TY - JOUR
T1 - Direct redox regulation of F-actin assembly and disassembly by Mical
AU - Hung, Ruei Jiun
AU - Pak, Chi W.
AU - Terman, Jonathan R.
PY - 2011/12/23
Y1 - 2011/12/23
N2 - Different types of cell behavior, including growth, motility, and navigation, require actin proteins to assemble into filaments. Here, we describe a biochemical process that was able to disassemble actin filaments and limit their reassembly. Actin was a specific substrate of the multidomain oxidation-reduction enzyme, Mical, a poorly understood actin disassembly factor that directly responds to Semaphorin/Plexin extracellular repulsive cues. Actin filament subunits were directly modified by Mical on their conserved pointed-end, which is critical for filament assembly. Mical posttranslationally oxidized the methionine 44 residue within the D-loop of actin, simultaneously severing filaments and decreasing polymerization. This mechanism underlying actin cytoskeletal collapse may have broad physiological and pathological ramifications.
AB - Different types of cell behavior, including growth, motility, and navigation, require actin proteins to assemble into filaments. Here, we describe a biochemical process that was able to disassemble actin filaments and limit their reassembly. Actin was a specific substrate of the multidomain oxidation-reduction enzyme, Mical, a poorly understood actin disassembly factor that directly responds to Semaphorin/Plexin extracellular repulsive cues. Actin filament subunits were directly modified by Mical on their conserved pointed-end, which is critical for filament assembly. Mical posttranslationally oxidized the methionine 44 residue within the D-loop of actin, simultaneously severing filaments and decreasing polymerization. This mechanism underlying actin cytoskeletal collapse may have broad physiological and pathological ramifications.
UR - http://www.scopus.com/inward/record.url?scp=84455205549&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84455205549&partnerID=8YFLogxK
U2 - 10.1126/science.1211956
DO - 10.1126/science.1211956
M3 - Article
C2 - 22116028
AN - SCOPUS:84455205549
SN - 0036-8075
VL - 334
SP - 1710
EP - 1713
JO - Science
JF - Science
IS - 6063
ER -