RRC ID 46492
Author Yoshina S, Sakaki K, Yonezumi-Hayashi A, Gengyo-Ando K, Inoue H, Iino Y, Mitani S.
Title Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi.
Journal Mol Biol Cell
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.
Volume 23(9)
Pages 1728-41
Published 2012-5-1
DOI 10.1091/mbc.E11-10-0857
PII mbc.E11-10-0857
PMID 22419820
PMC PMC3338439
MeSH ADAM Proteins / genetics ADAM Proteins / metabolism* ADAMTS9 Protein Animals Animals, Genetically Modified Caenorhabditis elegans Caenorhabditis elegans Proteins / genetics Caenorhabditis elegans Proteins / metabolism* Cell Line Conserved Sequence Endoplasmic Reticulum / metabolism* Golgi Apparatus / metabolism* HEK293 Cells Humans Metalloendopeptidases / genetics Metalloendopeptidases / metabolism* Protein Transport
IF 3.791
Times Cited 14
WOS Category CELL BIOLOGY
Resource
C.elegans tm3146