The MICALs are a family of phylogenetically conserved cytoplasmic proteins that modulate numerous cellular behaviors and play critical roles in semaphorin-plexin signaling. Our recent results have revealed that the MICALs are an unusual family of actin regulatory proteins that use actin filaments (F-actin) as a direct substrate-controlling F-actin dynamics via stereospecific oxidation of conserved methionine (Met44 and Met47) residues within actin. In particular, the MICALs have a highly conserved flavoprotein monooxygenase (redox) enzymatic domain in their N-terminus that directly oxidizes and destabilizes F-actin. Here, we describe methods to characterize MICAL-mediated F-actin disassembly using in vitro assays with purified proteins.
Jimok Yoon, Ruei-Jiun Hung, Jonathan R Terman. Characterizing F-actin Disassembly Induced by the Semaphorin-Signaling Component MICAL. Methods in molecular biology (Clifton, N.J.). 2017;1493:119-128
PMID: 27787846
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