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First published online September 28, 2007

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Hh signals break up

In Drosophila, when Hh binds to its receptor Ptc, Ptc releases its inhibition of Smo, resulting in Smo's phosphorylation and stabilization at the plasma membrane. Smo then transmits a signal to a multi-protein complex that contains the kinase Fu, the kinesin-like Cos2 and the Gli-like transcription factor Ci. In their investigation of Cos2's role in Hh signalling in Drosophila on p. 3677, Pascal Thérond's lab report that the phosphorylation of Cos2 by Fu induces it to undergo a conformational change that leads to this complex's disassembly, probably to free Ci to translocate to the nucleus to activate target genes. Their findings show that the Cos2 residue Ser572 is necessary for Hh signal transduction and is phosphorylated by Fu, either directly or indirectly. By using an antibody that specifically recognizes phosphorylated Ser572, the authors show that upon its phosphorylation, Cos2's association with Smo and Ci strongly decreases in vivo and in vitro. This study's results provide new mechanistic insights into Hh signal transduction, about which much remains unknown.

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Phosphorylation of the atypical kinesin Costal2 by the kinase Fused induces the partial disassembly of the Smoothened-Fused-Costal2-Cubitus interruptus complex in Hedgehog signalling

Laurent Ruel, Armel Gallet, Sophie Raisin, Arnaud Truchi, Laurence Staccini-Lavenant, Alexandra Cervantes, and Pascal P. Thérond
Development 2007 134: 3677-3689. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in Development Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?