The conserved metalloprotease invadolysin localizes to the surface of lipid droplets
Author(s) -
Neville Cobbe,
Kathryn M. Marshall,
Shubha Gururaja Rao,
Ching-Wen Chang,
Francesca Di Cara,
Edward Duca,
Sharron Vass,
Adam Kassan,
Margarete M. S. Heck
Publication year - 2009
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.044610
Subject(s) - biology , organelle , lipid droplet , metalloproteinase , lipid metabolism , microbiology and biotechnology , drosophila (subgenus) , mutant , matrix metalloproteinase , gene , biochemistry
Invadolysin is a metalloprotease conserved in many different organisms, previously shown to be essential in Drosophila with roles in cell division and cell migration. The gene seems to be ubiquitously expressed and four distinct splice variants have been identified in human cells but not in most other species examined. Immunofluorescent detection of human invadolysin in cultured cells reveals the protein to be associated with the surface of lipid droplets. By means of subcellular fractionation, we have independently confirmed the association of invadolysin with lipid droplets. We thus identify invadolysin as the first metalloprotease located on these dynamic organelles. In addition, analysis of larval fat-body morphological appearance and triglyceride levels in the Drosophila invadolysin mutant suggests that invadolysin plays a role in lipid storage or metabolism.
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