Cargando…
Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi
A disintegrin-like and metalloprotease with thrombospondin type I motif (ADAMTS9) is a member of the secreted metalloprotease family that is believed to digest extracellular matrix (ECM) proteins outside of cells. Its Caenorhabditis elegans orthologue, GON-1, is involved in ECM degradation and is re...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3338439/ https://www.ncbi.nlm.nih.gov/pubmed/22419820 http://dx.doi.org/10.1091/mbc.E11-10-0857 |
_version_ | 1782231190145597440 |
---|---|
author | Yoshina, Sawako Sakaki, Kenjiro Yonezumi-Hayashi, Aki Gengyo-Ando, Keiko Inoue, Hideshi Iino, Yuichi Mitani, Shohei |
author_facet | Yoshina, Sawako Sakaki, Kenjiro Yonezumi-Hayashi, Aki Gengyo-Ando, Keiko Inoue, Hideshi Iino, Yuichi Mitani, Shohei |
author_sort | Yoshina, Sawako |
collection | PubMed |
description | A disintegrin-like and metalloprotease with thrombospondin type I motif (ADAMTS9) is a member of the secreted metalloprotease family that is believed to digest extracellular matrix (ECM) proteins outside of cells. Its Caenorhabditis elegans orthologue, GON-1, is involved in ECM degradation and is required for gonad morphogenesis. ADAMTS9 and GON-1 have similar domain structures, and both have a unique C-terminal domain called the “GON domain,” whose function remains unknown. Here we show that down-regulation of human ADAMTS9 and C. elegans GON-1 results in the inhibition of protein transport from the endoplasmic reticulum (ER) to the Golgi. This phenotype was rescued by the expression of the GON domain localizing in the ER in human cells and C. elegans. We propose a novel function of ADAMTS9 and GON-1 in the ER that promotes protein transport from the ER to the Golgi. This function is GON-domain dependent but protease activity independent. |
format | Online Article Text |
id | pubmed-3338439 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-33384392012-07-16 Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi Yoshina, Sawako Sakaki, Kenjiro Yonezumi-Hayashi, Aki Gengyo-Ando, Keiko Inoue, Hideshi Iino, Yuichi Mitani, Shohei Mol Biol Cell Articles A disintegrin-like and metalloprotease with thrombospondin type I motif (ADAMTS9) is a member of the secreted metalloprotease family that is believed to digest extracellular matrix (ECM) proteins outside of cells. Its Caenorhabditis elegans orthologue, GON-1, is involved in ECM degradation and is required for gonad morphogenesis. ADAMTS9 and GON-1 have similar domain structures, and both have a unique C-terminal domain called the “GON domain,” whose function remains unknown. Here we show that down-regulation of human ADAMTS9 and C. elegans GON-1 results in the inhibition of protein transport from the endoplasmic reticulum (ER) to the Golgi. This phenotype was rescued by the expression of the GON domain localizing in the ER in human cells and C. elegans. We propose a novel function of ADAMTS9 and GON-1 in the ER that promotes protein transport from the ER to the Golgi. This function is GON-domain dependent but protease activity independent. The American Society for Cell Biology 2012-05-01 /pmc/articles/PMC3338439/ /pubmed/22419820 http://dx.doi.org/10.1091/mbc.E11-10-0857 Text en © 2012 Yoshina et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Yoshina, Sawako Sakaki, Kenjiro Yonezumi-Hayashi, Aki Gengyo-Ando, Keiko Inoue, Hideshi Iino, Yuichi Mitani, Shohei Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi |
title | Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi |
title_full | Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi |
title_fullStr | Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi |
title_full_unstemmed | Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi |
title_short | Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi |
title_sort | identification of a novel adamts9/gon-1 function for protein transport from the er to the golgi |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3338439/ https://www.ncbi.nlm.nih.gov/pubmed/22419820 http://dx.doi.org/10.1091/mbc.E11-10-0857 |
work_keys_str_mv | AT yoshinasawako identificationofanoveladamts9gon1functionforproteintransportfromtheertothegolgi AT sakakikenjiro identificationofanoveladamts9gon1functionforproteintransportfromtheertothegolgi AT yonezumihayashiaki identificationofanoveladamts9gon1functionforproteintransportfromtheertothegolgi AT gengyoandokeiko identificationofanoveladamts9gon1functionforproteintransportfromtheertothegolgi AT inouehideshi identificationofanoveladamts9gon1functionforproteintransportfromtheertothegolgi AT iinoyuichi identificationofanoveladamts9gon1functionforproteintransportfromtheertothegolgi AT mitanishohei identificationofanoveladamts9gon1functionforproteintransportfromtheertothegolgi |