Characterizing F-actin disassembly induced by the semaphorin-signaling component MICAL

Jimok Yoon, Ruei Jiun Hung, Jonathan R. Terman

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)119-128
Number of pages10
JournalMethods in Molecular Biology
Volume1493
DOIs
StatePublished - 2017

Keywords

  • Actin sedimentation
  • F-actin disassembly
  • MICALs
  • Oxidoreductase
  • Plexin
  • Pyrene-actin

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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