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MT1-MMP recruits the ER-Golgi SNARE Bet1 for efficient MT1-MMP transport to the plasma membrane
Metastasis is a major cause of cancer-related death. Membrane type 1–matrix metalloproteinase (MT1-MMP) is a critical protease for local invasion and metastasis. MT1-MMP is synthesized in the endoplasmic reticulum (ER) and transported in vesicles to invadopodia, specialized subdomains of the plasma...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6781441/ https://www.ncbi.nlm.nih.gov/pubmed/31519727 http://dx.doi.org/10.1083/jcb.201808149 |
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author | Miyagawa, Takuya Hasegawa, Kana Aoki, Yoko Watanabe, Takuya Otagiri, Yuka Arasaki, Kohei Wakana, Yuichi Asano, Kenichi Tanaka, Masato Yamaguchi, Hideki Tagaya, Mitsuo Inoue, Hiroki |
author_facet | Miyagawa, Takuya Hasegawa, Kana Aoki, Yoko Watanabe, Takuya Otagiri, Yuka Arasaki, Kohei Wakana, Yuichi Asano, Kenichi Tanaka, Masato Yamaguchi, Hideki Tagaya, Mitsuo Inoue, Hiroki |
author_sort | Miyagawa, Takuya |
collection | PubMed |
description | Metastasis is a major cause of cancer-related death. Membrane type 1–matrix metalloproteinase (MT1-MMP) is a critical protease for local invasion and metastasis. MT1-MMP is synthesized in the endoplasmic reticulum (ER) and transported in vesicles to invadopodia, specialized subdomains of the plasma membrane, through secretory and endocytic recycling pathways. The molecular mechanism underlying intracellular transport of MT1-MMP has been extensively studied, but is not fully understood. We show that MT1-MMP diverts the SNARE Bet1 from its function in ER-Golgi transport, to promote MT1-MMP trafficking to the cell surface, likely to invadopodia. In invasive cells, Bet1 is localized in MT1-MMP–positive endosomes in addition to the Golgi apparatus, and forms a novel SNARE complex with syntaxin 4 and endosomal SNAREs. MT1-MMP may also use Bet1 for its export from raft-like structures in the ER. Our results suggest the recruitment of Bet1 at an early stage after MT1-MMP expression promotes the exit of MT1-MMP from the ER and its efficient transport to invadopodia. |
format | Online Article Text |
id | pubmed-6781441 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-67814412020-04-07 MT1-MMP recruits the ER-Golgi SNARE Bet1 for efficient MT1-MMP transport to the plasma membrane Miyagawa, Takuya Hasegawa, Kana Aoki, Yoko Watanabe, Takuya Otagiri, Yuka Arasaki, Kohei Wakana, Yuichi Asano, Kenichi Tanaka, Masato Yamaguchi, Hideki Tagaya, Mitsuo Inoue, Hiroki J Cell Biol Research Articles Metastasis is a major cause of cancer-related death. Membrane type 1–matrix metalloproteinase (MT1-MMP) is a critical protease for local invasion and metastasis. MT1-MMP is synthesized in the endoplasmic reticulum (ER) and transported in vesicles to invadopodia, specialized subdomains of the plasma membrane, through secretory and endocytic recycling pathways. The molecular mechanism underlying intracellular transport of MT1-MMP has been extensively studied, but is not fully understood. We show that MT1-MMP diverts the SNARE Bet1 from its function in ER-Golgi transport, to promote MT1-MMP trafficking to the cell surface, likely to invadopodia. In invasive cells, Bet1 is localized in MT1-MMP–positive endosomes in addition to the Golgi apparatus, and forms a novel SNARE complex with syntaxin 4 and endosomal SNAREs. MT1-MMP may also use Bet1 for its export from raft-like structures in the ER. Our results suggest the recruitment of Bet1 at an early stage after MT1-MMP expression promotes the exit of MT1-MMP from the ER and its efficient transport to invadopodia. Rockefeller University Press 2019-10-07 2019-09-13 /pmc/articles/PMC6781441/ /pubmed/31519727 http://dx.doi.org/10.1083/jcb.201808149 Text en © 2019 Miyagawa 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 Miyagawa, Takuya Hasegawa, Kana Aoki, Yoko Watanabe, Takuya Otagiri, Yuka Arasaki, Kohei Wakana, Yuichi Asano, Kenichi Tanaka, Masato Yamaguchi, Hideki Tagaya, Mitsuo Inoue, Hiroki MT1-MMP recruits the ER-Golgi SNARE Bet1 for efficient MT1-MMP transport to the plasma membrane |
title | MT1-MMP recruits the ER-Golgi SNARE Bet1 for efficient MT1-MMP transport to the plasma membrane |
title_full | MT1-MMP recruits the ER-Golgi SNARE Bet1 for efficient MT1-MMP transport to the plasma membrane |
title_fullStr | MT1-MMP recruits the ER-Golgi SNARE Bet1 for efficient MT1-MMP transport to the plasma membrane |
title_full_unstemmed | MT1-MMP recruits the ER-Golgi SNARE Bet1 for efficient MT1-MMP transport to the plasma membrane |
title_short | MT1-MMP recruits the ER-Golgi SNARE Bet1 for efficient MT1-MMP transport to the plasma membrane |
title_sort | mt1-mmp recruits the er-golgi snare bet1 for efficient mt1-mmp transport to the plasma membrane |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6781441/ https://www.ncbi.nlm.nih.gov/pubmed/31519727 http://dx.doi.org/10.1083/jcb.201808149 |
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