Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins

Autores
Aguilar, Ruben Claudio; Longhi, Silvia Andrea; Shaw, Jonathan D.; Yeh, Lan Yu; Kim, Sean; Schön, Arne; Freire, Ernesto; Hsu, Ariel; McCormick, William K.; Watson, Hadiya A.; Wendland, Beverly
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Aguilar, Ruben Claudio. Purdue University; Estados Unidos. University Johns Hopkins; Estados Unidos
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
Fil: Shaw, Jonathan D.. University Johns Hopkins; Estados Unidos
Fil: Yeh, Lan Yu. National Institutes of Health; Estados Unidos
Fil: Kim, Sean. University Johns Hopkins; Estados Unidos
Fil: Schön, Arne. University Johns Hopkins; Estados Unidos
Fil: Freire, Ernesto. National Institutes of Health; Estados Unidos
Fil: Hsu, Ariel. University Johns Hopkins; Estados Unidos
Fil: McCormick, William K.. University Johns Hopkins; Estados Unidos
Fil: Watson, Hadiya A.. University Johns Hopkins; Estados Unidos. National Instituto Of Child Health & Human Development; Estados Unidos
Fil: Wendland, Beverly. University Johns Hopkins; Estados Unidos
Materia
Actin
Endocytosis
Polarity
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/79922
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/79922
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteinsAguilar, Ruben ClaudioLonghi, Silvia AndreaShaw, Jonathan D.Yeh, Lan YuKim, SeanSchön, ArneFreire, ErnestoHsu, ArielMcCormick, William K.Watson, Hadiya A.Wendland, BeverlyActinEndocytosisPolarityhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Epsins 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.Fil: Aguilar, Ruben Claudio. Purdue University; Estados Unidos. University Johns Hopkins; Estados UnidosFil: Longhi, Silvia Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Shaw, Jonathan D.. University Johns Hopkins; Estados UnidosFil: Yeh, Lan Yu. National Institutes of Health; Estados UnidosFil: Kim, Sean. University Johns Hopkins; Estados UnidosFil: Schön, Arne. University Johns Hopkins; Estados UnidosFil: Freire, Ernesto. National Institutes of Health; Estados UnidosFil: Hsu, Ariel. University Johns Hopkins; Estados UnidosFil: McCormick, William K.. University Johns Hopkins; Estados UnidosFil: Watson, Hadiya A.. University Johns Hopkins; Estados Unidos. National Instituto Of Child Health & Human Development; Estados UnidosFil: Wendland, Beverly. University Johns Hopkins; Estados UnidosNational Academy of Sciences2006-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/79922Aguilar, 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; 4116-41210027-8424CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.0510513103info:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/103/11/4116info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:52:43Zoai:ri.conicet.gov.ar:11336/79922instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:52:43.483CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins
title Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins
spellingShingle Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins
Aguilar, Ruben Claudio
Actin
Endocytosis
Polarity
title_short Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins
title_full Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins
title_fullStr Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins
title_full_unstemmed Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins
title_sort Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins
dc.creator.none.fl_str_mv Aguilar, Ruben Claudio
Longhi, Silvia Andrea
Shaw, Jonathan D.
Yeh, Lan Yu
Kim, Sean
Schön, Arne
Freire, Ernesto
Hsu, Ariel
McCormick, William K.
Watson, Hadiya A.
Wendland, Beverly
author Aguilar, Ruben Claudio
author_facet Aguilar, Ruben Claudio
Longhi, Silvia Andrea
Shaw, Jonathan D.
Yeh, Lan Yu
Kim, Sean
Schön, Arne
Freire, Ernesto
Hsu, Ariel
McCormick, William K.
Watson, Hadiya A.
Wendland, Beverly
author_role author
author2 Longhi, Silvia Andrea
Shaw, Jonathan D.
Yeh, Lan Yu
Kim, Sean
Schön, Arne
Freire, Ernesto
Hsu, Ariel
McCormick, William K.
Watson, Hadiya A.
Wendland, Beverly
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Actin
Endocytosis
Polarity
topic Actin
Endocytosis
Polarity
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
Fil: Aguilar, Ruben Claudio. Purdue University; Estados Unidos. University Johns Hopkins; Estados Unidos
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
Fil: Shaw, Jonathan D.. University Johns Hopkins; Estados Unidos
Fil: Yeh, Lan Yu. National Institutes of Health; Estados Unidos
Fil: Kim, Sean. University Johns Hopkins; Estados Unidos
Fil: Schön, Arne. University Johns Hopkins; Estados Unidos
Fil: Freire, Ernesto. National Institutes of Health; Estados Unidos
Fil: Hsu, Ariel. University Johns Hopkins; Estados Unidos
Fil: McCormick, William K.. University Johns Hopkins; Estados Unidos
Fil: Watson, Hadiya A.. University Johns Hopkins; Estados Unidos. National Instituto Of Child Health & Human Development; Estados Unidos
Fil: Wendland, Beverly. University Johns Hopkins; Estados Unidos
description 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.
publishDate 2006
dc.date.none.fl_str_mv 2006-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/79922
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
0027-8424
CONICET Digital
CONICET
url http://hdl.handle.net/11336/79922
identifier_str_mv 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
0027-8424
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.0510513103
info:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/103/11/4116
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv National Academy of Sciences
publisher.none.fl_str_mv National Academy of Sciences
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844613615463694336
score 13.069144

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