A Conserved LIR Motif in Connexins Mediates Ubiquitin-Independent Binding to LC3/GABARAP Proteins

Detalhes bibliográficos
Autor(a) principal: Catarino, Steve
Data de Publicação: 2020
Outros Autores: Ribeiro-Rodrigues, Teresa M, Sá Ferreira, Rita, Ramalho, José, Abert, Christine, Martens, Sascha, Girão, Henrique
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/96174
Resumo: This research was supported by the European Regional Development Fund (ERDF) through the Operational Program for Competitiveness Factors (COMPETE) [under the projects PAC “NETDIAMOND” POCI-01-0145-FEDER-016385; HealthyAging2020 CENTRO-01-0145-FEDER-000012-N2323; POCI-01-0145-FEDER-007440, CENTRO-01-0145-FEDER-032179, CENTRO-01-0145-FEDER-032414,FCTUID/NEU/04539/2013 and ID/NEU/04539/2019]. This research is based upon work from COST Action (PROTEOSTASIS BM1307), supported by COST (European Cooperation in Science and Technology).S.C. was supported by Action BM1307 – 39607 from COST Action PROTEOSTASIS BM1307, T.M.R.-R. was supported by PD/BD/52294/2013 from Fundação para a Ciência e a Tecnologia (FCT). C.A. was supported by a DOC Fellowship of the Austrian Academy of Sciences.
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spelling A Conserved LIR Motif in Connexins Mediates Ubiquitin-Independent Binding to LC3/GABARAP ProteinsThis research was supported by the European Regional Development Fund (ERDF) through the Operational Program for Competitiveness Factors (COMPETE) [under the projects PAC “NETDIAMOND” POCI-01-0145-FEDER-016385; HealthyAging2020 CENTRO-01-0145-FEDER-000012-N2323; POCI-01-0145-FEDER-007440, CENTRO-01-0145-FEDER-032179, CENTRO-01-0145-FEDER-032414,FCTUID/NEU/04539/2013 and ID/NEU/04539/2019]. This research is based upon work from COST Action (PROTEOSTASIS BM1307), supported by COST (European Cooperation in Science and Technology).S.C. was supported by Action BM1307 – 39607 from COST Action PROTEOSTASIS BM1307, T.M.R.-R. was supported by PD/BD/52294/2013 from Fundação para a Ciência e a Tecnologia (FCT). C.A. was supported by a DOC Fellowship of the Austrian Academy of Sciences.Gap junctions (GJ) are specialized cell-cell contacts formed by connexins (Cxs), which provide direct communication between adjacent cells. Cx43 ubiquitination has been suggested to induce the internalization of GJs, as well as the recruitment of the autophagy receptor p62 to mediate binding to LC3B and degradation by macroautophagy. In this report, we describe a functional LC3 interacting region (LIR), present in the amino terminal of most Cx protein family members, which can mediate the autophagy degradation of Cx43 without the need of ubiquitin. Mutation of the LIR motif on Cx37, Cx43, Cx46 and Cx50 impairs interaction with LC3B and GABARAP without compromising protein ubiquitination. Through in vitro protein-protein interaction assays, we demonstrate that this LIR motif is required for the binding of Cx43 to LC3B and GABARAP. Overall, our findings describe an alternative mechanism whereby Cxs interact with LC3/GABARAP proteins, envisioning a new model for the autophagy degradation of connexins.Centro de Estudos de Doenças Crónicas (CEDOC)NOVA Medical School|Faculdade de Ciências Médicas (NMS|FCM)RUNCatarino, SteveRibeiro-Rodrigues, Teresa MSá Ferreira, RitaRamalho, JoséAbert, ChristineMartens, SaschaGirão, Henrique2020-04-14T22:35:26Z2020-04-072020-04-07T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/96174eng2073-4409PURE: 17746275https://doi.org/10.3390/cells9040902info: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:RCAAP2024-03-11T04:43:53Zoai:run.unl.pt:10362/96174Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:38:29.806311Repositório 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 A Conserved LIR Motif in Connexins Mediates Ubiquitin-Independent Binding to LC3/GABARAP Proteins
title A Conserved LIR Motif in Connexins Mediates Ubiquitin-Independent Binding to LC3/GABARAP Proteins
spellingShingle A Conserved LIR Motif in Connexins Mediates Ubiquitin-Independent Binding to LC3/GABARAP Proteins
Catarino, Steve
title_short A Conserved LIR Motif in Connexins Mediates Ubiquitin-Independent Binding to LC3/GABARAP Proteins
title_full A Conserved LIR Motif in Connexins Mediates Ubiquitin-Independent Binding to LC3/GABARAP Proteins
title_fullStr A Conserved LIR Motif in Connexins Mediates Ubiquitin-Independent Binding to LC3/GABARAP Proteins
title_full_unstemmed A Conserved LIR Motif in Connexins Mediates Ubiquitin-Independent Binding to LC3/GABARAP Proteins
title_sort A Conserved LIR Motif in Connexins Mediates Ubiquitin-Independent Binding to LC3/GABARAP Proteins
author Catarino, Steve
author_facet Catarino, Steve
Ribeiro-Rodrigues, Teresa M
Sá Ferreira, Rita
Ramalho, José
Abert, Christine
Martens, Sascha
Girão, Henrique
author_role author
author2 Ribeiro-Rodrigues, Teresa M
Sá Ferreira, Rita
Ramalho, José
Abert, Christine
Martens, Sascha
Girão, Henrique
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Centro de Estudos de Doenças Crónicas (CEDOC)
NOVA Medical School|Faculdade de Ciências Médicas (NMS|FCM)
RUN
dc.contributor.author.fl_str_mv Catarino, Steve
Ribeiro-Rodrigues, Teresa M
Sá Ferreira, Rita
Ramalho, José
Abert, Christine
Martens, Sascha
Girão, Henrique
description This research was supported by the European Regional Development Fund (ERDF) through the Operational Program for Competitiveness Factors (COMPETE) [under the projects PAC “NETDIAMOND” POCI-01-0145-FEDER-016385; HealthyAging2020 CENTRO-01-0145-FEDER-000012-N2323; POCI-01-0145-FEDER-007440, CENTRO-01-0145-FEDER-032179, CENTRO-01-0145-FEDER-032414,FCTUID/NEU/04539/2013 and ID/NEU/04539/2019]. This research is based upon work from COST Action (PROTEOSTASIS BM1307), supported by COST (European Cooperation in Science and Technology).S.C. was supported by Action BM1307 – 39607 from COST Action PROTEOSTASIS BM1307, T.M.R.-R. was supported by PD/BD/52294/2013 from Fundação para a Ciência e a Tecnologia (FCT). C.A. was supported by a DOC Fellowship of the Austrian Academy of Sciences.
publishDate 2020
dc.date.none.fl_str_mv 2020-04-14T22:35:26Z
2020-04-07
2020-04-07T00:00:00Z
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/10362/96174
url http://hdl.handle.net/10362/96174
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2073-4409
PURE: 17746275
https://doi.org/10.3390/cells9040902
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.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
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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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