Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi

Sawako Yoshina, Kenjiro Sakaki, Aki Yonezumi-Hayashi, Keiko Gengyo-Ando, Hideshi Inoue, Yuichi Iino, Shohei Mitani

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1728-1741
Number of pages14
JournalMolecular Biology of the Cell
Issue number9
Publication statusPublished - 2012 May 1


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