Cargando…

A bipartite sorting signal ensures specificity of retromer complex in membrane protein recycling

Retromer is an evolutionarily conserved protein complex, which sorts functionally diverse membrane proteins into recycling tubules/vesicles from the endosome. Many of the identified cargos possess a recycling signal sequence defined as ØX[L/M/V], where Ø is F/Y/W. However, this sequence is present i...

Descripción completa

Detalles Bibliográficos
Autores principales: Suzuki, Sho W., Chuang, Ya-Shan, Li, Ming, Seaman, Matthew N.J., Emr, Scott D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6719449/
https://www.ncbi.nlm.nih.gov/pubmed/31337624
http://dx.doi.org/10.1083/jcb.201901019
_version_ 1783447936911278080
author Suzuki, Sho W.
Chuang, Ya-Shan
Li, Ming
Seaman, Matthew N.J.
Emr, Scott D.
author_facet Suzuki, Sho W.
Chuang, Ya-Shan
Li, Ming
Seaman, Matthew N.J.
Emr, Scott D.
author_sort Suzuki, Sho W.
collection PubMed
description Retromer is an evolutionarily conserved protein complex, which sorts functionally diverse membrane proteins into recycling tubules/vesicles from the endosome. Many of the identified cargos possess a recycling signal sequence defined as ØX[L/M/V], where Ø is F/Y/W. However, this sequence is present in almost all proteins encoded in the genome. Also, several identified recycling sequences do not follow this rule. How then does retromer precisely select its cargos? Here, we reveal that an additional motif is also required for cargo retrieval. The two distinct motifs form a bipartite recycling signal recognized by the retromer subunits, Vps26 and Vps35. Strikingly, Vps26 utilizes different binding sites depending on the cargo, allowing retromer to recycle different membrane proteins. Thus, retromer interacts with cargos in a more complex manner than previously thought, which facilitates precise cargo recognition.
format Online
Article
Text
id pubmed-6719449
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-67194492020-03-02 A bipartite sorting signal ensures specificity of retromer complex in membrane protein recycling Suzuki, Sho W. Chuang, Ya-Shan Li, Ming Seaman, Matthew N.J. Emr, Scott D. J Cell Biol Research Articles Retromer is an evolutionarily conserved protein complex, which sorts functionally diverse membrane proteins into recycling tubules/vesicles from the endosome. Many of the identified cargos possess a recycling signal sequence defined as ØX[L/M/V], where Ø is F/Y/W. However, this sequence is present in almost all proteins encoded in the genome. Also, several identified recycling sequences do not follow this rule. How then does retromer precisely select its cargos? Here, we reveal that an additional motif is also required for cargo retrieval. The two distinct motifs form a bipartite recycling signal recognized by the retromer subunits, Vps26 and Vps35. Strikingly, Vps26 utilizes different binding sites depending on the cargo, allowing retromer to recycle different membrane proteins. Thus, retromer interacts with cargos in a more complex manner than previously thought, which facilitates precise cargo recognition. Rockefeller University Press 2019-09-02 2019-07-23 /pmc/articles/PMC6719449/ /pubmed/31337624 http://dx.doi.org/10.1083/jcb.201901019 Text en © 2019 Suzuki et al. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/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 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Research Articles
Suzuki, Sho W.
Chuang, Ya-Shan
Li, Ming
Seaman, Matthew N.J.
Emr, Scott D.
A bipartite sorting signal ensures specificity of retromer complex in membrane protein recycling
title A bipartite sorting signal ensures specificity of retromer complex in membrane protein recycling
title_full A bipartite sorting signal ensures specificity of retromer complex in membrane protein recycling
title_fullStr A bipartite sorting signal ensures specificity of retromer complex in membrane protein recycling
title_full_unstemmed A bipartite sorting signal ensures specificity of retromer complex in membrane protein recycling
title_short A bipartite sorting signal ensures specificity of retromer complex in membrane protein recycling
title_sort bipartite sorting signal ensures specificity of retromer complex in membrane protein recycling
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6719449/
https://www.ncbi.nlm.nih.gov/pubmed/31337624
http://dx.doi.org/10.1083/jcb.201901019
work_keys_str_mv AT suzukishow abipartitesortingsignalensuresspecificityofretromercomplexinmembraneproteinrecycling
AT chuangyashan abipartitesortingsignalensuresspecificityofretromercomplexinmembraneproteinrecycling
AT liming abipartitesortingsignalensuresspecificityofretromercomplexinmembraneproteinrecycling
AT seamanmatthewnj abipartitesortingsignalensuresspecificityofretromercomplexinmembraneproteinrecycling
AT emrscottd abipartitesortingsignalensuresspecificityofretromercomplexinmembraneproteinrecycling
AT suzukishow bipartitesortingsignalensuresspecificityofretromercomplexinmembraneproteinrecycling
AT chuangyashan bipartitesortingsignalensuresspecificityofretromercomplexinmembraneproteinrecycling
AT liming bipartitesortingsignalensuresspecificityofretromercomplexinmembraneproteinrecycling
AT seamanmatthewnj bipartitesortingsignalensuresspecificityofretromercomplexinmembraneproteinrecycling
AT emrscottd bipartitesortingsignalensuresspecificityofretromercomplexinmembraneproteinrecycling