GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
TableEdit
PMID:18077144
You don't have sufficient rights on this wiki to edit tables. Perhaps you need to log in. Changes you make in the Table editor will not be saved back to the wiki
See Help for Help on this wiki. See the documentation for how to use the table editor
Citation |
Bickel, D, Shah, R, Gesualdi, SC and Haerry, TE Drosophila Follistatin exhibits unique structural modifications and interacts with several TGF-beta family members. Mech. Dev. 125:117-29 |
---|---|
Abstract |
Follistatin (FS) is one of several secreted proteins that modulate the activity of TGF-beta family members during development. The structural and functional analysis of Drosophila Follistatin (dFS) reveals important differences between dFS and its vertebrate orthologues: it is larger, more positively charged, and proteolytically processed. dFS primarily inhibits signaling of Drosophila Activin (dACT) but can also inhibit other ligands like Decapentaplegic (DPP). In contrast, the presence of dFS enhances signaling of the Activin-like protein Dawdle (DAW), indicating that dFS exhibits a dual function in promoting and inhibiting signaling of TGF-beta ligands. In addition, FS proteins may also function in facilitating ligand diffusion. We find that mutants of daw are rescued in significant numbers by expression of vertebrate FS proteins. Since two PiggyBac insertions in dfs are not lethal, it appears that the function of dFS is non-essential or functionally redundant. |
Links |
PubMed PMC2278114 Online version:10.1016/j.mod.2007.09.013 |
Keywords |
Animals; Base Sequence; DNA Primers; Drosophila; Follistatin/chemistry; Follistatin/genetics; Follistatin/metabolism; Hydrolysis; Immunohistochemistry; In Situ Hybridization; Ligands; Phenotype; Protein Binding; Protein Conformation; Transforming Growth Factor beta/metabolism |
public |
Cancel |