A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Reference Report

Reference
Citation McHugh, B., Krause, S.A., Yu, B., Deans, A.M., Heasman, S., McLaughlin, P., Heck, M.M. (2004). Invadolysin: a novel, conserved metalloprotease links mitotic structural rearrangements with cell migration.  J. Cell Biol. 167(4): 673--686. (Export to RIS)
FlyBase ID FBrf0180378
Publication Type Research paper
PubMed ID 15557119
PubMed Abstract 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.
DOI
Related Publication(s)
Review Metalloprotease, migration and mitosis.
Anonymous, 2004, Science 306(5703): 1862 [FBrf0188456]

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Language of Publication English
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Publication Type Journal
Abbreviation J. Cell Biol.
Title Journal of Cell Biology
Publication Year 1966-
ISBN/ISSN 0021-9525
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