Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport

We have previously reported that actin filaments are involved in protein transport from the Golgi complex to the endoplasmic reticulum. Herein, we examined whether myosin motors or actin comets mediate this transport. To address this issue we have used, on one hand, a combination of specific inhibit...

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Autores: Durán Serrano, Juan Manuel, Valderrama i Alfonso, Ferran, Castel i Gil, Susanna, Magdalena, Juana, Tomás, Mónica, Hosoya, Hiroshi, Renau Piqueras, Jaime, Malhotra, Vivek, Egea Guri, Gustavo
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2003
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/24654
Acceso en línea:https://hdl.handle.net/2445/24654
Access Level:acceso abierto
Palabra clave:Aparell de Golgi
Reticle endoplasmàtic
Proteïnes
Transport biològic
Citologia
Golgi apparatus
Endoplasmic reticulum
Proteins
Biological transport
Cytology
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spelling Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transportDurán Serrano, Juan ManuelValderrama i Alfonso, FerranCastel i Gil, SusannaMagdalena, JuanaTomás, MónicaHosoya, HiroshiRenau Piqueras, JaimeMalhotra, VivekEgea Guri, GustavoAparell de GolgiReticle endoplasmàticProteïnesTransport biològicCitologiaGolgi apparatusEndoplasmic reticulumProteinsBiological transportCytologyWe have previously reported that actin filaments are involved in protein transport from the Golgi complex to the endoplasmic reticulum. Herein, we examined whether myosin motors or actin comets mediate this transport. To address this issue we have used, on one hand, a combination of specific inhibitors such as 2,3-butanedione monoxime (BDM) and 1-[5-isoquinoline sulfonyl]-2-methyl piperazine (ML7), which inhibit myosin and the phosphorylation of myosin II by the myosin light chain kinase, respectively; and a mutant of the nonmuscle myosin II regulatory light chain, which cannot be phosphorylated (MRLC2AA). On the other hand, actin comet tails were induced by the overexpression of phosphatidylinositol phosphate 5-kinase. Cells treated with BDM/ML7 or those that express the MRLC2AA mutant revealed a significant reduction in the brefeldin A (BFA)-induced fusion of Golgi enzymes with the endoplasmic reticulum (ER). This delay was not caused by an alteration in the formation of the BFA-induced tubules from the Golgi complex. In addition, the Shiga toxin fragment B transport from the Golgi complex to the ER was also altered. This impairment in the retrograde protein transport was not due to depletion of intracellular calcium stores or to the activation of Rho kinase. Neither the reassembly of the Golgi complex after BFA removal nor VSV-G transport from ER to the Golgi was altered in cells treated with BDM/ML7 or expressing MRLC2AA. Finally, transport carriers containing Shiga toxin did not move into the cytosol at the tips of comet tails of polymerizing actin. Collectively, the results indicate that 1) myosin motors move to transport carriers from the Golgi complex to the ER along actin filaments; 2) nonmuscle myosin II mediates in this process; and 3) actin comets are not involved in retrograde transport.American Society for Cell Biology201220122003info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion15 p.application/pdfhttps://hdl.handle.net/2445/24654Articles publicats en revistes (Biomedicina)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: http://dx.doi.org/10.1091/mbc.E02-04-0214Molecular Biology of the Cell, 2003, vol. 14, núm. 2, p. 445-459http://dx.doi.org/10.1091/mbc.E02-04-0214cc-by-nc-sa (c) Durán et al., 2003http://creativecommons.org/licenses/by-nc-sa/3.0/info:eu-repo/semantics/openAccessoai:recercat.cat:2445/246542026-05-29T05:05:01Z
dc.title.none.fl_str_mv Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport
title Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport
spellingShingle Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport
Durán Serrano, Juan Manuel
Aparell de Golgi
Reticle endoplasmàtic
Proteïnes
Transport biològic
Citologia
Golgi apparatus
Endoplasmic reticulum
Proteins
Biological transport
Cytology
title_short Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport
title_full Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport
title_fullStr Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport
title_full_unstemmed Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport
title_sort Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport
dc.creator.none.fl_str_mv Durán Serrano, Juan Manuel
Valderrama i Alfonso, Ferran
Castel i Gil, Susanna
Magdalena, Juana
Tomás, Mónica
Hosoya, Hiroshi
Renau Piqueras, Jaime
Malhotra, Vivek
Egea Guri, Gustavo
author Durán Serrano, Juan Manuel
author_facet Durán Serrano, Juan Manuel
Valderrama i Alfonso, Ferran
Castel i Gil, Susanna
Magdalena, Juana
Tomás, Mónica
Hosoya, Hiroshi
Renau Piqueras, Jaime
Malhotra, Vivek
Egea Guri, Gustavo
author_role author
author2 Valderrama i Alfonso, Ferran
Castel i Gil, Susanna
Magdalena, Juana
Tomás, Mónica
Hosoya, Hiroshi
Renau Piqueras, Jaime
Malhotra, Vivek
Egea Guri, Gustavo
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Aparell de Golgi
Reticle endoplasmàtic
Proteïnes
Transport biològic
Citologia
Golgi apparatus
Endoplasmic reticulum
Proteins
Biological transport
Cytology
topic Aparell de Golgi
Reticle endoplasmàtic
Proteïnes
Transport biològic
Citologia
Golgi apparatus
Endoplasmic reticulum
Proteins
Biological transport
Cytology
description We have previously reported that actin filaments are involved in protein transport from the Golgi complex to the endoplasmic reticulum. Herein, we examined whether myosin motors or actin comets mediate this transport. To address this issue we have used, on one hand, a combination of specific inhibitors such as 2,3-butanedione monoxime (BDM) and 1-[5-isoquinoline sulfonyl]-2-methyl piperazine (ML7), which inhibit myosin and the phosphorylation of myosin II by the myosin light chain kinase, respectively; and a mutant of the nonmuscle myosin II regulatory light chain, which cannot be phosphorylated (MRLC2AA). On the other hand, actin comet tails were induced by the overexpression of phosphatidylinositol phosphate 5-kinase. Cells treated with BDM/ML7 or those that express the MRLC2AA mutant revealed a significant reduction in the brefeldin A (BFA)-induced fusion of Golgi enzymes with the endoplasmic reticulum (ER). This delay was not caused by an alteration in the formation of the BFA-induced tubules from the Golgi complex. In addition, the Shiga toxin fragment B transport from the Golgi complex to the ER was also altered. This impairment in the retrograde protein transport was not due to depletion of intracellular calcium stores or to the activation of Rho kinase. Neither the reassembly of the Golgi complex after BFA removal nor VSV-G transport from ER to the Golgi was altered in cells treated with BDM/ML7 or expressing MRLC2AA. Finally, transport carriers containing Shiga toxin did not move into the cytosol at the tips of comet tails of polymerizing actin. Collectively, the results indicate that 1) myosin motors move to transport carriers from the Golgi complex to the ER along actin filaments; 2) nonmuscle myosin II mediates in this process; and 3) actin comets are not involved in retrograde transport.
publishDate 2003
dc.date.none.fl_str_mv 2003
2012
2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/24654
url https://hdl.handle.net/2445/24654
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: http://dx.doi.org/10.1091/mbc.E02-04-0214
Molecular Biology of the Cell, 2003, vol. 14, núm. 2, p. 445-459
http://dx.doi.org/10.1091/mbc.E02-04-0214
dc.rights.none.fl_str_mv cc-by-nc-sa (c) Durán et al., 2003
http://creativecommons.org/licenses/by-nc-sa/3.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by-nc-sa (c) Durán et al., 2003
http://creativecommons.org/licenses/by-nc-sa/3.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 15 p.
application/pdf
dc.publisher.none.fl_str_mv American Society for Cell Biology
publisher.none.fl_str_mv American Society for Cell Biology
dc.source.none.fl_str_mv Articles publicats en revistes (Biomedicina)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869425359299018752
score 15.81155

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