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First published online 25 August 2009
doi: 10.1242/jcs.044610

Journal of Cell Science 122, 3414-3423 (2009)
Published by The Company of Biologists 2009
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Research Article

The conserved metalloprotease invadolysin localizes to the surface of lipid droplets

Neville Cobbe1, Kathryn M. Marshall2, Shubha Gururaja Rao3, Ching-Wen Chang1, Francesca Di Cara1, Edward Duca1, Sharron Vass1, Adam Kassan4 and Margarete M. S. Heck1,*

1 University of Edinburgh, Queen's Medical Research Institute, Centre for Cardiovascular Science, 47 Little France Crescent, Edinburgh EH16 4TJ, UK
2 Department of Surgery, University of Melbourne, Austin Health, Studley Road, Heidelberg, Melbourne, Victoria 3084, Australia
3 Department of Molecular, Cell and Developmental Biology, University of California Los Angeles, Los Angeles, CA 90095, USA
4 Departament de Biologia Cellular, Facultat de Medicina, Institut d'Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), Universitat de Barcelona, Casanova 143, 08036 Barcelona, Spain

* Author for correspondence (margarete.heck{at}ed.ac.uk)

Accepted 25 June 2009

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.

Key words: Invadolysin, Lipid droplets, Metalloprotease, Phylogeny


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