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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/242793
Ver los metadatos del registro completo
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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 |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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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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score |
13.22299 |