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Article: The ETS-domain transcription factor family.

Sharrocks, A D

2001 Volume 2, Issue 11, Page(s) 827–837

Abstract: ETS-domain transcription-factor networks represent a model for how combinatorial gene expression is achieved. These transcription factors interact with a multitude of co-regulatory partners to elicit gene-specific responses and drive distinct biological ... ...

Abstract	ETS-domain transcription-factor networks represent a model for how combinatorial gene expression is achieved. These transcription factors interact with a multitude of co-regulatory partners to elicit gene-specific responses and drive distinct biological processes. These proteins are controlled by a complex series of inter and intramolecular interactions, and signalling pathways impinge on these proteins to further regulate their action.
MeSH term(s)	Animals ; DNA/metabolism ; Humans ; Models, Biological ; Models, Molecular ; Multigene Family ; Neoplasms/metabolism ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; Proto-Oncogene Proteins/physiology ; Proto-Oncogene Proteins c-ets ; Transcription Factors/physiology
Chemical Substances	Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-ets ; Transcription Factors ; DNA (9007-49-2)
Language	English
Publishing date	2001-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2031313-5
ISSN	1471-0080 ; 1471-0072
ISSN (online)	1471-0080
ISSN	1471-0072
DOI	10.1038/35099076
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Zs.A 5446: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 26: Show issues

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Article ; Online: A decade of the Oesophageal Cancer Clinical and Molecular Stratification Consortium.

Peters, C J / Ang, Y / Ciccarelli, F D / Coles, H / Coleman, H G / Contino, G / Crosby, T / Devonshire, G / Eldridge, M / Freeman, A / Grehan, N / McCord, M / Nutzinger, B / Zamani, S / Parsons, S L / Petty, R / Sharrocks, A D / Skipworth, R J E / Smyth, E C /

Soomro, I / Underwood, T J / Fitzgerald, R C

Nature medicine

2023 Volume 30, Issue 1, Page(s) 14–16

MeSH term(s)	Humans ; Esophageal Neoplasms/genetics ; Adenocarcinoma
Language	English
Publishing date	2023-12-19
Publishing country	United States
Document type	Letter
ZDB-ID	1220066-9
ISSN	1546-170X ; 1078-8956
ISSN (online)	1546-170X
ISSN	1078-8956
DOI	10.1038/s41591-023-02676-y
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Zs.A 4212: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 39: Show issues

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Article: Introduction: the regulation of eukaryotic transcription factor function.

Sharrocks, A D

Cellular and molecular life sciences : CMLS

2000 Volume 57, Issue 8-9, Page(s) 1147–1148

MeSH term(s)	DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Eukaryotic Cells ; Protein Footprinting ; Transcription Factors/chemistry ; Transcription Factors/metabolism ; Transcription, Genetic
Chemical Substances	DNA-Binding Proteins ; Transcription Factors
Language	English
Publishing date	2000-08
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/pl00000754
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Article: Interplay of the SUMO and MAP kinase pathways.

Yang, S H / Sharrocks, A D

Ernst Schering Research Foundation workshop

2006 , Issue 57, Page(s) 193–209

Abstract: The SUMO modification pathway has been linked with controlling the activity of numerous transcriptional regulatory proteins. In the majority of substrates studied so far, sumoylation imparts repressive properties. In several cases, part of this mechanism ...

Abstract	The SUMO modification pathway has been linked with controlling the activity of numerous transcriptional regulatory proteins. In the majority of substrates studied so far, sumoylation imparts repressive properties. In several cases, part of this mechanism has been shown to be due to SUMO-dependent recruitment of histone deacetylases (HDACs). This is exemplified by the transcription factor Elk-1, where HDAC-2 is specifically recruited in response to sumoylation. Importantly, activation of the ERK MAP kinase pathway leads to Elk-1 desumoylation and HDAC loss. Furthermore, PIAS proteins can regulate the activities of transcription factors in SUMO-dependent and -independent manners. Further links between the MAP kinase pathways and PIAS proteins have been uncovered, suggesting a complex interplay been the MAP kinase and SUMO modification pathways. Here we discuss the current evidence suggesting links between the SUMO and MAP kinase pathways and point to other potential regulatory events and how these might be affected in cancer.
MeSH term(s)	Animals ; Cell Transformation, Neoplastic/genetics ; Cell Transformation, Neoplastic/metabolism ; Extracellular Signal-Regulated MAP Kinases/genetics ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Histone Deacetylases/genetics ; Histone Deacetylases/metabolism ; Humans ; MAP Kinase Signaling System/physiology ; Protein Inhibitors of Activated STAT/genetics ; Protein Inhibitors of Activated STAT/metabolism ; Regulatory Elements, Transcriptional/genetics ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Small Ubiquitin-Related Modifier Proteins/genetics ; Small Ubiquitin-Related Modifier Proteins/metabolism ; ets-Domain Protein Elk-1/genetics ; ets-Domain Protein Elk-1/metabolism
Chemical Substances	Protein Inhibitors of Activated STAT ; Repressor Proteins ; Small Ubiquitin-Related Modifier Proteins ; ets-Domain Protein Elk-1 ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24) ; Histone Deacetylases (EC 3.5.1.98)
Language	English
Publishing date	2006-03-28
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	0947-6075
ISSN	0947-6075
DOI	10.1007/3-540-37633-x_11
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Article: ERK2/p42 MAP kinase stimulates both autonomous and SRF-dependent DNA binding by Elk-1.

Sharrocks, A D

FEBS letters

1995 Volume 368, Issue 1, Page(s) 77–80

Abstract: A ternary complex comprised of SRF, ternary complex factor (TCF) and the c-fos SRE is the target of several extracellular signal regulated pathways. Phosphorylation of the TCF Elk-1 is a key event in the activation of this complex. We demonstrate that ... ...

Abstract	A ternary complex comprised of SRF, ternary complex factor (TCF) and the c-fos SRE is the target of several extracellular signal regulated pathways. Phosphorylation of the TCF Elk-1 is a key event in the activation of this complex. We demonstrate that ERK2/p42 phosphorylation of Elk-1 stimulates its recruitment into ternary complexes with SRF. Moreover, phosphorylation of Elk-1 also stimulates its autonomous SRF-independent binding to high affinity binding sites. Thus part of the effect of ERK2/p42 phosphorylation is to stimulate DNA-binding by the ETS DNA-binding domain of Elk-1.
MeSH term(s)	Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; DNA/metabolism ; DNA-Binding Proteins/metabolism ; Escherichia coli ; Mitogen-Activated Protein Kinase 1 ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Binding ; Proto-Oncogene Proteins/metabolism ; Recombinant Proteins/metabolism ; Serum Response Factor ; Transcription Factors ; ets-Domain Protein Elk-1
Chemical Substances	DNA-Binding Proteins ; Nuclear Proteins ; Proto-Oncogene Proteins ; Recombinant Proteins ; Serum Response Factor ; Transcription Factors ; ets-Domain Protein Elk-1 ; DNA (9007-49-2) ; Calcium-Calmodulin-Dependent Protein Kinases (EC 2.7.11.17) ; Mitogen-Activated Protein Kinase 1 (EC 2.7.11.24)
Language	English
Publishing date	1995-07-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/0014-5793(95)00604-8
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Zs.B 282: Show issues

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Article: A T7 expression vector for producing N- and C-terminal fusion proteins with glutathione S-transferase.

Sharrocks, A D

Gene

1994 Volume 138, Issue 1-2, Page(s) 105–108

Abstract: The pGEX system for protein production in E. coli is widely used in molecular biology. A bacterial expression vector, pETGEXCT, which incorporates features of the pGEX and pET expression systems was designed. pETGEXCT allows the production of N- and C- ... ...

Abstract	The pGEX system for protein production in E. coli is widely used in molecular biology. A bacterial expression vector, pETGEXCT, which incorporates features of the pGEX and pET expression systems was designed. pETGEXCT allows the production of N- and C-terminal fusions to glutathione S-transferase (GST) under the tight control of the T7 promoter. Use of this vector can circumvent problems associated with unstable or inactive fusions to the N terminus of GST. Indeed, it is demonstrated that fusions to the N terminus of the eukaryotic DNA-binding protein, RSRFC4, cannot be tolerated. Fusion of RSRFC4 to the N terminus of GST in the pETGEXCT vector is a prerequisite to purify the RSRFC4 DNA-binding domain in an active form using glutathione-agarose affinity chromatography.
MeSH term(s)	Amino Acid Sequence ; Animals ; Bacteriophage T7/genetics ; Base Sequence ; Cloning, Molecular/methods ; Consensus Sequence ; DNA Primers ; DNA-Binding Proteins/biosynthesis ; DNA-Binding Proteins/genetics ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Genetic Vectors ; Glutathione Transferase/biosynthesis ; MADS Domain Proteins ; MEF2 Transcription Factors ; Molecular Sequence Data ; Myogenic Regulatory Factors ; Nuclear Proteins/biosynthesis ; Nuclear Proteins/genetics ; Plasmids ; Polymerase Chain Reaction ; Recombinant Fusion Proteins/biosynthesis ; Restriction Mapping ; Schistosoma japonicum/enzymology ; Schistosoma japonicum/genetics ; Thrombin/metabolism ; Transcription Factors/biosynthesis ; Transcription Factors/genetics
Chemical Substances	DNA Primers ; DNA-Binding Proteins ; MADS Domain Proteins ; MEF2 Transcription Factors ; MEF2A protein, human ; Myogenic Regulatory Factors ; Nuclear Proteins ; Recombinant Fusion Proteins ; Transcription Factors ; Glutathione Transferase (EC 2.5.1.18) ; Thrombin (EC 3.4.21.5)
Language	English
Publishing date	1994-01-28
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	391792-7
ISSN	1879-0038 ; 0378-1119
ISSN (online)	1879-0038
ISSN	0378-1119
DOI	10.1016/0378-1119(94)90789-7
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Zs.A 1357: Show issues

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Article ; Online: FOXM1 and polo-like kinase 1 are co-ordinately overexpressed in patients with gastric adenocarcinomas.

Dibb, M / Han, N / Choudhury, J / Hayes, S / Valentine, H / West, C / Sharrocks, A D / Ang, Yeng S

BMC research notes

2015 Volume 8, Page(s) 676

Abstract: Background: Gastric cancers present late in life with advanced disease and carry a poor prognosis. Polo-like Kinase 1 (PLK1) is a mitotic kinase with regulatory functions during G2/M and mitosis in the cell cycle. In mammalian cells, there is an ... ...

Abstract	Background: Gastric cancers present late in life with advanced disease and carry a poor prognosis. Polo-like Kinase 1 (PLK1) is a mitotic kinase with regulatory functions during G2/M and mitosis in the cell cycle. In mammalian cells, there is an intricate co-regulatory relationship between PLK1 and the forkhead transcription factor FOXM1. It has been demonstrated that individually either PLK1 or FOXM1 expression predicts poorer survival. However, the co-expression of both of these markers in gastric adenocarcinomas has not been reported previously. Methods: We aimed to assess the expression of PLK1 and FOXM1 in Gastric adenocarcinomas in a Western Population, to examine whether there is a relationship of PLK1 to FOXM1 in cancer samples. We assess both the protein and mRNA expression in this patient population by Tissue Microarray immunohistochemistry and RT-PCR. Results: Immunohistochemistry was performed on biopsy samples from 79 patients with gastric cancer. Paired normal controls were available in 47 patients. FOXM1 expression was significantly associated with gastric adenocarcinoma (p = 0.001). PLK1 and FOXM1 co-expression was demonstrated in 6/8 (75 %) tumours when analysed by RT-PCR. FOXM1 is overexpressed in a large proportion of gastric carcinomas at the protein level and FOXM1 and PLK1 are concomitantly overexpressed at the mRNA level in this cancer type. Conclusions: This study has demonstrated that FOXM1 and its target gene PLK1 are coordinately overexpressed in a proportion of gastric adenocarcinomas. This suggests that chemotherapeutic treatments that target this pathway may be of clinical utility.
MeSH term(s)	Adenocarcinoma/enzymology ; Adenocarcinoma/metabolism ; Adenocarcinoma/pathology ; Aged ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Female ; Forkhead Box Protein M1 ; Forkhead Transcription Factors/genetics ; Forkhead Transcription Factors/metabolism ; Humans ; Male ; Middle Aged ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins/metabolism ; RNA, Messenger/genetics ; Stomach Neoplasms/enzymology ; Stomach Neoplasms/metabolism ; Stomach Neoplasms/pathology ; Polo-Like Kinase 1
Chemical Substances	Cell Cycle Proteins ; FOXM1 protein, human ; Forkhead Box Protein M1 ; Forkhead Transcription Factors ; Proto-Oncogene Proteins ; RNA, Messenger ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2015-11-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2413336-X
ISSN	1756-0500 ; 1756-0500
ISSN (online)	1756-0500
ISSN	1756-0500
DOI	10.1186/s13104-015-1658-y
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Article ; Online: The mechanism of complex formation between Fli-1 and SRF transcription factors.

Dalgleish, P / Sharrocks, A D

Nucleic acids research

2000 Volume 28, Issue 2, Page(s) 560–569

Abstract: The mechanisms of multicomponent transcription factor complex assembly are currently poorly defined. A paradigm for this type of complex is the ETS-domain transcription factor Elk-1 and the MADS-box transcription factor SRF which form a ternary complex ... ...

Abstract	The mechanisms of multicomponent transcription factor complex assembly are currently poorly defined. A paradigm for this type of complex is the ETS-domain transcription factor Elk-1 and the MADS-box transcription factor SRF which form a ternary complex with the c- fos serum response element (SRE). In this study we have analysed how a different ETS-domain transcription factor Fli-1 interacts with SRF to form ternary complexes with this element. Two regions of Fli-1 that are required for ternary complex formation have been identified. These SRF binding motifs are located on either side of the ETS DNA-binding domain. Hydrophobic amino acids within these motifs have been identified that play important roles in binding to SRF and ternary complex formation. By using Fli-1 derivatives with mutations in the N-terminal SRF binding motif, the significance of Fli-1-SRF interactions in recruitment of Fli-1 to the c- fos SRE in vivo has been demonstrated. Collectively our data provide a model of how Fli-1 interacts with SRF that differs significantly from the mechanism used by a different ETS-domain protein, Elk-1.
MeSH term(s)	3T3 Cells ; Amino Acid Sequence ; Animals ; Binding Sites ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Humans ; Mice ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Protein Binding ; Proto-Oncogene Protein c-fli-1 ; Proto-Oncogene Proteins ; Sequence Homology, Amino Acid ; Serum Response Factor ; Trans-Activators/metabolism
Chemical Substances	DNA-Binding Proteins ; Fli1 protein, mouse ; Nuclear Proteins ; Proto-Oncogene Protein c-fli-1 ; Proto-Oncogene Proteins ; Serum Response Factor ; Trans-Activators
Language	English
Publishing date	2000-01-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/28.2.560
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Zs.A 1067: Show issues

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Article: MADS-box transcription factors adopt alternative mechanisms for bending DNA.

West, A G / Sharrocks, A D

Journal of molecular biology

1999 Volume 286, Issue 5, Page(s) 1311–1323

Abstract: Transcription factor-induced DNA bending is important in determining local promoter architecture and it is thought to be a key determinant of their function. The human MADS-box transcription factors serum response factor and MEF2A exhibit different ... ...

Abstract	Transcription factor-induced DNA bending is important in determining local promoter architecture and it is thought to be a key determinant of their function. The human MADS-box transcription factors serum response factor and MEF2A exhibit different propensities to bend their binding sites. Here, we have investigated the ability of several family members from different species to bend DNA and the molecular mechanisms underlying this process. Differential DNA bending is observed in yeast and plant MADS-box proteins. Like MEF2A, the yeast proteins Rlm1 and Smp1 exhibit low DNA bending propensities. A comparison of serum response factor and SQUA reveals that the basic mechanisms of DNA bending appear to be conserved between these proteins, although several key differences do exist. In contrast to serum response factor, SQUA bends DNA in a DNA sequence-dependent manner. In both proteins, protein-DNA contacts made between residues in the beta-loop and the N-terminal end of the recognition helices in the MADS-box are the major determinants of DNA bending. However, although residues which are involved in DNA bending are predicted to be located in similar positions in their tertiary structures, different residues dictate bending by each protein. Further complexities are uncovered in the links between the DNA bending propensity and the binding specificity. In combination with structural studies, our results provide a model to explain how differential bending by MADS-box proteins is achieved at the molecular level and provide insights into how this might affect their biological function.
MeSH term(s)	Amino Acid Sequence ; Amino Acid Substitution ; Base Sequence ; Binding Sites ; DNA/chemistry ; DNA/genetics ; DNA/metabolism ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Fungal Proteins/chemistry ; Fungal Proteins/metabolism ; Humans ; MADS Domain Proteins ; MEF2 Transcription Factors ; Models, Molecular ; Molecular Sequence Data ; Myogenic Regulatory Factors ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Nucleic Acid Conformation ; Plant Proteins/chemistry ; Plant Proteins/genetics ; Plant Proteins/metabolism ; Plants/genetics ; Plants/metabolism ; Protein Structure, Secondary ; Response Elements/genetics ; Sequence Alignment ; Serum Response Factor ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Yeasts/genetics ; Yeasts/metabolism
Chemical Substances	DNA-Binding Proteins ; Fungal Proteins ; MADS Domain Proteins ; MEF2 Transcription Factors ; MEF2A protein, human ; Myogenic Regulatory Factors ; Nuclear Proteins ; Plant Proteins ; Serum Response Factor ; Transcription Factors ; SQUA protein, Antirrhinum majus (147336-50-3) ; DNA (9007-49-2)
Language	English
Publishing date	1999-03-12
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1006/jmbi.1999.2576
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Article: Signalling pathways and the regulation of SUMO modification.

Guo, B / Yang, S-H / Witty, J / Sharrocks, A D

Biochemical Society transactions

2007 Volume 35, Issue Pt 6, Page(s) 1414–1418

Abstract: The modification of proteins by SUMO (small ubiquitin-related modifier) conjugation is becoming increasingly recognized as an important regulatory event. Protein SUMOylation can control a whole range of activities, including subcellular localization, ... ...

Abstract	The modification of proteins by SUMO (small ubiquitin-related modifier) conjugation is becoming increasingly recognized as an important regulatory event. Protein SUMOylation can control a whole range of activities, including subcellular localization, protein-protein interactions and enzymatic activity. However, the SUMOylation process can itself be controlled. In the present review, the mechanisms through which protein SUMOylation is regulated are discussed, with particular emphasis on the impact of signalling pathways. A major point of regulation of the SUMO pathway is through targeting the E3 ligases, and a number of different ways to achieve this have been identified. More generally, the MAPK (mitogen-activated protein kinase) pathways represent one way through which SUMOylation of specific proteins is controlled, by using molecular mechanisms that at least in part also function by modifying the activity of SUMO E3 ligases. Further intricacies in signalling pathway interactions are hinted at through the growing number of examples of cross-talk between different post-translational modifications and SUMO modification.
MeSH term(s)	Mitogen-Activated Protein Kinases/metabolism ; Signal Transduction/physiology ; Small Ubiquitin-Related Modifier Proteins/metabolism ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Small Ubiquitin-Related Modifier Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2007-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST0351414
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