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Identification of a tetrameric hedgehog signaling complex.
M A Stegman1, J E Vallance, G Elangovan
1Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267-0524, USA.
The Journal of Biological Chemistry
|May 29, 2000
Summary
The Hedgehog signaling complex forms a trimer of Costal2, Fused, and Cubitus interruptus. Suppressor of Fused binds this complex but is not essential for its function in Drosophila.
Area of Science:
- Cellular Biology
- Molecular Biology
- Genetics
Background:
- Hedgehog (Hh) signal transduction relies on a large cytoplasmic protein complex.
- This complex interacts with microtubules in an Hh-dependent manner.
Purpose of the Study:
- To investigate the composition and regulation of the Hh signaling complex.
- To determine the role of Suppressor of Fused (Su(fu)) in Hh complex formation and function.
Main Methods:
- Co-immunoprecipitation assays to identify protein interactions.
- Analysis of protein complex formation in Drosophila mutants.
- Microscopy to assess complex localization.
Main Results:
- Costal2 (Cos2), Fused (Fu), and Cubitus interruptus (Ci) form a direct trimeric complex.
- Suppressor of Fused (Su(fu)) forms a separate tetrameric complex with Cos2, Fu, and Ci, but is not required for Hh signaling.
- Ci translocates to the nucleus upon Hh stimulation, dissociating from cytoplasmic partners like Su(fu).
Conclusions:
- Su(fu) and Cos2 may redundantly regulate Ci's cytoplasmic retention via interactions with Fu.
- Su(fu) is not essential for Hh signal transduction but modulates the pathway through complex interactions.