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Article ; Online: A Role for SMARCB1 in Synovial Sarcomagenesis Reveals That SS18-SSX Induces Canonical BAF Destruction.

Li, Jinxiu / Mulvihill, Timothy S / Li, Li / Barrott, Jared J / Nelson, Mary L / Wagner, Lena / Lock, Ian C / Pozner, Amir / Lambert, Sydney Lynn / Ozenberger, Benjamin B / Ward, Michael B / Grossmann, Allie H / Liu, Ting / Banito, Ana / Cairns, Bradley R / Jones, Kevin B

Cancer discovery

2021 Volume 11, Issue 10, Page(s) 2620–2637

Abstract: Reduced protein levels of SMARCB1 (also known as BAF47, INI1, SNF5) have long been observed in synovial sarcoma. Here, we show that ... ...

Abstract	Reduced protein levels of SMARCB1 (also known as BAF47, INI1, SNF5) have long been observed in synovial sarcoma. Here, we show that combined
MeSH term(s)	Animals ; Cell Line, Tumor ; Cell Transformation, Neoplastic ; Disease Models, Animal ; Female ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Oncogene Proteins, Fusion/genetics ; SMARCB1 Protein/genetics ; Sarcoma, Synovial/genetics ; Sarcoma, Synovial/pathology
Chemical Substances	Oncogene Proteins, Fusion ; SMARCB1 Protein ; SMARCB1 protein, human ; SS18-SSX1 fusion protein
Language	English
Publishing date	2021-06-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2625242-9
ISSN	2159-8290 ; 2159-8274
ISSN (online)	2159-8290
ISSN	2159-8274
DOI	10.1158/2159-8290.CD-20-1219
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Article ; Online: ASPSCR1-TFE3 reprograms transcription by organizing enhancer loops around hexameric VCP/p97.

Pozner, Amir / Li, Li / Verma, Shiv Prakash / Wang, Shuxin / Barrott, Jared J / Nelson, Mary L / Yu, Jamie S E / Negri, Gian Luca / Colborne, Shane / Hughes, Christopher S / Zhu, Ju-Fen / Lambert, Sydney L / Carroll, Lara S / Smith-Fry, Kyllie / Stewart, Michael G / Kannan, Sarmishta / Jensen, Bodrie / John, Cini M / Sikdar, Saif /

Liu, Hongrui / Dang, Ngoc Ha / Bourdage, Jennifer / Li, Jinxiu / Vahrenkamp, Jeffery M / Mortenson, Katelyn L / Groundland, John S / Wustrack, Rosanna / Senger, Donna L / Zemp, Franz J / Mahoney, Douglas J / Gertz, Jason / Zhang, Xiaoyang / Lazar, Alexander J / Hirst, Martin / Morin, Gregg B / Nielsen, Torsten O / Shen, Peter S / Jones, Kevin B

Nature communications

2024 Volume 15, Issue 1, Page(s) 1165

Abstract: The t(X,17) chromosomal translocation, generating the ASPSCR1::TFE3 fusion oncoprotein, is the singular genetic driver of alveolar soft part sarcoma (ASPS) and some Xp11-rearranged renal cell carcinomas (RCCs), frustrating efforts to identify therapeutic ...

Abstract	The t(X,17) chromosomal translocation, generating the ASPSCR1::TFE3 fusion oncoprotein, is the singular genetic driver of alveolar soft part sarcoma (ASPS) and some Xp11-rearranged renal cell carcinomas (RCCs), frustrating efforts to identify therapeutic targets for these rare cancers. Here, proteomic analysis identifies VCP/p97, an AAA+ ATPase with known segregase function, as strongly enriched in co-immunoprecipitated nuclear complexes with ASPSCR1::TFE3. We demonstrate that VCP is a likely obligate co-factor of ASPSCR1::TFE3, one of the only such fusion oncoprotein co-factors identified in cancer biology. Specifically, VCP co-distributes with ASPSCR1::TFE3 across chromatin in association with enhancers genome-wide. VCP presence, its hexameric assembly, and its enzymatic function orchestrate the oncogenic transcriptional signature of ASPSCR1::TFE3, by facilitating assembly of higher-order chromatin conformation structures demonstrated by HiChIP. Finally, ASPSCR1::TFE3 and VCP demonstrate co-dependence for cancer cell proliferation and tumorigenesis in vitro and in ASPS and RCC mouse models, underscoring VCP's potential as a novel therapeutic target.
MeSH term(s)	Animals ; Mice ; Humans ; Proteomics ; Carcinoma, Renal Cell/genetics ; Carcinoma, Renal Cell/pathology ; Translocation, Genetic ; Oncogene Proteins, Fusion/genetics ; Oncogene Proteins, Fusion/metabolism ; Kidney Neoplasms/genetics ; Chromatin/genetics ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/metabolism ; Chromosomes, Human, X/metabolism ; Intracellular Signaling Peptides and Proteins/genetics ; Valosin Containing Protein/genetics
Chemical Substances	Oncogene Proteins, Fusion ; Chromatin ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; TFE3 protein, human ; ASPSCR1 protein, human ; Intracellular Signaling Peptides and Proteins ; VCP protein, human (EC 3.6.4.6) ; Valosin Containing Protein (EC 3.6.4.6)
Language	English
Publishing date	2024-02-07
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-45280-5
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Article: ASPSCR1-TFE3 reprograms transcription by organizing enhancer loops around hexameric VCP/p97.

Pozner, Amir / Verma, Shiv Prakash / Li, Li / Wang, Shuxin / Barrott, Jared J / Nelson, Mary L / Yu, Jamie S E / Negri, Gian Luca / Colborne, Shane / Hughes, Christopher S / Zhu, Ju-Fen / Lambert, Sydney L / Carroll, Lara S / Smith-Fry, Kyllie / Stewart, Michael G / Kannan, Sarmishta / Jensen, Bodrie / Mortenson, Katelyn L / John, Cini /

Sikdar, Saif / Liu, Hongrui / Dang, Ngoc Ha / Bourdage, Jennifer / Li, Jinxiu / Vahrenkamp, Jeffery M / Groundland, John S / Wustrack, Rosanna / Senger, Donna L / Zemp, Franz J / Mahoney, Douglas J / Gertz, Jason / Zhang, Xiaoyang / Lazar, Alexander J / Hirst, Martin / Morin, Gregg B / Nielsen, Torsten O / Shen, Peter S / Jones, Kevin B

bioRxiv : the preprint server for biology

2023

Abstract: The t(X,17) chromosomal translocation, generating the ASPSCR1-TFE3 fusion oncoprotein, is the singular genetic driver of alveolar soft part sarcoma (ASPS) and some Xp11-rearranged renal cell carcinomas (RCC), frustrating efforts to identify therapeutic ... ...

Abstract	The t(X,17) chromosomal translocation, generating the ASPSCR1-TFE3 fusion oncoprotein, is the singular genetic driver of alveolar soft part sarcoma (ASPS) and some Xp11-rearranged renal cell carcinomas (RCC), frustrating efforts to identify therapeutic targets for these rare cancers. Proteomic analysis showed that VCP/p97, an AAA+ ATPase with known segregase function, was strongly enriched in co-immunoprecipitated nuclear complexes with ASPSCR1-TFE3. We demonstrate that VCP is a likely obligate co-factor of ASPSCR1-TFE3, one of the only such fusion oncoprotein co-factors identified in cancer biology. Specifically, VCP co-distributed with ASPSCR1-TFE3 across chromatin in association with enhancers genome-wide. VCP presence, its hexameric assembly, and its enzymatic function orchestrated the oncogenic transcriptional signature of ASPSCR1-TFE3, by facilitating assembly of higher-order chromatin conformation structures as demonstrated by HiChIP. Finally, ASPSCR1-TFE3 and VCP demonstrated co-dependence for cancer cell proliferation and tumorigenesis
Language	English
Publishing date	2023-10-02
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.09.29.560242
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Article: Detection and assignment of phosphoserine and phosphothreonine residues by ¹³C-³¹P spin-echo difference NMR spectroscopy

McIntosh, Lawrence P. / Kang, Hyun-Seo / Okon, Mark / Nelson, Mary L. / Graves, Barbara J. / Brutscher, Bernhard

Journal of biomolecular NMR. 2009 Jan., v. 43, no. 1

2009

Abstract: A simple NMR method is presented for the identification and assignment of phosphorylated serine and threonine residues in ¹³C- or ¹³C/¹⁵N-labeled proteins. By exploiting modest (~5 Hz) 2- and 3-bond ¹³C-³¹P scalar couplings, the aliphatic ¹H-¹³C signals ... ...

Abstract	A simple NMR method is presented for the identification and assignment of phosphorylated serine and threonine residues in ¹³C- or ¹³C/¹⁵N-labeled proteins. By exploiting modest (~5 Hz) 2- and 3-bond ¹³C-³¹P scalar couplings, the aliphatic ¹H-¹³C signals from phosphoserines and phosphothreonines can be detected selectively in a ³¹P spin-echo difference constant time ¹H-¹³C HSQC spectrum. Inclusion of the same ³¹P spin-echo element within the ¹³C frequency editing period of an intraHNCA or HN(CO)CA experiment allows identification of the amide ¹HN and ¹⁵N signals of residues (i) for which ¹³Cα(i) or ¹³Cα(i - 1), respectively, are coupled to a phosphate. Furthermore, ³¹P resonance assignments can be obtained by applying selective low power cw ³¹P decoupling during the spin-echo period. The approach is demonstrated using a PNT domain containing fragment of the transcription factor Ets-1, phosphorylated in vitro at Thr38 and Ser41 with the MAP kinase ERK2.
Keywords	mitogen-activated protein kinase ; nuclear magnetic resonance spectroscopy ; phosphates ; serine ; threonine ; transcription factors
Language	English
Dates of publication	2009-01
Size	p. 31-37.
Publisher	Springer Netherlands
Publishing place	Dordrecht
Document type	Article
ZDB-ID	1081696-3
ISSN	0925-2738
ISSN	0925-2738
DOI	10.1007/s10858-008-9287-6
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Article: Ras/mitogen-activated protein kinase signaling activates Ets-1 and Ets-2 by CBP/p300 recruitment.

Foulds, Charles E / Nelson, Mary L / Blaszczak, Adam G / Graves, Barbara J

Molecular and cellular biology

2004 Volume 24, Issue 24, Page(s) 10954–10964

Abstract: Cell signaling affects gene expression by regulating the activity of transcription factors. Here, we report that mitogen-activated protein kinase (MAPK) phosphorylation of Ets-1 and Ets-2, at a conserved site N terminal to their Pointed (PNT) domains, ... ...

Abstract	Cell signaling affects gene expression by regulating the activity of transcription factors. Here, we report that mitogen-activated protein kinase (MAPK) phosphorylation of Ets-1 and Ets-2, at a conserved site N terminal to their Pointed (PNT) domains, resulted in enhanced transactivation by preferential recruitment of the coactivators CREB binding protein (CBP) and p300. We discovered this phosphorylation-augmented interaction in an unbiased affinity chromatography screen of HeLa nuclear extracts by using either mock-treated or ERK2-phosphorylated ETS proteins as ligands. Binding between purified proteins demonstrated a direct interaction. Both the phosphoacceptor site, which lies in an unstructured region, and the PNT domain were required for the interaction. Minimal regions that were competent for induced CBP/p300 binding in vitro also supported MAPK-enhanced transcription in vivo. CBP coexpression potentiated MEK1-stimulated Ets-2 transactivation of promoters with Ras-responsive elements. Furthermore, CBP and Ets-2 interacted in a phosphorylation-enhanced manner in vivo. This study describes a distinctive interface for a transcription factor-coactivator complex and demonstrates a functional role for inducible CBP/p300 binding. In addition, our findings decipher the mechanistic link between Ras/MAPK signaling and two specific transcription factors that are relevant to both normal development and tumorigenesis.
MeSH term(s)	Acetyltransferases/metabolism ; Amino Acid Sequence ; Baculoviridae/genetics ; Blotting, Western ; CREB-Binding Protein ; Cell Cycle Proteins/metabolism ; Chromatography, Affinity ; Genes, Reporter ; Genes, ras ; HeLa Cells ; Histone Acetyltransferases ; Humans ; Luciferases/metabolism ; Mitogen-Activated Protein Kinases/metabolism ; Models, Biological ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Structure, Tertiary ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Protein c-ets-2 ; Proto-Oncogene Proteins/chemistry ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-ets ; Recombinant Proteins/metabolism ; Signal Transduction ; Silver Staining ; Trans-Activators/chemistry ; Trans-Activators/genetics ; Trans-Activators/metabolism ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcriptional Activation ; p300-CBP Transcription Factors
Chemical Substances	Cell Cycle Proteins ; ETS1 protein, human ; ETS2 protein, human ; Nuclear Proteins ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Protein c-ets-2 ; Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-ets ; Recombinant Proteins ; Trans-Activators ; Transcription Factors ; Luciferases (EC 1.13.12.-) ; Acetyltransferases (EC 2.3.1.-) ; CREB-Binding Protein (EC 2.3.1.48) ; CREBBP protein, human (EC 2.3.1.48) ; Histone Acetyltransferases (EC 2.3.1.48) ; p300-CBP Transcription Factors (EC 2.3.1.48) ; p300-CBP-associated factor (EC 2.3.1.48) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2004-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.24.24.10954-10964.2004
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Article ; Online: Ras signaling requires dynamic properties of Ets1 for phosphorylation-enhanced binding to coactivator CBP.

Nelson, Mary L / Kang, Hyun-Seo / Lee, Gregory M / Blaszczak, Adam G / Lau, Desmond K W / McIntosh, Lawrence P / Graves, Barbara J

Proceedings of the National Academy of Sciences of the United States of America

2010 Volume 107, Issue 22, Page(s) 10026–10031

Abstract: Ras/MAPK signaling is often aberrantly activated in human cancers. The downstream effectors are transcription factors, including those encoded by the ETS gene family. Using cell-based assays and biophysical measurements, we have determined the mechanism ... ...

Abstract	Ras/MAPK signaling is often aberrantly activated in human cancers. The downstream effectors are transcription factors, including those encoded by the ETS gene family. Using cell-based assays and biophysical measurements, we have determined the mechanism by which Ras/MAPK signaling affects the function of Ets1 via phosphorylation of Thr38 and Ser41. These ERK2 phosphoacceptors lie within the unstructured N-terminal region of Ets1, immediately adjacent to the PNT domain. NMR spectroscopic analyses demonstrated that the PNT domain is a four-helix bundle (H2-H5), resembling the SAM domain, appended with two additional helices (H0-H1). Phosphorylation shifted a conformational equilibrium, displacing the dynamic helix H0 from the core bundle. The affinity of Ets1 for the TAZ1 (or CH1) domain of the coactivator CBP was enhanced 34-fold by phosphorylation, and this binding was sensitive to ionic strength. NMR-monitored titration experiments mapped the interaction surfaces of the TAZ1 domain and Ets1, the latter encompassing both the phosphoacceptors and PNT domain. Charge complementarity of these surfaces indicate that electrostatic forces act in concert with a conformational equilibrium to mediate phosphorylation effects. We conclude that the dynamic helical elements of Ets1, appended to a conserved structural core, constitute a phospho-switch that directs Ras/MAPK signaling to downstream changes in gene expression. This detailed structural and mechanistic information will guide strategies for targeting ETS proteins in human disease.
MeSH term(s)	Amino Acid Sequence ; Animals ; CREB-Binding Protein/chemistry ; CREB-Binding Protein/metabolism ; Conserved Sequence ; Humans ; MAP Kinase Signaling System ; Mice ; Models, Molecular ; Molecular Dynamics Simulation ; Molecular Sequence Data ; NIH 3T3 Cells ; Nuclear Magnetic Resonance, Biomolecular ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Interaction Domains and Motifs ; Proto-Oncogene Protein c-ets-1/chemistry ; Proto-Oncogene Protein c-ets-1/genetics ; Proto-Oncogene Protein c-ets-1/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Homology, Amino Acid ; Signal Transduction ; Static Electricity ; ras Proteins/metabolism
Chemical Substances	Ets1 protein, mouse ; Proto-Oncogene Protein c-ets-1 ; Recombinant Proteins ; CREB-Binding Protein (EC 2.3.1.48) ; Crebbp protein, mouse (EC 2.3.1.48) ; ras Proteins (EC 3.6.5.2)
Language	English
Publishing date	2010-05-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0915137107
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Zs.A 1148: Show issues

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Article: Ras signaling requires dynamic properties of Ets1 for phosphorylation-enhanced binding to coactivator CBP

Nelson, Mary L / Kang, Hyun-Seo / Lee, Gregory M / Blaszczak, Adam G / Lau, Desmond K.W / McIntosh, Lawrence P / Graves, Barbara J

Proceedings of the National Academy of Sciences of the United States of America. 2010 June 1, v. 107, no. 22

2010

Abstract	Ras/MAPK signaling is often aberrantly activated in human cancers. The downstream effectors are transcription factors, including those encoded by the ETS gene family. Using cell-based assays and biophysical measurements, we have determined the mechanism by which Ras/MAPK signaling affects the function of Ets1 via phosphorylation of Thr38 and Ser41. These ERK2 phosphoacceptors lie within the unstructured N-terminal region of Ets1, immediately adjacent to the PNT domain. NMR spectroscopic analyses demonstrated that the PNT domain is a four-helix bundle (H2-H5), resembling the SAM domain, appended with two additional helices (H0-H1). Phosphorylation shifted a conformational equilibrium, displacing the dynamic helix H0 from the core bundle. The affinity of Ets1 for the TAZ1 (or CH1) domain of the coactivator CBP was enhanced 34-fold by phosphorylation, and this binding was sensitive to ionic strength. NMR-monitored titration experiments mapped the interaction surfaces of the TAZ1 domain and Ets1, the latter encompassing both the phosphoacceptors and PNT domain. Charge complementarity of these surfaces indicate that electrostatic forces act in concert with a conformational equilibrium to mediate phosphorylation effects. We conclude that the dynamic helical elements of Ets1, appended to a conserved structural core, constitute a phospho-switch that directs Ras/MAPK signaling to downstream changes in gene expression. This detailed structural and mechanistic information will guide strategies for targeting ETS proteins in human disease.
Keywords	electrostatic interactions ; gene expression regulation ; genes ; human diseases ; humans ; ionic strength ; mitogen-activated protein kinase ; neoplasms ; nuclear magnetic resonance spectroscopy ; phosphorylation ; proteins ; titration ; transcription factors
Language	English
Dates of publication	2010-0601
Size	p. 10026-10031.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0915137107
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Article ; Online: Detection and assignment of phosphoserine and phosphothreonine residues by (13)C- (31)P spin-echo difference NMR spectroscopy.

McIntosh, Lawrence P / Kang, Hyun-Seo / Okon, Mark / Nelson, Mary L / Graves, Barbara J / Brutscher, Bernhard

Journal of biomolecular NMR

2008 Volume 43, Issue 1, Page(s) 31–37

Abstract: A simple NMR method is presented for the identification and assignment of phosphorylated serine and threonine residues in (13)C- or (13)C/(15)N-labeled proteins. By exploiting modest (~5 Hz) 2- and 3-bond (13)C-(31)P scalar couplings, the aliphatic (1)H-( ...

Abstract	A simple NMR method is presented for the identification and assignment of phosphorylated serine and threonine residues in (13)C- or (13)C/(15)N-labeled proteins. By exploiting modest (~5 Hz) 2- and 3-bond (13)C-(31)P scalar couplings, the aliphatic (1)H-(13)C signals from phosphoserines and phosphothreonines can be detected selectively in a (31)P spin-echo difference constant time (1)H-(13)C HSQC spectrum. Inclusion of the same (31)P spin-echo element within the (13)C frequency editing period of an intraHNCA or HN(CO)CA experiment allows identification of the amide (1)H(N) and (15)N signals of residues (i) for which( 13)C(alpha)(i) or ( 13)C(alpha)(i - 1), respectively, are coupled to a phosphate. Furthermore, (31)P resonance assignments can be obtained by applying selective low power cw (31)P decoupling during the spin-echo period. The approach is demonstrated using a PNT domain containing fragment of the transcription factor Ets-1, phosphorylated in vitro at Thr38 and Ser41 with the MAP kinase ERK2.
MeSH term(s)	Carbon Isotopes/chemistry ; Escherichia coli/genetics ; Nitrogen Isotopes/chemistry ; Nuclear Magnetic Resonance, Biomolecular/methods ; Phosphoproteins/chemistry ; Phosphorus Isotopes/chemistry ; Phosphoserine/analysis ; Phosphothreonine/analysis ; Proteins/chemistry ; Proto-Oncogene Protein c-ets-1/chemistry ; Proto-Oncogene Protein c-ets-1/genetics
Chemical Substances	Carbon Isotopes ; Nitrogen Isotopes ; Phosphoproteins ; Phosphorus Isotopes ; Proteins ; Proto-Oncogene Protein c-ets-1 ; Phosphothreonine (1114-81-4) ; Phosphoserine (17885-08-4)
Language	English
Publishing date	2008-11-12
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1081696-3
ISSN	1573-5001 ; 0925-2738
ISSN (online)	1573-5001
ISSN	0925-2738
DOI	10.1007/s10858-008-9287-6
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Article ; Online: Identification and structural characterization of a CBP/p300-binding domain from the ETS family transcription factor GABP alpha.

Kang, Hyun-Seo / Nelson, Mary L / Mackereth, Cameron D / Schärpf, Manuela / Graves, Barbara J / McIntosh, Lawrence P

Journal of molecular biology

2008 Volume 377, Issue 3, Page(s) 636–646

Abstract: Using NMR spectroscopy, we identified and characterized a previously unrecognized structured domain near the N-terminus (residues 35-121) of the ETS family transcription factor GABP alpha. The monomeric domain folds as a five-stranded beta-sheet crossed ... ...

Abstract	Using NMR spectroscopy, we identified and characterized a previously unrecognized structured domain near the N-terminus (residues 35-121) of the ETS family transcription factor GABP alpha. The monomeric domain folds as a five-stranded beta-sheet crossed by a distorted helix. Although globally resembling ubiquitin, the GABP alpha fragment differs in its secondary structure topology and thus appears to represent a new protein fold that we term the OST (On-SighT) domain. The surface of the GABP alpha OST domain contains two predominant clusters of negatively-charged residues suggestive of electrostatically driven interactions with positively-charged partner proteins. Following a best-candidate approach to identify such a partner, we demonstrated through NMR-monitored titrations and glutathione S-transferase pulldown assays that the OST domain binds to the CH1 and CH3 domains of the co-activator histone acetyltransferase CBP/p300. This provides a direct structural link between GABP and a central component of the transcriptional machinery.
MeSH term(s)	Animals ; Binding Sites ; GA-Binding Protein Transcription Factor/chemistry ; Mice ; Nuclear Magnetic Resonance, Biomolecular ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; p300-CBP Transcription Factors/chemistry
Chemical Substances	GA-Binding Protein Transcription Factor ; p300-CBP Transcription Factors (EC 2.3.1.48)
Language	English
Publishing date	2008-01-30
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2008.01.054
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Article: Variable Control of Ets-1 DNA Binding by Multiple Phosphates in an Unstructured Region

Pufall, Miles A / Graves, Barbara J / Kang, Hyun-Seo / Kay, Lewis E / Lee, Gregory M / McIntosh, Lawrence P / Nelson, Mary L / Velyvis, Algirdas

Science. 2005 July 1, v. 309, no. 5731

2005

Abstract: Cell signaling that culminates in posttranslational modifications directs protein activity. Here we report how multiple CaÂ²âº-dependent phosphorylation sites within the transcription activator Ets-1 act additively to produce graded DNA binding affinity. ...

Abstract	Cell signaling that culminates in posttranslational modifications directs protein activity. Here we report how multiple CaÂ²âº-dependent phosphorylation sites within the transcription activator Ets-1 act additively to produce graded DNA binding affinity. Nuclear magnetic resonance spectroscopic analyses show that phosphorylation shifts Ets-1 from a dynamic conformation poised to bind DNA to a well-folded inhibited state. These phosphates lie in an unstructured flexible region that functions as the allosteric effector of autoinhibition. Variable phosphorylation thus serves as a "rheostat" for cell signaling to fine-tune transcription at the level of DNA binding.
Keywords	binding capacity ; DNA ; nuclear magnetic resonance spectroscopy ; phosphates ; phosphorylation ; post-translational modification ; spectral analysis
Language	English
Dates of publication	2005-0701
Size	p. 142-145.
Document type	Article
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.1111915
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In stock of ZB MED Cologne/Königswinter

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Inter-library loan at ZB MED

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In stock of ZB MED Cologne/Königswinter

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In stock of ZB MED Cologne/Königswinter

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In stock of ZB MED Cologne/Königswinter

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In stock of ZB MED Bonn / Germany

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In stock of ZB MED Cologne/Königswinter

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In stock of ZB MED Cologne/Königswinter

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In stock of ZB MED Bonn / Germany

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Inter-library loan at ZB MED