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Dimeric PKD regulates membrane fission to form transport carriers at the TGN

Protein kinase D (PKD) is recruited to the trans-Golgi network (TGN) through interaction with diacylglycerol (DAG) and is required for the biogenesis of TGN to cell surface transport carriers. We now provide definitive evidence that PKD has a function in membrane fission. PKD depletion by siRNA inhi...

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Detalles Bibliográficos
Autores principales: Bossard, Carine, Bresson, Damien, Polishchuk, Roman S., Malhotra, Vivek
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140039/
https://www.ncbi.nlm.nih.gov/pubmed/18086912
http://dx.doi.org/10.1083/jcb.200703166
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author Bossard, Carine
Bresson, Damien
Polishchuk, Roman S.
Malhotra, Vivek
author_facet Bossard, Carine
Bresson, Damien
Polishchuk, Roman S.
Malhotra, Vivek
author_sort Bossard, Carine
collection PubMed
description Protein kinase D (PKD) is recruited to the trans-Golgi network (TGN) through interaction with diacylglycerol (DAG) and is required for the biogenesis of TGN to cell surface transport carriers. We now provide definitive evidence that PKD has a function in membrane fission. PKD depletion by siRNA inhibits trafficking from the TGN, whereas expression of a constitutively active PKD converts TGN into small vesicles. These findings demonstrate that PKD regulates membrane fission and this activity is used to control the size of transport carriers, and to prevent uncontrolled vesiculation of TGN during protein transport.
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spelling pubmed-21400392008-06-17 Dimeric PKD regulates membrane fission to form transport carriers at the TGN Bossard, Carine Bresson, Damien Polishchuk, Roman S. Malhotra, Vivek J Cell Biol Research Articles Protein kinase D (PKD) is recruited to the trans-Golgi network (TGN) through interaction with diacylglycerol (DAG) and is required for the biogenesis of TGN to cell surface transport carriers. We now provide definitive evidence that PKD has a function in membrane fission. PKD depletion by siRNA inhibits trafficking from the TGN, whereas expression of a constitutively active PKD converts TGN into small vesicles. These findings demonstrate that PKD regulates membrane fission and this activity is used to control the size of transport carriers, and to prevent uncontrolled vesiculation of TGN during protein transport. The Rockefeller University Press 2007-12-17 /pmc/articles/PMC2140039/ /pubmed/18086912 http://dx.doi.org/10.1083/jcb.200703166 Text en Copyright © 2007, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Research Articles
Bossard, Carine
Bresson, Damien
Polishchuk, Roman S.
Malhotra, Vivek
Dimeric PKD regulates membrane fission to form transport carriers at the TGN
title Dimeric PKD regulates membrane fission to form transport carriers at the TGN
title_full Dimeric PKD regulates membrane fission to form transport carriers at the TGN
title_fullStr Dimeric PKD regulates membrane fission to form transport carriers at the TGN
title_full_unstemmed Dimeric PKD regulates membrane fission to form transport carriers at the TGN
title_short Dimeric PKD regulates membrane fission to form transport carriers at the TGN
title_sort dimeric pkd regulates membrane fission to form transport carriers at the tgn
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2140039/
https://www.ncbi.nlm.nih.gov/pubmed/18086912
http://dx.doi.org/10.1083/jcb.200703166
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