Direct redox regulation of F-actin assembly and disassembly by Mical

Ruei Jiun Hung, Chi W. Pak, Jonathan R. Terman

Research output: Contribution to journalArticle

149 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1710-1713
Number of pages4
JournalScience
Volume334
Issue number6063
DOIs
StatePublished - Dec 23 2011

Fingerprint

Oxidation-Reduction
Actins
Actin Cytoskeleton
Biochemical Phenomena
Semaphorins
Polymerization
Methionine
Cues
Enzymes
Growth
Proteins

ASJC Scopus subject areas

  • General

Cite this

Direct redox regulation of F-actin assembly and disassembly by Mical. / Hung, Ruei Jiun; Pak, Chi W.; Terman, Jonathan R.

In: Science, Vol. 334, No. 6063, 23.12.2011, p. 1710-1713.

Research output: Contribution to journalArticle

Hung, Ruei Jiun ; Pak, Chi W. ; Terman, Jonathan R. / Direct redox regulation of F-actin assembly and disassembly by Mical. In: Science. 2011 ; Vol. 334, No. 6063. pp. 1710-1713.
@article{01bc464dc08647ef8fde6d76bb6b8f13,
title = "Direct redox regulation of F-actin assembly and disassembly by Mical",
abstract = "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.",
author = "Hung, {Ruei Jiun} and Pak, {Chi W.} and Terman, {Jonathan R.}",
year = "2011",
month = "12",
day = "23",
doi = "10.1126/science.1211956",
language = "English (US)",
volume = "334",
pages = "1710--1713",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6063",

}

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

VL - 334

SP - 1710

EP - 1713

JO - Science

JF - Science

SN - 0036-8075

IS - 6063

ER -