First published online September 28, 2007
Development 134, 2003e (2007)
© The Company of Biologists Limited
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.
Related articles in Development:
- 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]
