The conserved metalloprotease invadolysin localizes to the surface of lipid droplets

Author:

Cobbe Neville1,Marshall Kathryn M.2,Rao Shubha Gururaja3,Chang Ching-Wen1,Di Cara Francesca1,Duca Edward1,Vass Sharron1,Kassan Adam4,Heck Margarete M. S.1

Affiliation:

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

Abstract

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.

Publisher

The Company of Biologists

Subject

Cell Biology

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