Cargando…

A syntaxin 10–SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells

Mannose 6-phosphate receptors (MPRs) are transported from endosomes to the Golgi after delivering lysosomal enzymes to the endocytic pathway. This process requires Rab9 guanosine triphosphatase (GTPase) and the putative tether GCC185. We show in human cells that a soluble NSF attachment protein rece...

Descripción completa

Detalles Bibliográficos
Autores principales: Ganley, Ian G., Espinosa, Eric, Pfeffer, Suzanne R.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2213607/
https://www.ncbi.nlm.nih.gov/pubmed/18195106
http://dx.doi.org/10.1083/jcb.200707136
_version_ 1782148917132001280
author Ganley, Ian G.
Espinosa, Eric
Pfeffer, Suzanne R.
author_facet Ganley, Ian G.
Espinosa, Eric
Pfeffer, Suzanne R.
author_sort Ganley, Ian G.
collection PubMed
description Mannose 6-phosphate receptors (MPRs) are transported from endosomes to the Golgi after delivering lysosomal enzymes to the endocytic pathway. This process requires Rab9 guanosine triphosphatase (GTPase) and the putative tether GCC185. We show in human cells that a soluble NSF attachment protein receptor (SNARE) complex comprised of syntaxin 10 (STX10), STX16, Vti1a, and VAMP3 is required for this MPR transport but not for the STX6-dependent transport of TGN46 or cholera toxin from early endosomes to the Golgi. Depletion of STX10 leads to MPR missorting and hypersecretion of hexosaminidase. Mouse and rat cells lack STX10 and, thus, must use a different target membrane SNARE for this process. GCC185 binds directly to STX16 and is competed by Rab6. These data support a model in which the GCC185 tether helps Rab9-bearing transport vesicles deliver their cargo to the trans-Golgi and suggest that Rab GTPases can regulate SNARE–tether interactions. Importantly, our data provide a clear molecular distinction between the transport of MPRs and TGN46 to the trans-Golgi.
format Text
id pubmed-2213607
institution National Center for Biotechnology Information
language English
publishDate 2008
publisher The Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-22136072008-07-14 A syntaxin 10–SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells Ganley, Ian G. Espinosa, Eric Pfeffer, Suzanne R. J Cell Biol Research Articles Mannose 6-phosphate receptors (MPRs) are transported from endosomes to the Golgi after delivering lysosomal enzymes to the endocytic pathway. This process requires Rab9 guanosine triphosphatase (GTPase) and the putative tether GCC185. We show in human cells that a soluble NSF attachment protein receptor (SNARE) complex comprised of syntaxin 10 (STX10), STX16, Vti1a, and VAMP3 is required for this MPR transport but not for the STX6-dependent transport of TGN46 or cholera toxin from early endosomes to the Golgi. Depletion of STX10 leads to MPR missorting and hypersecretion of hexosaminidase. Mouse and rat cells lack STX10 and, thus, must use a different target membrane SNARE for this process. GCC185 binds directly to STX16 and is competed by Rab6. These data support a model in which the GCC185 tether helps Rab9-bearing transport vesicles deliver their cargo to the trans-Golgi and suggest that Rab GTPases can regulate SNARE–tether interactions. Importantly, our data provide a clear molecular distinction between the transport of MPRs and TGN46 to the trans-Golgi. The Rockefeller University Press 2008-01-14 /pmc/articles/PMC2213607/ /pubmed/18195106 http://dx.doi.org/10.1083/jcb.200707136 Text en Copyright © 2008, 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
Ganley, Ian G.
Espinosa, Eric
Pfeffer, Suzanne R.
A syntaxin 10–SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells
title A syntaxin 10–SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells
title_full A syntaxin 10–SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells
title_fullStr A syntaxin 10–SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells
title_full_unstemmed A syntaxin 10–SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells
title_short A syntaxin 10–SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells
title_sort syntaxin 10–snare complex distinguishes two distinct transport routes from endosomes to the trans-golgi in human cells
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2213607/
https://www.ncbi.nlm.nih.gov/pubmed/18195106
http://dx.doi.org/10.1083/jcb.200707136
work_keys_str_mv AT ganleyiang asyntaxin10snarecomplexdistinguishestwodistincttransportroutesfromendosomestothetransgolgiinhumancells
AT espinosaeric asyntaxin10snarecomplexdistinguishestwodistincttransportroutesfromendosomestothetransgolgiinhumancells
AT pfeffersuzanner asyntaxin10snarecomplexdistinguishestwodistincttransportroutesfromendosomestothetransgolgiinhumancells
AT ganleyiang syntaxin10snarecomplexdistinguishestwodistincttransportroutesfromendosomestothetransgolgiinhumancells
AT espinosaeric syntaxin10snarecomplexdistinguishestwodistincttransportroutesfromendosomestothetransgolgiinhumancells
AT pfeffersuzanner syntaxin10snarecomplexdistinguishestwodistincttransportroutesfromendosomestothetransgolgiinhumancells