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Title: | The conserved metalloprotease invadolysin localizes to the surface of lipid droplets |
Authors: | Cobbe, Neville Marshall, Kathryn M. Gururaja Rao, Shubha Chang, Ching-Wen Cara, Francesca Di Duca, Edward Vass, Sharron Kassan, Adam Heck, Margarete M.S. |
Keywords: | Lipids -- Analysis Metalloproteinases Phylogeny |
Issue Date: | 2009 |
Publisher: | The Company of Biologists Ltd. |
Citation: | Cobbe, N., Marshall, K. M., Rao, S. G., Chang, C. W., Di Cara, F., Duca, E., ... & Heck, M. M. (2009). The conserved metalloprotease invadolysin localizes to the surface of lipid droplets. Journal of cell science, 122(18), 3414-3423. |
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. |
URI: | https://www.um.edu.mt/library/oar/handle/123456789/102069 |
Appears in Collections: | Scholarly Works - FacEduMSE |
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