Spatiotemporal phosphoregulation of Lgl: Finding meaning in multiple on/off buttons

Detalhes bibliográficos
Autor(a) principal: Moreira, S
Data de Publicação: 2016
Outros Autores: Morais-de-Sá, E
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10216/114510
Resumo: Intracellular asymmetries, often termed cell polarity, determine how cells organize and divide to ultimately control cell fate and shape animal tissues. The tumor suppressor Lethal giant larvae (Lgl) functions at the core of the evolutionarily conserved cell polarity machinery that controls apico-basal polarization. This function relies on its restricted basolateral localization via phosphorylation by aPKC. Here, we summarize the spatial and temporal control of Lgl during the cell cycle, highlighting two ideas that emerged from our recent findings: 1) Aurora A directly phosphorylates Lgl during symmetric division to couple reorganization of epithelial polarity with the cell cycle; 2) Phosphorylation of Lgl within three conserved serines controls its localization and function in a site-specific manner. Considering the importance of phosphorylation to regulate the concentration of Lgl at the plasma membrane, we will further discuss how it may work as an on-off switch for the interaction with cortical binding partners, with implications on epithelial polarization and spindle orientation.
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spelling Spatiotemporal phosphoregulation of Lgl: Finding meaning in multiple on/off buttonsAnimalsAurora Kinase A/metabolismCell DivisionDrosophila Proteins/metabolismProtein Kinase C/metabolismSpindle Apparatus/physiologyTumor Suppressor Proteins/metabolismIntracellular asymmetries, often termed cell polarity, determine how cells organize and divide to ultimately control cell fate and shape animal tissues. The tumor suppressor Lethal giant larvae (Lgl) functions at the core of the evolutionarily conserved cell polarity machinery that controls apico-basal polarization. This function relies on its restricted basolateral localization via phosphorylation by aPKC. Here, we summarize the spatial and temporal control of Lgl during the cell cycle, highlighting two ideas that emerged from our recent findings: 1) Aurora A directly phosphorylates Lgl during symmetric division to couple reorganization of epithelial polarity with the cell cycle; 2) Phosphorylation of Lgl within three conserved serines controls its localization and function in a site-specific manner. Considering the importance of phosphorylation to regulate the concentration of Lgl at the plasma membrane, we will further discuss how it may work as an on-off switch for the interaction with cortical binding partners, with implications on epithelial polarization and spindle orientation.Taylor & Francis20162016-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10216/114510eng1949-099210.1080/19490992.2016.1149290Moreira, SMorais-de-Sá, Einfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-29T15:29:23Zoai:repositorio-aberto.up.pt:10216/114510Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T00:24:48.758667Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Spatiotemporal phosphoregulation of Lgl: Finding meaning in multiple on/off buttons
title Spatiotemporal phosphoregulation of Lgl: Finding meaning in multiple on/off buttons
spellingShingle Spatiotemporal phosphoregulation of Lgl: Finding meaning in multiple on/off buttons
Moreira, S
Animals
Aurora Kinase A/metabolism
Cell Division
Drosophila Proteins/metabolism
Protein Kinase C/metabolism
Spindle Apparatus/physiology
Tumor Suppressor Proteins/metabolism
title_short Spatiotemporal phosphoregulation of Lgl: Finding meaning in multiple on/off buttons
title_full Spatiotemporal phosphoregulation of Lgl: Finding meaning in multiple on/off buttons
title_fullStr Spatiotemporal phosphoregulation of Lgl: Finding meaning in multiple on/off buttons
title_full_unstemmed Spatiotemporal phosphoregulation of Lgl: Finding meaning in multiple on/off buttons
title_sort Spatiotemporal phosphoregulation of Lgl: Finding meaning in multiple on/off buttons
author Moreira, S
author_facet Moreira, S
Morais-de-Sá, E
author_role author
author2 Morais-de-Sá, E
author2_role author
dc.contributor.author.fl_str_mv Moreira, S
Morais-de-Sá, E
dc.subject.por.fl_str_mv Animals
Aurora Kinase A/metabolism
Cell Division
Drosophila Proteins/metabolism
Protein Kinase C/metabolism
Spindle Apparatus/physiology
Tumor Suppressor Proteins/metabolism
topic Animals
Aurora Kinase A/metabolism
Cell Division
Drosophila Proteins/metabolism
Protein Kinase C/metabolism
Spindle Apparatus/physiology
Tumor Suppressor Proteins/metabolism
description Intracellular asymmetries, often termed cell polarity, determine how cells organize and divide to ultimately control cell fate and shape animal tissues. The tumor suppressor Lethal giant larvae (Lgl) functions at the core of the evolutionarily conserved cell polarity machinery that controls apico-basal polarization. This function relies on its restricted basolateral localization via phosphorylation by aPKC. Here, we summarize the spatial and temporal control of Lgl during the cell cycle, highlighting two ideas that emerged from our recent findings: 1) Aurora A directly phosphorylates Lgl during symmetric division to couple reorganization of epithelial polarity with the cell cycle; 2) Phosphorylation of Lgl within three conserved serines controls its localization and function in a site-specific manner. Considering the importance of phosphorylation to regulate the concentration of Lgl at the plasma membrane, we will further discuss how it may work as an on-off switch for the interaction with cortical binding partners, with implications on epithelial polarization and spindle orientation.
publishDate 2016
dc.date.none.fl_str_mv 2016
2016-01-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10216/114510
url http://hdl.handle.net/10216/114510
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1949-0992
10.1080/19490992.2016.1149290
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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