The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathway

Autores
Mukherjee, Debarati; Coon, Brian G,; Edwards III, Daniel F.; Hanna, Claudia B.; Longhi, Silvia Andrea; McCaffery J. M.; Wendland, Beverly; Retegui, Lilia Alicia; Bi, Erfei; Aguilar, R. C.
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The epsins are a family of adaptors involved in recruiting other endocytic proteins, binding of ubiquitylated cargo and induction of membrane curvature. These molecules bear a characteristic epsin N-terminal homology (ENTH) domain and multiple peptide motifs that mediate protein-protein interactions. We have previously demonstrated that the ENTH domain of epsin is involved in Cdc42 signaling regulation. Here, we present evidence that yeast epsin 2 (Ent2) plays a signaling role during cell division. We observed that overexpression of the ENTH domain of Ent2 (ENTH2), but not Ent1, promoted the formation of chains of cells and aberrant septa. This dominant-negative effect resulted from ENTH2-mediated interference with septin assembly pathways. We mapped the ENTH2 determinants responsible for induction of the phenotype and found them to be important for efficient binding to the septin regulatory protein, Bem3. Supporting a physiological role for epsin 2 in cell division, the protein localized to sites of polarized growth and cytokinesis and rescued a defect in cell division induced by Bem3 misregulation. Collectively, our findings provide a potential molecular mechanism linking endocytosis (via epsin 2) with signaling pathways regulating cell division.
Fil: Mukherjee, Debarati. Purdue University; Estados Unidos
Fil: Coon, Brian G,. Purdue University; Estados Unidos
Fil: Edwards III, Daniel F.. Purdue University; Estados Unidos
Fil: Hanna, Claudia B.. Purdue University; 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. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica.; Argentina
Fil: McCaffery J. M.. University Johns Hopkins; Estados Unidos
Fil: Wendland, Beverly. University Johns Hopkins; Estados Unidos
Fil: Retegui, Lilia Alicia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica.; Argentina
Fil: Bi, Erfei. University of Pennsylvania; Estados Unidos
Fil: Aguilar, R. C.. Purdue University; Estados Unidos
Materia
CELL DIVISION
EPSIN
SEPTIN
ENDOCYTOSIS
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:11336/242793

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network_name_str CONICET Digital (CONICET)
spelling The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathwayMukherjee, DebaratiCoon, Brian G,Edwards III, Daniel F.Hanna, Claudia B.Longhi, Silvia AndreaMcCaffery J. M.Wendland, BeverlyRetegui, Lilia AliciaBi, ErfeiAguilar, R. C.CELL DIVISIONEPSINSEPTINENDOCYTOSIShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The epsins are a family of adaptors involved in recruiting other endocytic proteins, binding of ubiquitylated cargo and induction of membrane curvature. These molecules bear a characteristic epsin N-terminal homology (ENTH) domain and multiple peptide motifs that mediate protein-protein interactions. We have previously demonstrated that the ENTH domain of epsin is involved in Cdc42 signaling regulation. Here, we present evidence that yeast epsin 2 (Ent2) plays a signaling role during cell division. We observed that overexpression of the ENTH domain of Ent2 (ENTH2), but not Ent1, promoted the formation of chains of cells and aberrant septa. This dominant-negative effect resulted from ENTH2-mediated interference with septin assembly pathways. We mapped the ENTH2 determinants responsible for induction of the phenotype and found them to be important for efficient binding to the septin regulatory protein, Bem3. Supporting a physiological role for epsin 2 in cell division, the protein localized to sites of polarized growth and cytokinesis and rescued a defect in cell division induced by Bem3 misregulation. Collectively, our findings provide a potential molecular mechanism linking endocytosis (via epsin 2) with signaling pathways regulating cell division.Fil: Mukherjee, Debarati. Purdue University; Estados UnidosFil: Coon, Brian G,. Purdue University; Estados UnidosFil: Edwards III, Daniel F.. Purdue University; Estados UnidosFil: Hanna, Claudia B.. Purdue University; 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"; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica.; ArgentinaFil: McCaffery J. M.. University Johns Hopkins; Estados UnidosFil: Wendland, Beverly. University Johns Hopkins; Estados UnidosFil: Retegui, Lilia Alicia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica.; ArgentinaFil: Bi, Erfei. University of Pennsylvania; Estados UnidosFil: Aguilar, R. C.. Purdue University; Estados UnidosCompany of Biologists2009-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/242793Mukherjee, Debarati; Coon, Brian G,; Edwards III, Daniel F.; Hanna, Claudia B.; Longhi, Silvia Andrea; et al.; The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathway; Company of Biologists; Journal of Cell Science; 122; 15; 1-8-2009; 2453-24630021-9533CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://journals.biologists.com/jcs/search-results?f_AllAuthors=Daniel+F.+Edwardsinfo:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.057349info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:22:57Zoai:ri.conicet.gov.ar:11336/242793instacron: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:34982025-10-15 15:22:58.068CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathway
title The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathway
spellingShingle The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathway
Mukherjee, Debarati
CELL DIVISION
EPSIN
SEPTIN
ENDOCYTOSIS
title_short The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathway
title_full The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathway
title_fullStr The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathway
title_full_unstemmed The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathway
title_sort The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathway
dc.creator.none.fl_str_mv Mukherjee, Debarati
Coon, Brian G,
Edwards III, Daniel F.
Hanna, Claudia B.
Longhi, Silvia Andrea
McCaffery J. M.
Wendland, Beverly
Retegui, Lilia Alicia
Bi, Erfei
Aguilar, R. C.
author Mukherjee, Debarati
author_facet Mukherjee, Debarati
Coon, Brian G,
Edwards III, Daniel F.
Hanna, Claudia B.
Longhi, Silvia Andrea
McCaffery J. M.
Wendland, Beverly
Retegui, Lilia Alicia
Bi, Erfei
Aguilar, R. C.
author_role author
author2 Coon, Brian G,
Edwards III, Daniel F.
Hanna, Claudia B.
Longhi, Silvia Andrea
McCaffery J. M.
Wendland, Beverly
Retegui, Lilia Alicia
Bi, Erfei
Aguilar, R. C.
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv CELL DIVISION
EPSIN
SEPTIN
ENDOCYTOSIS
topic CELL DIVISION
EPSIN
SEPTIN
ENDOCYTOSIS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The epsins are a family of adaptors involved in recruiting other endocytic proteins, binding of ubiquitylated cargo and induction of membrane curvature. These molecules bear a characteristic epsin N-terminal homology (ENTH) domain and multiple peptide motifs that mediate protein-protein interactions. We have previously demonstrated that the ENTH domain of epsin is involved in Cdc42 signaling regulation. Here, we present evidence that yeast epsin 2 (Ent2) plays a signaling role during cell division. We observed that overexpression of the ENTH domain of Ent2 (ENTH2), but not Ent1, promoted the formation of chains of cells and aberrant septa. This dominant-negative effect resulted from ENTH2-mediated interference with septin assembly pathways. We mapped the ENTH2 determinants responsible for induction of the phenotype and found them to be important for efficient binding to the septin regulatory protein, Bem3. Supporting a physiological role for epsin 2 in cell division, the protein localized to sites of polarized growth and cytokinesis and rescued a defect in cell division induced by Bem3 misregulation. Collectively, our findings provide a potential molecular mechanism linking endocytosis (via epsin 2) with signaling pathways regulating cell division.
Fil: Mukherjee, Debarati. Purdue University; Estados Unidos
Fil: Coon, Brian G,. Purdue University; Estados Unidos
Fil: Edwards III, Daniel F.. Purdue University; Estados Unidos
Fil: Hanna, Claudia B.. Purdue University; 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. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica.; Argentina
Fil: McCaffery J. M.. University Johns Hopkins; Estados Unidos
Fil: Wendland, Beverly. University Johns Hopkins; Estados Unidos
Fil: Retegui, Lilia Alicia. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica.; Argentina
Fil: Bi, Erfei. University of Pennsylvania; Estados Unidos
Fil: Aguilar, R. C.. Purdue University; Estados Unidos
description The epsins are a family of adaptors involved in recruiting other endocytic proteins, binding of ubiquitylated cargo and induction of membrane curvature. These molecules bear a characteristic epsin N-terminal homology (ENTH) domain and multiple peptide motifs that mediate protein-protein interactions. We have previously demonstrated that the ENTH domain of epsin is involved in Cdc42 signaling regulation. Here, we present evidence that yeast epsin 2 (Ent2) plays a signaling role during cell division. We observed that overexpression of the ENTH domain of Ent2 (ENTH2), but not Ent1, promoted the formation of chains of cells and aberrant septa. This dominant-negative effect resulted from ENTH2-mediated interference with septin assembly pathways. We mapped the ENTH2 determinants responsible for induction of the phenotype and found them to be important for efficient binding to the septin regulatory protein, Bem3. Supporting a physiological role for epsin 2 in cell division, the protein localized to sites of polarized growth and cytokinesis and rescued a defect in cell division induced by Bem3 misregulation. Collectively, our findings provide a potential molecular mechanism linking endocytosis (via epsin 2) with signaling pathways regulating cell division.
publishDate 2009
dc.date.none.fl_str_mv 2009-08-01
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/11336/242793
Mukherjee, Debarati; Coon, Brian G,; Edwards III, Daniel F.; Hanna, Claudia B.; Longhi, Silvia Andrea; et al.; The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathway; Company of Biologists; Journal of Cell Science; 122; 15; 1-8-2009; 2453-2463
0021-9533
CONICET Digital
CONICET
url http://hdl.handle.net/11336/242793
identifier_str_mv Mukherjee, Debarati; Coon, Brian G,; Edwards III, Daniel F.; Hanna, Claudia B.; Longhi, Silvia Andrea; et al.; The yeast endocytic protein Epsin-2 (Ent2) functions in a conserved cell division signaling pathway; Company of Biologists; Journal of Cell Science; 122; 15; 1-8-2009; 2453-2463
0021-9533
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://journals.biologists.com/jcs/search-results?f_AllAuthors=Daniel+F.+Edwards
info:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.057349
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
application/pdf
dc.publisher.none.fl_str_mv Company of Biologists
publisher.none.fl_str_mv Company of Biologists
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
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