PI4P and BLOC-1 remodel endosomal membranes into tubules
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , , , , , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.14/40745 |
Resumo: | Intracellular trafficking is mediated by transport carriers that originate by membrane remodeling from donor organelles. Tubular carriers contribute to the flux of membrane lipids and proteins to acceptor organelles, but how lipids and proteins impose a tubular geometry on the carriers is incompletely understood. Using imaging approaches on cells and in vitro membrane systems, we show that phosphatidylinositol-4-phosphate (PI4P) and biogenesis of lysosome-related organelles complex 1 (BLOC-1) govern the formation, stability, and functions of recycling endosomal tubules. In vitro, BLOC-1 binds and tubulates negatively charged membranes, including those containing PI4P. In cells, endosomal PI4P production by type II PI4-kinases is needed to form and stabilize BLOC-1-dependent recycling endosomal tubules. Decreased PI4KIIs expression impairs the recycling of endosomal cargoes and the life cycles of intracellular pathogens such as Chlamydia bacteria and influenza virus that exploit the membrane dynamics of recycling endosomes. This study demonstrates how a phospholipid and a protein complex coordinate the remodeling of cellular membranes into functional tubules. |
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PI4P and BLOC-1 remodel endosomal membranes into tubulesBiophysicsMembrane and lipid biologyOrganellesPhysiologyIntracellular trafficking is mediated by transport carriers that originate by membrane remodeling from donor organelles. Tubular carriers contribute to the flux of membrane lipids and proteins to acceptor organelles, but how lipids and proteins impose a tubular geometry on the carriers is incompletely understood. Using imaging approaches on cells and in vitro membrane systems, we show that phosphatidylinositol-4-phosphate (PI4P) and biogenesis of lysosome-related organelles complex 1 (BLOC-1) govern the formation, stability, and functions of recycling endosomal tubules. In vitro, BLOC-1 binds and tubulates negatively charged membranes, including those containing PI4P. In cells, endosomal PI4P production by type II PI4-kinases is needed to form and stabilize BLOC-1-dependent recycling endosomal tubules. Decreased PI4KIIs expression impairs the recycling of endosomal cargoes and the life cycles of intracellular pathogens such as Chlamydia bacteria and influenza virus that exploit the membrane dynamics of recycling endosomes. This study demonstrates how a phospholipid and a protein complex coordinate the remodeling of cellular membranes into functional tubules.Veritati - Repositório Institucional da Universidade Católica PortuguesaJani, Riddhi AtulDi Cicco, AurélieKeren-Kaplan, TalVale-Costa, SilviaHamaoui, DanielHurbain, IlseTsai, Feng-ChingDimarco, MathildeMacé, Anne-SophieZhu, YueyaoAmorim, Maria JoãoBassereau, PatriciaBonifacino, JuanSubtil, AgatheMarks, MichaelLévy, DanielRaposo, GraçaDelevoye, Cédric2023-03-29T09:17:12Z2022-11-072022-11-07T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.14/40745eng0021-952510.1083/jcb.20211013285139376272PMC952420436169638001044895300001info: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:RCAAP2023-09-05T01:38:29Zoai:repositorio.ucp.pt:10400.14/40745Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:33:26.538855Repositório 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 |
PI4P and BLOC-1 remodel endosomal membranes into tubules |
title |
PI4P and BLOC-1 remodel endosomal membranes into tubules |
spellingShingle |
PI4P and BLOC-1 remodel endosomal membranes into tubules Jani, Riddhi Atul Biophysics Membrane and lipid biology Organelles Physiology |
title_short |
PI4P and BLOC-1 remodel endosomal membranes into tubules |
title_full |
PI4P and BLOC-1 remodel endosomal membranes into tubules |
title_fullStr |
PI4P and BLOC-1 remodel endosomal membranes into tubules |
title_full_unstemmed |
PI4P and BLOC-1 remodel endosomal membranes into tubules |
title_sort |
PI4P and BLOC-1 remodel endosomal membranes into tubules |
author |
Jani, Riddhi Atul |
author_facet |
Jani, Riddhi Atul Di Cicco, Aurélie Keren-Kaplan, Tal Vale-Costa, Silvia Hamaoui, Daniel Hurbain, Ilse Tsai, Feng-Ching Dimarco, Mathilde Macé, Anne-Sophie Zhu, Yueyao Amorim, Maria João Bassereau, Patricia Bonifacino, Juan Subtil, Agathe Marks, Michael Lévy, Daniel Raposo, Graça Delevoye, Cédric |
author_role |
author |
author2 |
Di Cicco, Aurélie Keren-Kaplan, Tal Vale-Costa, Silvia Hamaoui, Daniel Hurbain, Ilse Tsai, Feng-Ching Dimarco, Mathilde Macé, Anne-Sophie Zhu, Yueyao Amorim, Maria João Bassereau, Patricia Bonifacino, Juan Subtil, Agathe Marks, Michael Lévy, Daniel Raposo, Graça Delevoye, Cédric |
author2_role |
author author author author author author author author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Veritati - Repositório Institucional da Universidade Católica Portuguesa |
dc.contributor.author.fl_str_mv |
Jani, Riddhi Atul Di Cicco, Aurélie Keren-Kaplan, Tal Vale-Costa, Silvia Hamaoui, Daniel Hurbain, Ilse Tsai, Feng-Ching Dimarco, Mathilde Macé, Anne-Sophie Zhu, Yueyao Amorim, Maria João Bassereau, Patricia Bonifacino, Juan Subtil, Agathe Marks, Michael Lévy, Daniel Raposo, Graça Delevoye, Cédric |
dc.subject.por.fl_str_mv |
Biophysics Membrane and lipid biology Organelles Physiology |
topic |
Biophysics Membrane and lipid biology Organelles Physiology |
description |
Intracellular trafficking is mediated by transport carriers that originate by membrane remodeling from donor organelles. Tubular carriers contribute to the flux of membrane lipids and proteins to acceptor organelles, but how lipids and proteins impose a tubular geometry on the carriers is incompletely understood. Using imaging approaches on cells and in vitro membrane systems, we show that phosphatidylinositol-4-phosphate (PI4P) and biogenesis of lysosome-related organelles complex 1 (BLOC-1) govern the formation, stability, and functions of recycling endosomal tubules. In vitro, BLOC-1 binds and tubulates negatively charged membranes, including those containing PI4P. In cells, endosomal PI4P production by type II PI4-kinases is needed to form and stabilize BLOC-1-dependent recycling endosomal tubules. Decreased PI4KIIs expression impairs the recycling of endosomal cargoes and the life cycles of intracellular pathogens such as Chlamydia bacteria and influenza virus that exploit the membrane dynamics of recycling endosomes. This study demonstrates how a phospholipid and a protein complex coordinate the remodeling of cellular membranes into functional tubules. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-11-07 2022-11-07T00:00:00Z 2023-03-29T09:17:12Z |
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/10400.14/40745 |
url |
http://hdl.handle.net/10400.14/40745 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0021-9525 10.1083/jcb.202110132 85139376272 PMC9524204 36169638 001044895300001 |
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 |
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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