MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation.
MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation.
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MSRB1和Micals通过可逆的立体选择性蛋氨酸氧化来调节肌动蛋白的组装和巨噬细胞功能。
DOI:
10.1016/j.molcel.2013.06.019
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发表时间:
2013-08-08
期刊:
影响因子:
16
通讯作者:
Gladyshev, Vadim N.
中科院分区:
文献类型:
--
作者:
Lee, Byung Cheon;Peterfi, Zalan;Hoffmann, Fukun W.;Moore, Richard E.;Kaya, Alaattin;Avanesov, Andrei;Tarrago, Lionel;Zhou, Yani;Weerapana, Eranthie;Fomenko, Dmitri E.;Hoffmann, Peter R.;Gladyshev, Vadim N.
Redox control of protein function involves oxidation and reduction of amino acid residues, but mechanisms and regulators involved are insufficiently understood. Here, we report that methionine-R-sulfoxide reductase B1 (MsrB1) regulates, in conjunction with Mical proteins, 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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影响因子:
7.4
作者:
Lim, Jung Chae;Kim, Geumsoo;Levine, Rodney L.
通讯作者:
Levine, Rodney L.
影响因子:
64.8
作者:
通讯作者:
--
DOI:
10.1016/j.bbagen.2009.04.014
发表时间:
2009-11
期刊:
Biochimica et biophysica acta
影响因子:
--
作者:
Lee BC;Dikiy A;Kim HY;Gladyshev VN
通讯作者:
Gladyshev VN
DOI:
10.1038/nrm3255
发表时间:
2011-12-22
期刊:
Nature reviews. Molecular cell biology
影响因子:
--
作者:
通讯作者:
--
影响因子:
4.8
作者:
Fomenko, Dmitri E.;Novoselov, Sergey V.;Gladyshev, Vadim N.
通讯作者:
Gladyshev, Vadim N.