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Lisa K Philp Australian Prostate Cancer Research Centre – Queensland, Institute of Health and Biomedical Innovation, School of Biomedical Sciences, Faculty of Health, Queensland University of Technology, Princess Alexandra Hospital, Translational Research Institute, Brisbane, Queensland, Australia

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Anja Rockstroh Australian Prostate Cancer Research Centre – Queensland, Institute of Health and Biomedical Innovation, School of Biomedical Sciences, Faculty of Health, Queensland University of Technology, Princess Alexandra Hospital, Translational Research Institute, Brisbane, Queensland, Australia

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Melanie Lehman Australian Prostate Cancer Research Centre – Queensland, Institute of Health and Biomedical Innovation, School of Biomedical Sciences, Faculty of Health, Queensland University of Technology, Princess Alexandra Hospital, Translational Research Institute, Brisbane, Queensland, Australia
Vancouver Prostate Centre, Department of Urologic Sciences, University of British Columbia, Vancouver, Canada

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Martin C Sadowski Australian Prostate Cancer Research Centre – Queensland, Institute of Health and Biomedical Innovation, School of Biomedical Sciences, Faculty of Health, Queensland University of Technology, Princess Alexandra Hospital, Translational Research Institute, Brisbane, Queensland, Australia

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Nenad Bartonicek Garvan Institute of Medical Research, Sydney, New South Wales, Australia

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John D Wade Florey Institute of Neuroscience and Mental Health, University of Melbourne, Melbourne, Victoria, Australia
School of Chemistry, University of Melbourne, Melbourne, Victoria, Australia

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Laszlo Otvos Jr OLPE, LLC, Audubon, Pennsylvania, USA
Institute of Medical Microbiology, Semmelweis University, Budapest, Hungary

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Colleen C Nelson Australian Prostate Cancer Research Centre – Queensland, Institute of Health and Biomedical Innovation, School of Biomedical Sciences, Faculty of Health, Queensland University of Technology, Princess Alexandra Hospital, Translational Research Institute, Brisbane, Queensland, Australia

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signalling pathway 0.87 −1.89 M CREB signalling in neurons 0.79 −1.67 N T cell exhaustion signalling pathway 0.64 +2.12 Assessed using IPA and differentially expressed transcripts mapping only to the human genome, in

Article Type:
Research Article
DOI:
https://doi.org/10.1530/ERC-20-0297
Volume/Issue:
Volume 27: Issue 12
Restricted access
Sudipan Karmakar Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030, USA

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Estrella A Foster Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030, USA

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Julia K Blackmore Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030, USA

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Carolyn L Smith Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030, USA

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Cell 21 555 – 564 doi:10.1016/j.molcel.2006.01.014 . Dutertre M Smith CL 2003 Ligand-independent interactions of p160/steroid receptor coactivators and CREB-binding protein (CBP) with estrogen receptor-α: regulation by phosphorylation sites

Article Type:
Research Article
DOI:
https://doi.org/10.1677/ERC-09-0285
Volume/Issue:
Volume 18: Issue 1
Free access
Leigh C Murphy Department of Biochemistry and Medical Genetics, Manitoba Institute of Cell Biology, Deeley Research Centre, Faculty of Medicine
Department of Biochemistry and Medical Genetics, Manitoba Institute of Cell Biology, Deeley Research Centre, Faculty of Medicine

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Srinivas V Seekallu Department of Biochemistry and Medical Genetics, Manitoba Institute of Cell Biology, Deeley Research Centre, Faculty of Medicine
Department of Biochemistry and Medical Genetics, Manitoba Institute of Cell Biology, Deeley Research Centre, Faculty of Medicine

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Peter H Watson Department of Biochemistry and Medical Genetics, Manitoba Institute of Cell Biology, Deeley Research Centre, Faculty of Medicine
Department of Biochemistry and Medical Genetics, Manitoba Institute of Cell Biology, Deeley Research Centre, Faculty of Medicine

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receptor-positive primary breast cancer . Cancer Research 61 8452 – 8458 . Dutertre M Smith C 2003 Ligand-independent interactions of p160/steroid receptor coactivators and CREB-binding protein (CBP) with estrogen receptor-alpha: regulation by

Article Type:
Research Article
DOI:
https://doi.org/10.1677/ERC-10-0070
Volume/Issue:
Volume 18: Issue 1
Free access
K-M Rau
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H-Y Kang
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T-L Cha
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S A Miller
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M-C Hung
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work) The authors declare that there is no conflict of interest that would prejudice the impartiality of this scientific work. References Aarnisalo P , Palvimo JJ & Janne OA 1998 CREB-binding protein

Article Type:
Review Article
DOI:
https://doi.org/10.1677/erc.1.01026
Volume/Issue:
Volume 12: Issue 3
Free access
E M Rosen Department of Oncology, Lombardi Cancer Center, Georgetown University, 3970 Reservoir Road, NW, Washington, District of Columbia 20057, USA

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S Fan Department of Oncology, Lombardi Cancer Center, Georgetown University, 3970 Reservoir Road, NW, Washington, District of Columbia 20057, USA

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C Isaacs Department of Oncology, Lombardi Cancer Center, Georgetown University, 3970 Reservoir Road, NW, Washington, District of Columbia 20057, USA

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these targets could contribute to the inhibition of ER-α is not ruled out. wtBRCA1 down-regulated the expression of p300 but not its functional homolog, the CREB binding protein (CBP) ( Fan et al. 1998 , 2002 ). Exogenous p300 or CBP

Article Type:
Review Article
DOI:
https://doi.org/10.1677/erc.1.00972
Volume/Issue:
Volume 12: Issue 3
Free access
Paul Benjamin Loughrey Patrick G Johnston Centre for Cancer Research, Queen’s University, Belfast, UK
Regional Centre for Endocrinology and Diabetes, Royal Victoria Hospital, Belfast Health & Social Care Trust, Belfast, UK

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Federico Roncaroli Geoffrey Jefferson Brain Research Centre, Division of Neuroscience and Experimental Psychology, School of Medicine, Manchester University, Manchester, UK

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Estelle Healy Department of Cellular Pathology, Royal Victoria Hospital, Belfast Health & Social Care Trust, Belfast, UK

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Philip Weir Department of Neurosurgery, Royal Victoria Hospital, Belfast Health & Social Care Trust, Belfast, UK

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Madhu Basetti Cancer Research UK Cambridge Institute, Li Ka Shing Centre, University of Cambridge, Cambridge, UK

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Ruth T Casey Department of Endocrinology, Cambridge University Hospital NHS Foundation Trust, Cambridge, UK

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Steven J Hunter Regional Centre for Endocrinology and Diabetes, Royal Victoria Hospital, Belfast Health & Social Care Trust, Belfast, UK

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Márta Korbonits Centre for Endocrinology, William Harvey Research Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University of London, London, UK

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, and a recent study has established a link between HIF-1α excess and protein kinase A, CREB and downstream excess growth hormone secretion via repression of PRKAR2B transcription ( Lucia et al. 2020 ). SDHx variants SDHB , SDHA and SDHC

Article Type:
Review Article
Collections:
Advances and Future Directions in Pheochromocytoma and Paraganglioma
DOI:
https://doi.org/10.1530/ERC-22-0157
Volume/Issue:
Volume 29: Issue 10
Open access
Jesús Morillo-Bernal Instituto de Investigaciones Biomédicas ‘Alberto Sols’, Consejo Superior Investigaciones Científicas, and Universidad Autónoma de Madrid (CSIC-UAM), Madrid, Spain

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Lara P Fernández Instituto de Investigaciones Biomédicas ‘Alberto Sols’, Consejo Superior Investigaciones Científicas, and Universidad Autónoma de Madrid (CSIC-UAM), Madrid, Spain
Molecular Oncology Group, IMDEA Food Institute, CEI UAM-CSIC, Madrid, Spain

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Pilar Santisteban Instituto de Investigaciones Biomédicas ‘Alberto Sols’, Consejo Superior Investigaciones Científicas, and Universidad Autónoma de Madrid (CSIC-UAM), Madrid, Spain
Centro de Investigación Biomédica en Red de Cáncer (CIBERONC), Instituto de Salud Carlos III (ISCIII), Madrid, Spain

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-Marquez A Fernandez-Mendez C Recacha P Santisteban P 2019 Regulation of Foxe1 by TSH and TGFbeta depends on the interplay between thyroid-specific, CREB and SMAD transcription factors . Thyroid 714 – 725 . ( https://doi.org/10.1089/thy.2018

Article Type:
Research Article
DOI:
https://doi.org/10.1530/ERC-19-0156
Volume/Issue:
Volume 27: Issue 3
Open access
Perrine Raymond Endocrinology Department, CHRU de Brabois, Vandoeuvre Les Nancy, France

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Gérald Raverot Endocrinology Department, Reference Center for Rare Pituitary Diseases HYPO, “Groupement Hospitalier Est” Hospices Civils de Lyon, Bron, France
Inserm U1052, CNRS UMR5286, Claude Bernard Lyon 1 University, Cancer Research Center of Lyon, Lyon, France

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Mirela-Diana Ilie Inserm U1052, CNRS UMR5286, Claude Bernard Lyon 1 University, Cancer Research Center of Lyon, Lyon, France
Endocrinology Department, “C.I. Parhon” National Institute of Endocrinology, Bucharest, Romania

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MutS Homolog 2 ( MSH2) mutation, while in two cases, no MEN1 mutations were identified. Somatic mutations were analyzed in five cases: two had a hypermutator phenotype, one had a CREB-binding protein ( CREBBP ) mutation, while two did not have any

Article Type:
Research Article
DOI:
https://doi.org/10.1530/ERC-22-0338
Volume/Issue:
Volume 30: Issue 5
Restricted access
Gerard A Tarulli Dame Roma Mitchell Cancer Research Laboratories (DRMCRL) Faculty of Health Sciences, School of Medicine, The University of Adelaide, Adelaide, South Australia 5005, Australia

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Lisa M Butler Dame Roma Mitchell Cancer Research Laboratories (DRMCRL) Faculty of Health Sciences, School of Medicine, The University of Adelaide, Adelaide, South Australia 5005, Australia

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Wayne D Tilley Dame Roma Mitchell Cancer Research Laboratories (DRMCRL) Faculty of Health Sciences, School of Medicine, The University of Adelaide, Adelaide, South Australia 5005, Australia

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Theresa E Hickey Dame Roma Mitchell Cancer Research Laboratories (DRMCRL) Faculty of Health Sciences, School of Medicine, The University of Adelaide, Adelaide, South Australia 5005, Australia

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(RBPJ – also known as C-promoter-binding factor 1 (CBF1)), converting it from a transcriptional repressor to an activator via the recruitment of coactivators such as CREB-binding protein (CBP), mastermind-like proteins (MAML) and histone

Article Type:
Research Article
DOI:
https://doi.org/10.1530/ERC-14-0248
Volume/Issue:
Volume 21: Issue 4
Free access
Kathryn E Ware Departments of Molecular Genetics and Medicine Duke University, 213 Research Dr, 0045 CARL Building, Durham, North Carolina 27710, USA

Department of Medicine Duke Cancer Institute, Duke University, Durham, North Carolina, USA

Masonic Cancer Center University of Minnesota Masonic Cancer Center, Mayo Mail Code 806, 420 Delaware Street SE, Minneapolis, Minnesota 55455, USA

Department of Laboratory Medicine and Pathology University of Minnesota, Minneapolis, Minnesota, USA

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Mariano A Garcia-Blanco Departments of Molecular Genetics and Medicine Duke University, 213 Research Dr, 0045 CARL Building, Durham, North Carolina 27710, USA

Department of Medicine Duke Cancer Institute, Duke University, Durham, North Carolina, USA

Masonic Cancer Center University of Minnesota Masonic Cancer Center, Mayo Mail Code 806, 420 Delaware Street SE, Minneapolis, Minnesota 55455, USA

Department of Laboratory Medicine and Pathology University of Minnesota, Minneapolis, Minnesota, USA
Departments of Molecular Genetics and Medicine Duke University, 213 Research Dr, 0045 CARL Building, Durham, North Carolina 27710, USA

Department of Medicine Duke Cancer Institute, Duke University, Durham, North Carolina, USA

Masonic Cancer Center University of Minnesota Masonic Cancer Center, Mayo Mail Code 806, 420 Delaware Street SE, Minneapolis, Minnesota 55455, USA

Department of Laboratory Medicine and Pathology University of Minnesota, Minneapolis, Minnesota, USA

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Andrew J Armstrong Departments of Molecular Genetics and Medicine Duke University, 213 Research Dr, 0045 CARL Building, Durham, North Carolina 27710, USA

Department of Medicine Duke Cancer Institute, Duke University, Durham, North Carolina, USA

Masonic Cancer Center University of Minnesota Masonic Cancer Center, Mayo Mail Code 806, 420 Delaware Street SE, Minneapolis, Minnesota 55455, USA

Department of Laboratory Medicine and Pathology University of Minnesota, Minneapolis, Minnesota, USA
Departments of Molecular Genetics and Medicine Duke University, 213 Research Dr, 0045 CARL Building, Durham, North Carolina 27710, USA

Department of Medicine Duke Cancer Institute, Duke University, Durham, North Carolina, USA

Masonic Cancer Center University of Minnesota Masonic Cancer Center, Mayo Mail Code 806, 420 Delaware Street SE, Minneapolis, Minnesota 55455, USA

Department of Laboratory Medicine and Pathology University of Minnesota, Minneapolis, Minnesota, USA

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Scott M Dehm Departments of Molecular Genetics and Medicine Duke University, 213 Research Dr, 0045 CARL Building, Durham, North Carolina 27710, USA

Department of Medicine Duke Cancer Institute, Duke University, Durham, North Carolina, USA

Masonic Cancer Center University of Minnesota Masonic Cancer Center, Mayo Mail Code 806, 420 Delaware Street SE, Minneapolis, Minnesota 55455, USA

Department of Laboratory Medicine and Pathology University of Minnesota, Minneapolis, Minnesota, USA
Departments of Molecular Genetics and Medicine Duke University, 213 Research Dr, 0045 CARL Building, Durham, North Carolina 27710, USA

Department of Medicine Duke Cancer Institute, Duke University, Durham, North Carolina, USA

Masonic Cancer Center University of Minnesota Masonic Cancer Center, Mayo Mail Code 806, 420 Delaware Street SE, Minneapolis, Minnesota 55455, USA

Department of Laboratory Medicine and Pathology University of Minnesota, Minneapolis, Minnesota, USA

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for binding many AR co-regulators, and is responsible for the majority of AR transcriptional activity. Binding of EPI-001 to the AR AF-1 region inhibits the ability of AR to interact with proteins such as CREB-binding protein ( Andersen et al . 2010

Article Type:
Review Article
DOI:
https://doi.org/10.1530/ERC-13-0470
Volume/Issue:
Volume 21: Issue 4
Free access