Co-regulation of the transcription controlling ATF2 phosphoswitch by JNK and p38.

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Tytuł:: Co-regulation of the transcription controlling ATF2 phosphoswitch by JNK and p38.
Autorzy:: Kirsch K; Biomolecular Interactions Research Group, Institute of Organic Chemistry, Research Center for Natural Sciences, H-1117, Budapest, Hungary.
Zeke A; Biomolecular Interactions Research Group, Institute of Organic Chemistry, Research Center for Natural Sciences, H-1117, Budapest, Hungary.
Tőke O; Laboratory for NMR Spectroscopy, Research Center for Natural Sciences, H-1117, Budapest, Hungary.
Sok P; Biomolecular Interactions Research Group, Institute of Organic Chemistry, Research Center for Natural Sciences, H-1117, Budapest, Hungary.
Sethi A; Department of Biochemistry and Molecular Biology and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.
Sebő A; Biomolecular Interactions Research Group, Institute of Organic Chemistry, Research Center for Natural Sciences, H-1117, Budapest, Hungary.
Kumar GS; Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, USA.
Egri P; Biomolecular Interactions Research Group, Institute of Organic Chemistry, Research Center for Natural Sciences, H-1117, Budapest, Hungary.
Póti ÁL; Biomolecular Interactions Research Group, Institute of Organic Chemistry, Research Center for Natural Sciences, H-1117, Budapest, Hungary.
Gooley P; Department of Biochemistry and Molecular Biology and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.
Peti W; Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, USA.
Bento I; European Molecular Biology Laboratory, Hamburg, Germany.
Alexa A; Biomolecular Interactions Research Group, Institute of Organic Chemistry, Research Center for Natural Sciences, H-1117, Budapest, Hungary.
Reményi A; Biomolecular Interactions Research Group, Institute of Organic Chemistry, Research Center for Natural Sciences, H-1117, Budapest, Hungary. .
Źródło:: Nature communications [Nat Commun] 2020 Nov 13; Vol. 11 (1), pp. 5769. Date of Electronic Publication: 2020 Nov 13.
Typ publikacji:: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Original Publication: [London] : Nature Pub. Group
MeSH Terms:: Gene Expression Regulation*
Transcription, Genetic*
Activating Transcription Factor 2/*metabolism
JNK Mitogen-Activated Protein Kinases/*metabolism
p38 Mitogen-Activated Protein Kinases/*metabolism
Activating Transcription Factor 2/chemistry ; Amino Acid Motifs ; Amino Acid Sequence ; HEK293 Cells ; Humans ; Luciferases/metabolism ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Phosphorylation ; Protein Binding ; Zinc Fingers
References:: Bioinformatics. 2015 Apr 15;31(8):1325-7. (PMID: 25505092)
J Mol Biol. 1999 Apr 2;287(3):593-607. (PMID: 10092462)
Nature. 1991 Dec 12;354(6353):494-6. (PMID: 1749429)
EMBO J. 2006 Mar 8;25(5):1058-69. (PMID: 16511568)
Nat Rev Cancer. 2009 Aug;9(8):537-49. (PMID: 19629069)
PLoS Comput Biol. 2017 Mar 27;13(3):e1005462. (PMID: 28346509)
EMBO J. 1992 Jul;11(7):2415-24. (PMID: 1628615)
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674. (PMID: 19461840)
Sci Signal. 2012 Oct 09;5(245):ra74. (PMID: 23047924)
Pharmacol Res. 2017 May;119:347-357. (PMID: 28212892)
Structure. 2012 Dec 5;20(12):2174-84. (PMID: 23142346)
Mol Cell. 2004 Apr 9;14(1):43-55. (PMID: 15068802)
Nature. 1996 Jan 18;379(6562):262-5. (PMID: 8538792)
Methods. 2011 Sep;55(1):94-106. (PMID: 21821126)
Proc Natl Acad Sci U S A. 2018 May 1;115(18):4655-4660. (PMID: 29666261)
EMBO J. 1995 Apr 18;14(8):1785-97. (PMID: 7737129)
FEBS J. 2007 Feb;274(3):783-90. (PMID: 17288558)
Bioinformatics. 2016 Nov 1;32(21):3366-3368. (PMID: 27402907)
Microbiol Mol Biol Rev. 2016 Jul 27;80(3):793-835. (PMID: 27466283)
J Mol Biol. 1993 Dec 5;234(3):779-815. (PMID: 8254673)
FEBS Lett. 2004 Aug 13;572(1-3):177-83. (PMID: 15304344)
Cell Mol Life Sci. 2000 Aug;57(8-9):1172-83. (PMID: 11028910)
Genes Dev. 1993 Nov;7(11):2135-48. (PMID: 8224842)
J Mol Biol. 2001 Jun 15;309(4):961-74. (PMID: 11399072)
Nature. 2011 Nov 13;480(7377):383-6. (PMID: 22080951)
ACS Chem Biol. 2016 Feb 19;11(2):400-8. (PMID: 26569370)
Mol Cell Biol. 1996 Mar;16(3):1247-55. (PMID: 8622669)
Genes Dev. 1996 Sep 15;10(18):2276-88. (PMID: 8824587)
Nat Commun. 2016 Mar 18;7:10879. (PMID: 26988444)
iScience. 2019 Sep 27;19:1012-1036. (PMID: 31522114)
J Biomol NMR. 1995 Nov;6(3):277-93. (PMID: 8520220)
Sci Rep. 2015 Jun 08;5:11127. (PMID: 26054059)
Protein Sci. 2006 Dec;15(12):2795-804. (PMID: 17088319)
Genes Dev. 1999 Jan 15;13(2):163-75. (PMID: 9925641)
J Mol Biol. 2012 Dec 14;424(5):339-53. (PMID: 23079240)
J Mol Biol. 2016 Feb 22;428(4):720-725. (PMID: 26410586)
Structure. 2013 Jun 4;21(6):986-96. (PMID: 23665168)
J Biol Chem. 2008 Jul 11;283(28):19511-20. (PMID: 18482985)
Science. 2016 Oct 14;354(6309):233-237. (PMID: 27738173)
J Biol Chem. 2013 Mar 22;288(12):8596-609. (PMID: 23382384)
J Biol Chem. 2013 Jul 5;288(27):19537-47. (PMID: 23671282)
Mol Syst Biol. 2015 Nov 03;11(11):837. (PMID: 26538579)
Science. 1995 Jan 20;267(5196):389-93. (PMID: 7824938)
Mol Biol Cell. 2005 Jun;16(6):2934-46. (PMID: 15788564)
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501. (PMID: 20383002)
Int J Mol Sci. 2020 Feb 07;21(3):. (PMID: 32046099)
Oncogene. 1999 Apr 8;18(14):2311-21. (PMID: 10327051)
Org Biomol Chem. 2004 Jan 7;2(1):142-9. (PMID: 14737674)
J Biol Chem. 2001 Feb 23;276(8):5676-84. (PMID: 11069918)
Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):10952-6. (PMID: 8248197)
Trends Biochem Sci. 2000 Sep;25(9):448-53. (PMID: 10973059)
Arch Toxicol. 2015 Jun;89(6):867-82. (PMID: 25690731)
Nat Rev Mol Cell Biol. 2002 Jan;3(1):30-40. (PMID: 11823796)
Science. 2002 Apr 26;296(5568):755-8. (PMID: 11934987)
Substance Nomenclature:: 0 (Activating Transcription Factor 2)
EC 1.13.12.- (Luciferases)
EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases)
EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases)
Entry Date(s):: Date Created: 20201114 Date Completed: 20201124 Latest Revision: 20240108
Update Code:: 20240108
PubMed Central ID:: PMC7666158
DOI:: 10.1038/s41467-020-19582-3
PMID:: 33188182
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Transcription factor phosphorylation at specific sites often activates gene expression, but how environmental cues quantitatively control transcription is not well-understood. Activating protein 1 transcription factors are phosphorylated by mitogen-activated protein kinases (MAPK) in their transactivation domains (TAD) at so-called phosphoswitches, which are a hallmark in response to growth factors, cytokines or stress. We show that the ATF2 TAD is controlled by functionally distinct signaling pathways (JNK and p38) through structurally different MAPK binding sites. Moreover, JNK mediated phosphorylation at an evolutionarily more recent site diminishes p38 binding and made the phosphoswitch differently sensitive to JNK and p38 in vertebrates. Structures of MAPK-TAD complexes and mechanistic modeling of ATF2 TAD phosphorylation in cells suggest that kinase binding motifs and phosphorylation sites line up to maximize MAPK based co-regulation. This study shows how the activity of an ancient transcription controlling phosphoswitch became dependent on the relative flux of upstream signals.

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