Lipid phosphate phosphatase 3 participates in transport carrier formation and protein trafficking in the early secretory pathway

The inhibition of phosphatidic acid phosphatase (PAP) activity by propanolol indicates that diacylglycerol (DAG) is required for the formation of transport carriers at the Golgi and for retrograde trafficking to the ER. Here we report that the PAP2 family member lipid phosphate phosphatase 3 (LPP3,...

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Autores: Gutiérrez Martínez, Enric, Fernández Ulibarri, Inés, Lázaro Diégez, Francisco, Johannes, Ludger, Pyne, Susan, Sarri Plans, Elisabet, Egea Guri, Gustavo
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2013
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:2445/48065
Acceso en línea:https://hdl.handle.net/2445/48065
Access Level:acceso abierto
Palabra clave:Aparell de Golgi
Reticle endoplasmàtic
Homeòstasi
Lípids
Golgi apparatus
Endoplasmic reticulum
Homeostasis
Lipids
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spelling Lipid phosphate phosphatase 3 participates in transport carrier formation and protein trafficking in the early secretory pathwayGutiérrez Martínez, EnricFernández Ulibarri, InésLázaro Diégez, FranciscoJohannes, LudgerPyne, SusanSarri Plans, ElisabetEgea Guri, GustavoAparell de GolgiReticle endoplasmàticHomeòstasiLípidsGolgi apparatusEndoplasmic reticulumHomeostasisLipidsThe inhibition of phosphatidic acid phosphatase (PAP) activity by propanolol indicates that diacylglycerol (DAG) is required for the formation of transport carriers at the Golgi and for retrograde trafficking to the ER. Here we report that the PAP2 family member lipid phosphate phosphatase 3 (LPP3, also known as PAP2b) localizes in compartments of the secretory pathway from ER export sites to the Golgi complex. The depletion of human LPP3: (i) reduces the number of tubules generated from the ER-Golgi intermediate compartment and the Golgi, with those formed from the Golgi being longer in LPP3-silenced cells than in control cells; (ii) impairs the Rab6-dependent retrograde transport of Shiga toxin subunit B from the Golgi to the ER, but not the anterograde transport of VSV-G or ssDsRed; and (iii) induces a high accumulation of Golgi-associated membrane buds. LPP3 depletion also reduces levels of de novo synthesized DAG and the Golgi-associated DAG contents. Remarkably, overexpression of a catalytically inactive form of LPP3 mimics the effects of LPP3 knockdown on Rab6-dependent retrograde transport. We conclude that LPP3 participates in the formation of retrograde transport carriers at the ER-Golgi interface, where it transitorily cycles, and during its route to the plasma membrane.The Company of Biologists2013201320132013info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersion15 p.application/pdfhttps://hdl.handle.net/2445/48065Articles 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)InglésVersió postprint del document publicat a: http://dx.doi.org/10.1242/jcs.117705Journal of Cell Science, 2013, vol. 126, num. 12, p. 2641-2655http://dx.doi.org/10.1242/jcs.117705(c) Gutiérrez Martínez, E. et al., 2013info:eu-repo/semantics/openAccessoai:recercat.cat:2445/480652026-05-29T05:05:01Z
dc.title.none.fl_str_mv Lipid phosphate phosphatase 3 participates in transport carrier formation and protein trafficking in the early secretory pathway
title Lipid phosphate phosphatase 3 participates in transport carrier formation and protein trafficking in the early secretory pathway
spellingShingle Lipid phosphate phosphatase 3 participates in transport carrier formation and protein trafficking in the early secretory pathway
Gutiérrez Martínez, Enric
Aparell de Golgi
Reticle endoplasmàtic
Homeòstasi
Lípids
Golgi apparatus
Endoplasmic reticulum
Homeostasis
Lipids
title_short Lipid phosphate phosphatase 3 participates in transport carrier formation and protein trafficking in the early secretory pathway
title_full Lipid phosphate phosphatase 3 participates in transport carrier formation and protein trafficking in the early secretory pathway
title_fullStr Lipid phosphate phosphatase 3 participates in transport carrier formation and protein trafficking in the early secretory pathway
title_full_unstemmed Lipid phosphate phosphatase 3 participates in transport carrier formation and protein trafficking in the early secretory pathway
title_sort Lipid phosphate phosphatase 3 participates in transport carrier formation and protein trafficking in the early secretory pathway
dc.creator.none.fl_str_mv Gutiérrez Martínez, Enric
Fernández Ulibarri, Inés
Lázaro Diégez, Francisco
Johannes, Ludger
Pyne, Susan
Sarri Plans, Elisabet
Egea Guri, Gustavo
author Gutiérrez Martínez, Enric
author_facet Gutiérrez Martínez, Enric
Fernández Ulibarri, Inés
Lázaro Diégez, Francisco
Johannes, Ludger
Pyne, Susan
Sarri Plans, Elisabet
Egea Guri, Gustavo
author_role author
author2 Fernández Ulibarri, Inés
Lázaro Diégez, Francisco
Johannes, Ludger
Pyne, Susan
Sarri Plans, Elisabet
Egea Guri, Gustavo
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Aparell de Golgi
Reticle endoplasmàtic
Homeòstasi
Lípids
Golgi apparatus
Endoplasmic reticulum
Homeostasis
Lipids
topic Aparell de Golgi
Reticle endoplasmàtic
Homeòstasi
Lípids
Golgi apparatus
Endoplasmic reticulum
Homeostasis
Lipids
description The inhibition of phosphatidic acid phosphatase (PAP) activity by propanolol indicates that diacylglycerol (DAG) is required for the formation of transport carriers at the Golgi and for retrograde trafficking to the ER. Here we report that the PAP2 family member lipid phosphate phosphatase 3 (LPP3, also known as PAP2b) localizes in compartments of the secretory pathway from ER export sites to the Golgi complex. The depletion of human LPP3: (i) reduces the number of tubules generated from the ER-Golgi intermediate compartment and the Golgi, with those formed from the Golgi being longer in LPP3-silenced cells than in control cells; (ii) impairs the Rab6-dependent retrograde transport of Shiga toxin subunit B from the Golgi to the ER, but not the anterograde transport of VSV-G or ssDsRed; and (iii) induces a high accumulation of Golgi-associated membrane buds. LPP3 depletion also reduces levels of de novo synthesized DAG and the Golgi-associated DAG contents. Remarkably, overexpression of a catalytically inactive form of LPP3 mimics the effects of LPP3 knockdown on Rab6-dependent retrograde transport. We conclude that LPP3 participates in the formation of retrograde transport carriers at the ER-Golgi interface, where it transitorily cycles, and during its route to the plasma membrane.
publishDate 2013
dc.date.none.fl_str_mv 2013
2013
2013
2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/48065
url https://hdl.handle.net/2445/48065
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió postprint del document publicat a: http://dx.doi.org/10.1242/jcs.117705
Journal of Cell Science, 2013, vol. 126, num. 12, p. 2641-2655
http://dx.doi.org/10.1242/jcs.117705
dc.rights.none.fl_str_mv (c) Gutiérrez Martínez, E. et al., 2013
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) Gutiérrez Martínez, E. et al., 2013
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 15 p.
application/pdf
dc.publisher.none.fl_str_mv The Company of Biologists
publisher.none.fl_str_mv The Company of Biologists
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
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score 15.811543

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