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dc.contributor.author
Aguilar, Ruben Claudio
dc.contributor.author
Longhi, Silvia Andrea
dc.contributor.author
Shaw, Jonathan D.
dc.contributor.author
Yeh, Lan Yu
dc.contributor.author
Kim, Sean
dc.contributor.author
Schön, Arne
dc.contributor.author
Freire, Ernesto
dc.contributor.author
Hsu, Ariel
dc.contributor.author
McCormick, William K.
dc.contributor.author
Watson, Hadiya A.
dc.contributor.author
Wendland, Beverly
dc.date.available
2019-07-19T18:56:58Z
dc.date.issued
2006-03
dc.identifier.citation
Aguilar, Ruben Claudio; Longhi, Silvia Andrea; Shaw, Jonathan D.; Yeh, Lan Yu; Kim, Sean; et al.; Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 103; 11; 3-2006; 4116-4121
dc.identifier.issn
0027-8424
dc.identifier.uri
http://hdl.handle.net/11336/79922
dc.description.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 ent1Δent2Δ 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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
National Academy of Sciences
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Actin
dc.subject
Endocytosis
dc.subject
Polarity
dc.subject.classification
Bioquímica y Biología Molecular
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Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-07-18T13:01:41Z
dc.journal.volume
103
dc.journal.number
11
dc.journal.pagination
4116-4121
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Washington
dc.description.fil
Fil: Aguilar, Ruben Claudio. Purdue University; Estados Unidos. University Johns Hopkins; Estados Unidos
dc.description.fil
Fil: Longhi, Silvia Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
dc.description.fil
Fil: Shaw, Jonathan D.. University Johns Hopkins; Estados Unidos
dc.description.fil
Fil: Yeh, Lan Yu. National Institutes of Health; Estados Unidos
dc.description.fil
Fil: Kim, Sean. University Johns Hopkins; Estados Unidos
dc.description.fil
Fil: Schön, Arne. University Johns Hopkins; Estados Unidos
dc.description.fil
Fil: Freire, Ernesto. National Institutes of Health; Estados Unidos
dc.description.fil
Fil: Hsu, Ariel. University Johns Hopkins; Estados Unidos
dc.description.fil
Fil: McCormick, William K.. University Johns Hopkins; Estados Unidos
dc.description.fil
Fil: Watson, Hadiya A.. University Johns Hopkins; Estados Unidos. National Instituto Of Child Health & Human Development; Estados Unidos
dc.description.fil
Fil: Wendland, Beverly. University Johns Hopkins; Estados Unidos
dc.journal.title
Proceedings of the National Academy of Sciences of The United States of America
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1073/pnas.0510513103
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/103/11/4116
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