ArticleMolecular biology of the cell2012
Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi.
Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
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- Optical manipulation of molecular function by chromophore-assisted light inactivation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2021Review
- Genetic interactions among ADAMTS metalloproteases and basement membrane molecules in cell migration in Caenorhabditis elegans.PloS one · 2020Article
- Fibroblastic Reticular Cells Control Conduit Matrix Deposition during Lymph Node Expansion.Cell reports · 2019Article
- AMPK blocks starvation-inducible transgenerational defects inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Comprehensive functional genomics using Caenorhabditis elegans as a model organism.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Article
- Risk factors and biomarkers of age-related macular degeneration.Progress in retinal and eye research · 2016Review
- Proinsulin misfolding and endoplasmic reticulum stress during the development and progression of diabetes.Molecular aspects of medicine · 2015Review
- The Tumor Suppressor BCL7B Functions in the Wnt Signaling Pathway.PLoS genetics · 2015Article
- Loss of C. elegans GON-1, an ADAMTS9 Homolog, Decreases Secretion Resulting in Altered Lifespan and Dauer Formation.PloS one · 2015Article
- Worming our way in and out of the Caenorhabditis elegans germline and developing embryo.Traffic (Copenhagen, Denmark) · 2013Review
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Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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