with ubiquitin and endocytic machinery, including clathrin and endocytic scaffolding proteins. Yeast has two redundant genes encoding epsins, ENT1 and ENT2; deleting both genes is lethal. We demonstrate that the ENTH domain is both necessary and sufficient for viability of ent1Deltaent2Delta cells. Mutational analysis of the ENTH domain revealed a surface patch that is essential for viability and that binds guanine nucleotide triphosphatase-activating proteins for Cdc42, a critical regulator of cell polarity in all eukaryotes. Furthermore, the epsins contribute to regulation of specific Cdc42 signaling pathways in yeast cells. These data support a model in which the epsins function as spatial and temporal coordinators of endocytosis and cell polarity.
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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.