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Updated: Jul 14, 2026
12:08
Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
MICAL flavoprotein monooxygenases: structure, function and role in semaphorin signaling
Sharon M Kolk1, R Jeroen Pasterkamp
1Department of Pharmacology and Anatomy, Rudolf Magnus Institute of Neuroscience, University Medical Center Utrecht, Universiteitsweg 100, 3584 CG Utrecht, The Netherlands.
Advances in Experimental Medicine and Biology
|July 5, 2007
Summary
Molecule Interacting with CasL (MICALs) are signaling proteins crucial for axonal pathfinding. Their flavoenzyme activity is vital for repulsive axon guidance mediated by semaphorin/plexin signaling in Drosophila.
Area of Science:
- Molecular Biology
- Neuroscience
- Cell Signaling
Background:
- MICALs (Molecule Interacting with CasL) are conserved signal transduction proteins.
- They possess domains for cytoskeletal interaction and a flavoprotein monooxygenase enzymatic domain.
- MICALs are implicated in various cellular processes, notably axonal pathfinding.
Purpose of the Study:
- To review the current understanding of MICAL proteins.
- To emphasize the role of MICALs in semaphorin signaling during axonal pathfinding.
Main Methods:
- Literature review of MICALs function.
- Analysis of mutagenesis and pharmacological inhibitor studies.
- Focus on Drosophila neuromuscular system models.
Main Results:
- MICALs bind the axon guidance receptor Plexin A.
- They transduce semaphorin-1a-mediated repulsive axon guidance.
- MICAL flavoenzyme redox functions are critical for this process.
Conclusions:
- MICALs play a significant role in axonal pathfinding via semaphorin/plexin signaling.
- The enzymatic activity of MICALs is essential for their function in axon guidance.
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