Drosophila metalloproteases in development and differentiation: the role of ADAM proteins and their relatives
- PMID: 21684629
- DOI: 10.1016/j.ejcb.2011.04.015
Drosophila metalloproteases in development and differentiation: the role of ADAM proteins and their relatives
Abstract
ADAM metalloproteases are membrane bound glycoproteins that control many biological processes during development and differentiation, mainly by acting as ectodomain sheddases. The Drosophila genome contains five genes that code for classical ADAM proteins which are characterized by a highly conserved domain structure with the respective catalytic domains facing the extracellular space. More than 50 genes encode related proteins such as those that have lost their primary enzymatic activity while retaining, e.g., their adhesive properties. The physiological relevance of many Drosophila ADAMs and their relatives is still unknown, however for others, a striking role during organogenesis and tissue maintenance has been demonstrated during the last few years. We have carried out genetic screenings combined with candidate approaches, aiming to identify new components involved in cardiogenesis and muscle differentiation. Herein we summarize our results with a particular focus on metalloproteases with known or potential roles in tissue differentiation.
Copyright © 2011 Elsevier GmbH. All rights reserved.
Similar articles
-
(Make) stick and cut loose--disintegrin metalloproteases in development and disease.Birth Defects Res C Embryo Today. 2006 Mar;78(1):24-46. doi: 10.1002/bdrc.20066. Birth Defects Res C Embryo Today. 2006. PMID: 16622847 Review.
-
The disintegrin and metalloprotease Meltrin from Drosophila forms oligomers via its protein binding domain and is regulated by the homeobox protein VND during embryonic development.Insect Biochem Mol Biol. 2010 Nov;40(11):814-23. doi: 10.1016/j.ibmb.2010.07.010. Epub 2010 Aug 10. Insect Biochem Mol Biol. 2010. PMID: 20705134
-
Active metalloproteases of the A Disintegrin and Metalloprotease (ADAM) family: biological function and structure.J Proteome Res. 2011 Jan 7;10(1):17-33. doi: 10.1021/pr100556z. Epub 2010 Oct 14. J Proteome Res. 2011. PMID: 20849079 Review.
-
Ectodomain shedding and ADAMs in development.Development. 2012 Oct;139(20):3693-709. doi: 10.1242/dev.076398. Development. 2012. PMID: 22991436 Review.
-
Lipid rafts identified as locations of ectodomain shedding mediated by Meltrin beta/ADAM19.J Neurochem. 2004 Apr;89(1):119-23. doi: 10.1046/j.1471-4159.2003.02303.x. J Neurochem. 2004. PMID: 15030395
Cited by
-
Neprilysins regulate muscle contraction and heart function via cleavage of SERCA-inhibitory micropeptides.Nat Commun. 2022 Jul 29;13(1):4420. doi: 10.1038/s41467-022-31974-1. Nat Commun. 2022. PMID: 35906206 Free PMC article.
-
Natural and laboratory mutations in kuzbanian are associated with zinc stress phenotypes in Drosophila melanogaster.Sci Rep. 2017 Feb 20;7:42663. doi: 10.1038/srep42663. Sci Rep. 2017. PMID: 28218276 Free PMC article.
-
Drosophila neprilysins control insulin signaling and food intake via cleavage of regulatory peptides.Elife. 2016 Dec 6;5:e19430. doi: 10.7554/eLife.19430. Elife. 2016. PMID: 27919317 Free PMC article.
-
Frazzled/DCC facilitates cardiac cell outgrowth and attachment during Drosophila dorsal vessel formation.Dev Biol. 2013 Aug 15;380(2):233-42. doi: 10.1016/j.ydbio.2013.05.007. Epub 2013 May 16. Dev Biol. 2013. PMID: 23685255 Free PMC article.
-
Identification of the extracellular metallo-endopeptidases ADAM and ADAMTS in the yellow fever mosquito Aedes aegypti.Insect Biochem Mol Biol. 2022 Sep;148:103815. doi: 10.1016/j.ibmb.2022.103815. Epub 2022 Aug 3. Insect Biochem Mol Biol. 2022. PMID: 35932972 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Miscellaneous
