MsrB1 and MICALs Regulate Actin Assembly and Macrophage Function via Reversible Stereoselective Methionine Oxidation

Byung Cheon Lee; Zalán Péterfi; Fu Kun W. Hoffmann; Richard E. Moore; Alaattin Kaya; Andrei Avanesov; Lionel Tarrago; Yani Zhou; Eranthie Weerapana; Dmitri E. Fomenko; Peter R. Hoffmann; Vadim N. Gladyshev

doi:10.1016/j.molcel.2013.06.019

MsrB1 and MICALs Regulate Actin Assembly and Macrophage Function via Reversible Stereoselective Methionine Oxidation

Byung Cheon Lee, Zalán Péterfi, Fu Kun W. Hoffmann, Richard E. Moore, Alaattin Kaya, Andrei Avanesov, Lionel Tarrago, Yani Zhou, Eranthie Weerapana, Dmitri E. Fomenko, Peter R. Hoffmann, Vadim N. Gladyshev

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185 Citations (Scopus)

Abstract

Redox control of protein function involves oxidation and reduction of amino acid residues, but the mechanisms and regulators involved are insufficiently understood. Here, we report that in conjunction with Mical proteins, methionine-. R-sulfoxide reductase B1 (MsrB1) regulates mammalian actin assembly via stereoselective methionine oxidation and reduction in a reversible, site-specific manner. Two methionine residues in actin are specifically converted to methionine-. R-sulfoxide by Mical1 and Mical2 and reduced back to methionine by selenoprotein MsrB1, supporting actin disassembly and assembly, respectively. Macrophages utilize this redox control during cellular activation by stimulating MsrB1 expression and activity as a part of innate immunity. We identified the regulatory role of MsrB1 as a Mical antagonist in orchestrating actin dynamics and macrophage function. More generally, our study shows that proteins can be regulated by reversible site-specific methionine-. R-sulfoxidation.

Original language	English
Pages (from-to)	397-404
Number of pages	8
Journal	Molecular Cell
Volume	51
Issue number	3
DOIs	https://doi.org/10.1016/j.molcel.2013.06.019
Publication status	Published - 2013 Aug 8
Externally published	Yes

Bibliographical note

Funding Information:
This research was supported by NIH grants AG021518, GM061603, RR017675, RR003061, P20RR016453, and AI089999.

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/j.molcel.2013.06.019

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Lee, B. C., Péterfi, Z., Hoffmann, F. K. W., Moore, R. E., Kaya, A., Avanesov, A., Tarrago, L., Zhou, Y., Weerapana, E., Fomenko, D. E., Hoffmann, P. R., & Gladyshev, V. N. (2013). MsrB1 and MICALs Regulate Actin Assembly and Macrophage Function via Reversible Stereoselective Methionine Oxidation. Molecular Cell, 51(3), 397-404. https://doi.org/10.1016/j.molcel.2013.06.019

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title = "MsrB1 and MICALs Regulate Actin Assembly and Macrophage Function via Reversible Stereoselective Methionine Oxidation",

abstract = "Redox control of protein function involves oxidation and reduction of amino acid residues, but the mechanisms and regulators involved are insufficiently understood. Here, we report that in conjunction with Mical proteins, methionine-. R-sulfoxide reductase B1 (MsrB1) regulates mammalian actin assembly via stereoselective methionine oxidation and reduction in a reversible, site-specific manner. Two methionine residues in actin are specifically converted to methionine-. R-sulfoxide by Mical1 and Mical2 and reduced back to methionine by selenoprotein MsrB1, supporting actin disassembly and assembly, respectively. Macrophages utilize this redox control during cellular activation by stimulating MsrB1 expression and activity as a part of innate immunity. We identified the regulatory role of MsrB1 as a Mical antagonist in orchestrating actin dynamics and macrophage function. More generally, our study shows that proteins can be regulated by reversible site-specific methionine-. R-sulfoxidation.",

author = "Lee, {Byung Cheon} and Zal{\'a}n P{\'e}terfi and Hoffmann, {Fu Kun W.} and Moore, {Richard E.} and Alaattin Kaya and Andrei Avanesov and Lionel Tarrago and Yani Zhou and Eranthie Weerapana and Fomenko, {Dmitri E.} and Hoffmann, {Peter R.} and Gladyshev, {Vadim N.}",

note = "Funding Information: This research was supported by NIH grants AG021518, GM061603, RR017675, RR003061, P20RR016453, and AI089999. ",

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AU - Lee, Byung Cheon

AU - Péterfi, Zalán

AU - Hoffmann, Fu Kun W.

AU - Moore, Richard E.

AU - Kaya, Alaattin

AU - Avanesov, Andrei

AU - Tarrago, Lionel

AU - Zhou, Yani

AU - Weerapana, Eranthie

AU - Fomenko, Dmitri E.

AU - Hoffmann, Peter R.

AU - Gladyshev, Vadim N.

N1 - Funding Information: This research was supported by NIH grants AG021518, GM061603, RR017675, RR003061, P20RR016453, and AI089999.

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Y1 - 2013/8/8

N2 - Redox control of protein function involves oxidation and reduction of amino acid residues, but the mechanisms and regulators involved are insufficiently understood. Here, we report that in conjunction with Mical proteins, methionine-. R-sulfoxide reductase B1 (MsrB1) regulates mammalian actin assembly via stereoselective methionine oxidation and reduction in a reversible, site-specific manner. Two methionine residues in actin are specifically converted to methionine-. R-sulfoxide by Mical1 and Mical2 and reduced back to methionine by selenoprotein MsrB1, supporting actin disassembly and assembly, respectively. Macrophages utilize this redox control during cellular activation by stimulating MsrB1 expression and activity as a part of innate immunity. We identified the regulatory role of MsrB1 as a Mical antagonist in orchestrating actin dynamics and macrophage function. More generally, our study shows that proteins can be regulated by reversible site-specific methionine-. R-sulfoxidation.

AB - Redox control of protein function involves oxidation and reduction of amino acid residues, but the mechanisms and regulators involved are insufficiently understood. Here, we report that in conjunction with Mical proteins, methionine-. R-sulfoxide reductase B1 (MsrB1) regulates mammalian actin assembly via stereoselective methionine oxidation and reduction in a reversible, site-specific manner. Two methionine residues in actin are specifically converted to methionine-. R-sulfoxide by Mical1 and Mical2 and reduced back to methionine by selenoprotein MsrB1, supporting actin disassembly and assembly, respectively. Macrophages utilize this redox control during cellular activation by stimulating MsrB1 expression and activity as a part of innate immunity. We identified the regulatory role of MsrB1 as a Mical antagonist in orchestrating actin dynamics and macrophage function. More generally, our study shows that proteins can be regulated by reversible site-specific methionine-. R-sulfoxidation.

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MsrB1 and MICALs Regulate Actin Assembly and Macrophage Function via Reversible Stereoselective Methionine Oxidation

Abstract

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