A potential role for Drosophila mucins in development and physiology
- PMID: 18725942
- PMCID: PMC2515642
- DOI: 10.1371/journal.pone.0003041
A potential role for Drosophila mucins in development and physiology
Abstract
Vital vertebrate organs are protected from the external environment by a barrier that to a large extent consists of mucins. These proteins are characterized by poorly conserved repeated sequences that are rich in prolines and potentially glycosylated threonines and serines (PTS). We have now used the characteristics of the PTS repeat domain to identify Drosophila mucins in a simple bioinformatics approach. Searching the predicted protein database for proteins with at least 4 repeats and a high ST content, more than 30 mucin-like proteins were identified, ranging from 300-23000 amino acids in length. We find that Drosophila mucins are present at all stages of the fly life cycle, and that their transcripts localize to selective organs analogous to sites of vertebrate mucin expression. The results could allow for addressing basic questions about human mucin-related diseases in this model system. Additionally, many of the mucins are expressed in selective tissues during embryogenesis, thus revealing new potential functions for mucins as apical matrix components during organ morphogenesis.
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References
-
- Hollingsworth MA, Swanson BJ. Mucins in cancer: protection and control of the cell surface. Nat Rev Cancer. 2004;4:45–60. - PubMed
-
- Perez-Vilar J, Hill RL. The structure and assembly of secreted mucins. J Biol Chem. 1999;274:31751–31754. - PubMed
-
- Wilkin MB, Becker MN, Mulvey D, Phan I, Chao A, et al. Drosophila dumpy is a gigantic extracellular protein required to maintain tension at epidermal-cuticle attachment sites. Curr Biol. 2000;10:559–567. - PubMed
-
- Fraichard S, Bouge AL, Chauvel I, Bouhin H. Tenectin, a novel extracellular matrix protein expressed during Drosophila melanogaster embryonic development. Gene Expr Patterns. 2006;6:772–776. - PubMed
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