Actin filaments—A target for redox regulation

Carlos Wilson, Jonathan R. Terman, Christian González-Billault, Giasuddin Ahmed

Research output: Contribution to journalReview article

26 Citations (Scopus)

Abstract

Actin and its ability to polymerize into dynamic filaments is critical for the form and function of cells throughout the body. While multiple proteins have been characterized as affecting actin dynamics through noncovalent means, actin and its protein regulators are also susceptible to covalent modifications of their amino acid residues. In this regard, oxidation-reduction (Redox) intermediates have emerged as key modulators of the actin cytoskeleton with multiple different effects on cellular form and function. Here, we review work implicating Redox intermediates in post-translationally altering actin and discuss what is known regarding how these alterations affect the properties of actin. We also focus on two of the best characterized enzymatic sources of these Redox intermediates—the NADPH oxidase NOX and the flavoprotein monooxygenase MICAL—and detail how they have both been identified as altering actin, but share little similarity and employ different means to regulate actin dynamics. Finally, we discuss the role of these enzymes and redox signaling in regulating the actin cytoskeleton in vivo and highlight their importance for neuronal form and function in health and disease.

Original languageEnglish (US)
Pages (from-to)577-595
Number of pages19
JournalCytoskeleton
Volume73
Issue number10
DOIs
StatePublished - Oct 1 2016

Fingerprint

Oxidation-Reduction
Actins
Actin Cytoskeleton
Flavoproteins
NADPH Oxidase
Mixed Function Oxygenases
Proteins
Amino Acids
Health
Enzymes

Keywords

  • actin
  • MICAL
  • NADPH oxidase
  • post-translational modification
  • redox

ASJC Scopus subject areas

  • Structural Biology
  • Cell Biology

Cite this

Wilson, C., Terman, J. R., González-Billault, C., & Ahmed, G. (2016). Actin filaments—A target for redox regulation. Cytoskeleton, 73(10), 577-595. https://doi.org/10.1002/cm.21315

Actin filaments—A target for redox regulation. / Wilson, Carlos; Terman, Jonathan R.; González-Billault, Christian; Ahmed, Giasuddin.

In: Cytoskeleton, Vol. 73, No. 10, 01.10.2016, p. 577-595.

Research output: Contribution to journalReview article

Wilson, C, Terman, JR, González-Billault, C & Ahmed, G 2016, 'Actin filaments—A target for redox regulation', Cytoskeleton, vol. 73, no. 10, pp. 577-595. https://doi.org/10.1002/cm.21315
Wilson C, Terman JR, González-Billault C, Ahmed G. Actin filaments—A target for redox regulation. Cytoskeleton. 2016 Oct 1;73(10):577-595. https://doi.org/10.1002/cm.21315
Wilson, Carlos ; Terman, Jonathan R. ; González-Billault, Christian ; Ahmed, Giasuddin. / Actin filaments—A target for redox regulation. In: Cytoskeleton. 2016 ; Vol. 73, No. 10. pp. 577-595.
@article{d20adcdbe4034c09b727cd2bf5f71972,
title = "Actin filaments—A target for redox regulation",
abstract = "Actin and its ability to polymerize into dynamic filaments is critical for the form and function of cells throughout the body. While multiple proteins have been characterized as affecting actin dynamics through noncovalent means, actin and its protein regulators are also susceptible to covalent modifications of their amino acid residues. In this regard, oxidation-reduction (Redox) intermediates have emerged as key modulators of the actin cytoskeleton with multiple different effects on cellular form and function. Here, we review work implicating Redox intermediates in post-translationally altering actin and discuss what is known regarding how these alterations affect the properties of actin. We also focus on two of the best characterized enzymatic sources of these Redox intermediates—the NADPH oxidase NOX and the flavoprotein monooxygenase MICAL—and detail how they have both been identified as altering actin, but share little similarity and employ different means to regulate actin dynamics. Finally, we discuss the role of these enzymes and redox signaling in regulating the actin cytoskeleton in vivo and highlight their importance for neuronal form and function in health and disease.",
keywords = "actin, MICAL, NADPH oxidase, post-translational modification, redox",
author = "Carlos Wilson and Terman, {Jonathan R.} and Christian Gonz{\'a}lez-Billault and Giasuddin Ahmed",
year = "2016",
month = "10",
day = "1",
doi = "10.1002/cm.21315",
language = "English (US)",
volume = "73",
pages = "577--595",
journal = "Cytoskeleton",
issn = "1949-3584",
publisher = "Wiley-Liss Inc.",
number = "10",

}

TY - JOUR

T1 - Actin filaments—A target for redox regulation

AU - Wilson, Carlos

AU - Terman, Jonathan R.

AU - González-Billault, Christian

AU - Ahmed, Giasuddin

PY - 2016/10/1

Y1 - 2016/10/1

N2 - Actin and its ability to polymerize into dynamic filaments is critical for the form and function of cells throughout the body. While multiple proteins have been characterized as affecting actin dynamics through noncovalent means, actin and its protein regulators are also susceptible to covalent modifications of their amino acid residues. In this regard, oxidation-reduction (Redox) intermediates have emerged as key modulators of the actin cytoskeleton with multiple different effects on cellular form and function. Here, we review work implicating Redox intermediates in post-translationally altering actin and discuss what is known regarding how these alterations affect the properties of actin. We also focus on two of the best characterized enzymatic sources of these Redox intermediates—the NADPH oxidase NOX and the flavoprotein monooxygenase MICAL—and detail how they have both been identified as altering actin, but share little similarity and employ different means to regulate actin dynamics. Finally, we discuss the role of these enzymes and redox signaling in regulating the actin cytoskeleton in vivo and highlight their importance for neuronal form and function in health and disease.

AB - Actin and its ability to polymerize into dynamic filaments is critical for the form and function of cells throughout the body. While multiple proteins have been characterized as affecting actin dynamics through noncovalent means, actin and its protein regulators are also susceptible to covalent modifications of their amino acid residues. In this regard, oxidation-reduction (Redox) intermediates have emerged as key modulators of the actin cytoskeleton with multiple different effects on cellular form and function. Here, we review work implicating Redox intermediates in post-translationally altering actin and discuss what is known regarding how these alterations affect the properties of actin. We also focus on two of the best characterized enzymatic sources of these Redox intermediates—the NADPH oxidase NOX and the flavoprotein monooxygenase MICAL—and detail how they have both been identified as altering actin, but share little similarity and employ different means to regulate actin dynamics. Finally, we discuss the role of these enzymes and redox signaling in regulating the actin cytoskeleton in vivo and highlight their importance for neuronal form and function in health and disease.

KW - actin

KW - MICAL

KW - NADPH oxidase

KW - post-translational modification

KW - redox

UR - http://www.scopus.com/inward/record.url?scp=84982071006&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84982071006&partnerID=8YFLogxK

U2 - 10.1002/cm.21315

DO - 10.1002/cm.21315

M3 - Review article

C2 - 27309342

AN - SCOPUS:84982071006

VL - 73

SP - 577

EP - 595

JO - Cytoskeleton

JF - Cytoskeleton

SN - 1949-3584

IS - 10

ER -