|
|
|
|
|
|
|
||
Article |
Invadolysin
: a novel, conserved metalloprotease links mitotic structural rearrangements with cell migration
2 Medical Research Council Centre for Inflammation Research, University of Edinburgh, Edinburgh EH8 9AG, Scotland, UK
Correspondence to M.M.S. Heck: margarete.heck{at}ed.ac.uk
The cell cycle is widely known to be regulated by networks of phosphorylation and ubiquitin-directed proteolysis. Here, we describe IX-14/invadolysin, a novel metalloprotease present only in metazoa, whose activity appears to be essential for mitotic progression. Mitotic neuroblasts of Drosophila melanogaster IX-14 mutant larvae exhibit increased levels of nuclear envelope proteins, monopolar and asymmetric spindles, and chromosomes that appear hypercondensed in length with a surrounding halo of loosely condensed chromatin. Zymography reveals that a protease activity, present in wild-type larval brains, is missing from homozygous tissue, and we show that IX-14/invadolysin cleaves lamin in vitro. The IX-14/invadolysin protein is predominantly found in cytoplasmic structures resembling invadopodia in fly and human cells, but is dramatically relocalized to the leading edge of migrating cells. Strikingly, we find that the directed migration of germ cells is affected in Drosophila IX-14 mutant embryos. Thus, invadolysin identifies a new family of conserved metalloproteases whose activity appears to be essential for the coordination of mitotic progression, but which also plays an unexpected role in cell migration.
S.A. Krause's present address is University of Glasgow, Institute of Biological and Life Sciences, Glasgow G11 6NU, UK.
A.-M. Deans's present address is Institute of Immunology and Infection Research, University of Edinburgh, Edinburgh EH9 3JT, UK.
Abbreviations used in this paper: MMP, matrix metalloproteases; S2, Schneider 2.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Facebook 
Reddit 
Technorati 
Twitter What's this?
Related Article
This article has been cited by other articles:
|
|
