Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins
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- Rubén C. Aguilar
- Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
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- Silvia A. Longhi
- Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
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- Jonathan D. Shaw
- Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
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- Lan-Yu Yeh
- Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
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- Sean Kim
- Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
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- Arne Schön
- Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
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- Ernesto Freire
- Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
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- Ariel Hsu
- Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
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- William K. McCormick
- Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
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- Hadiya A. Watson
- Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
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- Beverly Wendland
- Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
Abstract
<jats:p> 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, <jats:italic>ENT1</jats:italic> and <jats:italic>ENT2</jats:italic> ; deleting both genes is lethal. We demonstrate that the ENTH domain is both necessary and sufficient for viability of <jats:italic>ent1</jats:italic> Δ <jats:italic>ent2</jats:italic> Δ 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. </jats:p>
Journal
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 103 (11), 4116-4121, 2006-03-06
Proceedings of the National Academy of Sciences
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Keywords
Details 詳細情報について
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- CRID
- 1360011146639863424
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- ISSN
- 10916490
- 00278424
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- Data Source
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- Crossref