Cryo-EM structure of CtBP2 confirms tetrameric architecture.

Tytuł:: Cryo-EM structure of CtBP2 confirms tetrameric architecture.
Autorzy:: Jecrois AM; Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Dcona MM; Department of Internal Medicine, Virginia Commonwealth University, Richmond, VA 23298, USA.
Deng X; Department of Biostatistics, Virginia Commonwealth University, Richmond, VA 23298, USA.
Bandyopadhyay D; Department of Biostatistics, Virginia Commonwealth University, Richmond, VA 23298, USA; Massey Cancer Center, Virginia Commonwealth University, Richmond, VA 23298, USA.
Grossman SR; Department of Internal Medicine, Virginia Commonwealth University, Richmond, VA 23298, USA; Massey Cancer Center, Virginia Commonwealth University, Richmond, VA 23298, USA.
Schiffer CA; Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Royer WE Jr; Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA. Electronic address: .
Źródło:: Structure (London, England : 1993) [Structure] 2021 Apr 01; Vol. 29 (4), pp. 310-319.e5. Date of Electronic Publication: 2020 Dec 01.
Typ publikacji:: Journal Article; Research Support, N.I.H., Extramural
Język:: English
Imprint Name(s):: Publication: 2000- : Cambridge, Mass. : Cell Press
Original Publication: London : Current Biology, c1993-
MeSH Terms:: Protein Multimerization*
Alcohol Oxidoreductases/*chemistry
Co-Repressor Proteins/*chemistry
DNA-Binding Proteins/*chemistry
Alcohol Oxidoreductases/genetics ; Alcohol Oxidoreductases/metabolism ; Cadherins/metabolism ; Catalytic Domain ; Cell Movement ; Co-Repressor Proteins/genetics ; Co-Repressor Proteins/metabolism ; Cryoelectron Microscopy ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation, Neoplastic ; HCT116 Cells ; Humans ; Mutation ; NADP/metabolism ; Protein Binding ; T-Lymphoma Invasion and Metastasis-inducing Protein 1/metabolism
References:: Nat Methods. 2014 Jan;11(1):63-5. (PMID: 24213166)
Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21. (PMID: 20057044)
Neoplasia. 2012 Oct;14(10):905-14. (PMID: 23097625)
Oncogene. 2013 Aug 15;32(33):3896-903. (PMID: 22945647)
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21. (PMID: 20124702)
Elife. 2018 Nov 09;7:. (PMID: 30412051)
Cell Mol Life Sci. 2016 Dec;73(23):4493-4515. (PMID: 27392607)
J Invest Dermatol. 2013 May;133(5):1294-301. (PMID: 23303449)
J Biol Chem. 2018 Jun 8;293(23):9101-9112. (PMID: 29700119)
Chem Biol. 2015 May 21;22(5):583-92. (PMID: 25937312)
Mol Cell Biol. 2008 Jan;28(1):269-81. (PMID: 17967884)
Cancer Res. 2009 Feb 1;69(3):731-4. (PMID: 19155295)
Nature. 2003 Apr 17;422(6933):735-8. (PMID: 12700765)
Biochem Biophys Res Commun. 2018 Jan 8;495(2):1980-1985. (PMID: 29225171)
Mol Cell Biol. 2002 Aug;22(15):5296-307. (PMID: 12101226)
Bioessays. 2001 Aug;23(8):683-90. (PMID: 11494316)
Nat Methods. 2017 Aug;14(8):793-796. (PMID: 28671674)
Nat Rev Mol Cell Biol. 2018 Apr;19(4):262-274. (PMID: 29209056)
EMBO J. 2003 Jun 16;22(12):3122-30. (PMID: 12805226)
Biochem Biophys Res Commun. 2009 Mar 27;381(1):70-4. (PMID: 19351597)
J Comput Chem. 2004 Oct;25(13):1605-12. (PMID: 15264254)
Elife. 2018 Mar 07;7:. (PMID: 29513216)
Apoptosis. 2006 Jun;11(6):879-88. (PMID: 16547590)
Phys Rev Lett. 2009 Mar 20;102(11):118106. (PMID: 19392244)
Mol Cell. 2002 Oct;10(4):857-69. (PMID: 12419229)
Nat Commun. 2013;4:1449. (PMID: 23385593)
Science. 2002 Mar 8;295(5561):1895-7. (PMID: 11847309)
Bioinformatics. 2015 May 1;31(9):1484-6. (PMID: 25540183)
Curr Opin Genet Dev. 2005 Apr;15(2):136-44. (PMID: 15797196)
Protein Sci. 2006 May;15(5):1042-50. (PMID: 16597837)
ACS Chem Biol. 2015 Apr 17;10(4):1118-27. (PMID: 25636004)
Nat Protoc. 2008;3(6):1101-8. (PMID: 18546601)
EMBO J. 1993 Feb;12(2):469-78. (PMID: 8440238)
Oncogenesis. 2019 Oct 4;8(10):55. (PMID: 31586042)
FEBS Lett. 2014 May 2;588(9):1743-8. (PMID: 24657618)
J Mol Biol. 2007 Sep 21;372(3):774-97. (PMID: 17681537)
Science. 2011 May 6;332(6030):680-6. (PMID: 21551057)
Oncotarget. 2018 Aug 21;9(65):32408-32418. (PMID: 30197752)
Mol Pharmacol. 2019 Jul;96(1):99-108. (PMID: 31036695)
J Struct Biol. 2005 Oct;152(1):36-51. (PMID: 16182563)
Cancer Biol Ther. 2017 Jun 3;18(6):379-391. (PMID: 28532298)
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32. (PMID: 15572765)
Biochem Biophys Res Commun. 2020 Mar 5;523(2):354-360. (PMID: 31866012)
Methods Enzymol. 2016;579:191-226. (PMID: 27572728)
J Biol Chem. 2013 Sep 27;288(39):27836-48. (PMID: 23940047)
Protein Sci. 2013 Apr;22(4):510-5. (PMID: 23389845)
FEBS Lett. 2007 Nov 13;581(27):5241-6. (PMID: 17964573)
Nucleic Acids Res. 2004 Mar 22;32(5):1836-47. (PMID: 15037661)
Oncotarget. 2015 Feb 28;6(6):3752-69. (PMID: 25686837)
J Struct Biol. 1996 Jan-Feb;116(1):71-6. (PMID: 8742726)
Int J Biochem Cell Biol. 2007;39(9):1593-607. (PMID: 17336131)
Proc Natl Acad Sci U S A. 2003 Apr 15;100(8):4568-73. (PMID: 12676992)
Genes Cancer. 2012 Jul;3(7-8):481-90. (PMID: 23264848)
Grant Information:: F31 GM129988 United States GM NIGMS NIH HHS; P30 CA016059 United States CA NCI NIH HHS; R01 GM119014 United States GM NIGMS NIH HHS
Contributed Indexing:: Keywords: C-terminal binding-protein CtBP; TIAM1; cancer; metastasis; tetrameric assembly; transcription regulation
Substance Nomenclature:: 0 (Cadherins)
0 (Co-Repressor Proteins)
0 (DNA-Binding Proteins)
0 (T-Lymphoma Invasion and Metastasis-inducing Protein 1)
0 (TIAM1 protein, human)
53-59-8 (NADP)
EC 1.1.- (Alcohol Oxidoreductases)
EC 1.1.- (CTBP2 protein, human)
EC 1.1.1.- (C-terminal binding protein)
Entry Date(s):: Date Created: 20201202 Date Completed: 20211123 Latest Revision: 20220716
Update Code:: 20240105
PubMed Central ID:: PMC9159756
DOI:: 10.1016/j.str.2020.11.008
PMID:: 33264605
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C-terminal binding proteins 1 and 2 (CtBP1 and CtBP2) are transcriptional regulators that activate or repress many genes involved in cellular development, apoptosis, and metastasis. NADH-dependent CtBP activation has been implicated in multiple types of cancer and poor patient prognosis. Central to understanding activation of CtBP in oncogenesis is uncovering how NADH triggers protein assembly, what level of assembly occurs, and if oncogenic activity depends upon such assembly. Here, we present the cryoelectron microscopic structures of two different constructs of CtBP2 corroborating that the native state of CtBP2 in the presence of NADH is tetrameric. The physiological relevance of the observed tetramer was demonstrated in cell culture, showing that CtBP tetramer-destabilizing mutants are defective for cell migration, transcriptional repression of E-cadherin, and activation of TIAM1. Together with our cryoelectron microscopy studies, these results highlight the tetramer as the functional oligomeric form of CtBP2.
Competing Interests: Declaration of interests The authors declare no competing interests.
(Copyright © 2020 Elsevier Ltd. All rights reserved.)

Comment in: Structure. 2021 Apr 1;29(4):307-309. (PMID: 33798426)

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