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  • ubiquitin-protein ligases x
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Melody Lok-Yi Chan Department of Medicine, University of Hong Kong, Hong Kong SAR

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Sammy Wing-Ming Shiu Department of Medicine, University of Hong Kong, Hong Kong SAR

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Ching-Lung Cheung Department of Pharmacology and Pharmacy, University of Hong Kong, Hong Kong SAR

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Anskar Yu-Hung Leung Department of Medicine, University of Hong Kong, Hong Kong SAR

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Kathryn Choon-Beng Tan Department of Medicine, University of Hong Kong, Hong Kong SAR

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Introduction Inducible degrader of LDL receptor (IDOL), an E3 ubiquitin ligase, has recently been identified as a novel post-translational regulator of the LDL receptor (LDLR) in addition to proprotein convertase subtilisin/kexin type 9 (PCSK9

Article Type:
Research Article
Collections:
Cardiovascular
DOI:
https://doi.org/10.1530/EC-22-0019
Volume/Issue:
Volume 11: Issue 6
Open access
T S Nilsen Department of Physical Performance, Norwegian School of Sports Sciences, Oslo, Norway

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L Thorsen Department of Oncology, Oslo University Hospital, Oslo, Norway

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C Kirkegaard Department of Physical Performance, Norwegian School of Sports Sciences, Oslo, Norway

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I Ugelstad Department of Physical Performance, Norwegian School of Sports Sciences, Oslo, Norway

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S D Fosså Department of Oncology, Oslo University Hospital, Oslo, Norway

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T Raastad Department of Physical Performance, Norwegian School of Sports Sciences, Oslo, Norway

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E3 ligases promote ubiquitin conjugation of proteins destined for breakdown by the 26s proteasome ( 10 ). Removal of testosterone has been shown to increase the expression of muscle-specific E3 ligases ( 11 ), and this may also play a role in ADT

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-15-0120
Volume/Issue:
Volume 5: Issue 2
Open access
Hong Tang Departments of Gynaecology and Obstetrics Seventh People’s Hospital of Shanghai University of Traditional Chinese Medicine, Shanghai, China

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Xiaomei Jiang Departments of Gynaecology and Obstetrics Seventh People’s Hospital of Shanghai University of Traditional Chinese Medicine, Shanghai, China

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Yu Hua Departments of Gynaecology and Obstetrics Seventh People’s Hospital of Shanghai University of Traditional Chinese Medicine, Shanghai, China

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Heyue Li Departments of Gynaecology and Obstetrics Seventh People’s Hospital of Shanghai University of Traditional Chinese Medicine, Shanghai, China

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Chunlan Zhu Departments of Gynaecology and Obstetrics Seventh People’s Hospital of Shanghai University of Traditional Chinese Medicine, Shanghai, China

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Xiaobai Hao Departments of Gynaecology and Obstetrics Seventh People’s Hospital of Shanghai University of Traditional Chinese Medicine, Shanghai, China

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Minhui Yi Departments of Gynaecology and Obstetrics Seventh People’s Hospital of Shanghai University of Traditional Chinese Medicine, Shanghai, China

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Linxia Li Departments of Gynaecology and Obstetrics Seventh People’s Hospital of Shanghai University of Traditional Chinese Medicine, Shanghai, China

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GCs by promoting the ubiquitin-mediated proteasome degradation of GPX4. (A) NEDD4L interacts with GPX4 directly. The protein lysis from GCs was immunoprecipitated with IgG or antibodies against NEDD4L or GXP4 and then IB with NEDD4L and GXP4 ( n  = 3

Article Type:
Research Article
Collections:
Reproduction
DOI:
https://doi.org/10.1530/EC-22-0459
Volume/Issue:
Volume 12: Issue 4
Open access
Legh Wilkinson Department of Biochemistry, Stellenbosch University, Stellenbosch, South Africa

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Nicolette J D Verhoog Department of Biochemistry, Stellenbosch University, Stellenbosch, South Africa

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Ann Louw Department of Biochemistry, Stellenbosch University, Stellenbosch, South Africa

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the ubiquitin-proteasome system (UPS) in the control GRα degradation rates, ultimately contributing to the stringent regulation of the GRα protein pool ( 99 , 102 , 104 , 105 , 139 , 142 , 145 , 147 ). Similarly to ubiquitination, sumoylation

Article Type:
Review Article
DOI:
https://doi.org/10.1530/EC-18-0421
Volume/Issue:
Volume 7: Issue 12
Open access
P G Murray Centre for Paediatrics and Child Health, Faculty of Medicine, Centre for Genetic Medicine, 5th Floor Research, Genetic Medicine, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK
Centre for Paediatrics and Child Health, Faculty of Medicine, Centre for Genetic Medicine, 5th Floor Research, Genetic Medicine, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK

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D Hanson Centre for Paediatrics and Child Health, Faculty of Medicine, Centre for Genetic Medicine, 5th Floor Research, Genetic Medicine, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK

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T Coulson Centre for Paediatrics and Child Health, Faculty of Medicine, Centre for Genetic Medicine, 5th Floor Research, Genetic Medicine, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK

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A Stevens Centre for Paediatrics and Child Health, Faculty of Medicine, Centre for Genetic Medicine, 5th Floor Research, Genetic Medicine, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK

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A Whatmore Centre for Paediatrics and Child Health, Faculty of Medicine, Centre for Genetic Medicine, 5th Floor Research, Genetic Medicine, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK

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R L Poole Centre for Paediatrics and Child Health, Faculty of Medicine, Centre for Genetic Medicine, 5th Floor Research, Genetic Medicine, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK

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D J Mackay Centre for Paediatrics and Child Health, Faculty of Medicine, Centre for Genetic Medicine, 5th Floor Research, Genetic Medicine, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK

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G C M Black Centre for Paediatrics and Child Health, Faculty of Medicine, Centre for Genetic Medicine, 5th Floor Research, Genetic Medicine, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK
Centre for Paediatrics and Child Health, Faculty of Medicine, Centre for Genetic Medicine, 5th Floor Research, Genetic Medicine, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK

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P E Clayton Centre for Paediatrics and Child Health, Faculty of Medicine, Centre for Genetic Medicine, 5th Floor Research, Genetic Medicine, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK
Centre for Paediatrics and Child Health, Faculty of Medicine, Centre for Genetic Medicine, 5th Floor Research, Genetic Medicine, Institute of Human Development, Faculty of Medical and Human Sciences, University of Manchester, UK

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) and coiled-coil domain containing 8 ( CCDC8 ) (3) . CUL7 is a scaffold protein forming part of an E3 ubiquitin ligase enzyme responsible for cytoplasmic protein degradation (4) , while OBSL1 is a cytoskeletal adaptor protein which localises to the

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-13-0065
Volume/Issue:
Volume 2: Issue 4
Open access
Kelly Brewer Center for Molecular Oncology, University of Connecticut School of Medicine, Farmington, Connecticut, USA

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Isabel Nip Center for Molecular Oncology, University of Connecticut School of Medicine, Farmington, Connecticut, USA

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Justin Bellizzi Center for Molecular Oncology, University of Connecticut School of Medicine, Farmington, Connecticut, USA

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Jessica Costa-Guda Center for Molecular Oncology, University of Connecticut School of Medicine, Farmington, Connecticut, USA
Center for Regenerative Medicine and Skeletal Development, Department of Reconstructive Sciences, University of Connecticut School of Dental Medicine, Farmington, Connecticut, USA

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Andrew Arnold Center for Molecular Oncology, University of Connecticut School of Medicine, Farmington, Connecticut, USA
Division of Endocrinology and Metabolism, University of Connecticut School of Medicine, Farmington, Connecticut, USA

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components PRKN (PARK2 or Parkin), an E3 ubiquitin ligase, and FBXO4 (FBX4), a substrate recognition protein, have been implicated as important regulators of proteasomal cyclin D1 degradation and other tumor-suppressive functions ( 22 , 23 , 24 , 25

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-21-0055
Volume/Issue:
Volume 10: Issue 3
Open access
Peng Fan Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Chao-Xia Lu McKusick-Zhang Center for Genetic Medicine, State Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Di Zhang Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Kun-Qi Yang Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Pei-Pei Lu Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Ying Zhang Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Xu Meng Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Su-Fang Hao Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Fang Luo Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Ya-Xin Liu Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Hui-Min Zhang Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Lei Song Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Jun Cai Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Xue Zhang McKusick-Zhang Center for Genetic Medicine, State Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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Xian-Liang Zhou Department of Cardiology, Fuwai Hospital, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China

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-terminus and C-terminus ( 5 ). The PY motif, located within the C-terminus, is a crucial binding site for ubiquitin ligase Nedd4-2 ( 14 ). LS is mainly caused by missense mutations that alter an amino acid in the PY motif of β-ENaC or γ-ENaC and nonsense or

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-18-0484
Volume/Issue:
Volume 7: Issue 12
Open access
Kristian Almstrup Department of Growth and Reproduction, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark
International Center for Research and Research Training in Endocrine Disruption of Male Reproduction and Child Health (EDMaRC), Rigshospitalet, University of Copenhagen, Copenhagen, Denmark

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Hanne Frederiksen Department of Growth and Reproduction, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark
International Center for Research and Research Training in Endocrine Disruption of Male Reproduction and Child Health (EDMaRC), Rigshospitalet, University of Copenhagen, Copenhagen, Denmark

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Anna-Maria Andersson Department of Growth and Reproduction, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark
International Center for Research and Research Training in Endocrine Disruption of Male Reproduction and Child Health (EDMaRC), Rigshospitalet, University of Copenhagen, Copenhagen, Denmark

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Anders Juul Department of Growth and Reproduction, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark
International Center for Research and Research Training in Endocrine Disruption of Male Reproduction and Child Health (EDMaRC), Rigshospitalet, University of Copenhagen, Copenhagen, Denmark

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) CLDN9 TCS, 2,4-DCP TCS No Mainly expressed in brain. Enriched in GnRH neurons (46) DTX1 Σphth.m Σphth.m Σphth.m No Ubiquitin ligase involved in Notch signalling FAM71F1 Σphth.m TCS, 2,4-DCP, Σphth.m Σphth.m No

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-20-0286
Volume/Issue:
Volume 9: Issue 8
Open access
E T Aristizabal Prada Department of Internal Medicine IV, Campus Grosshadern, University-Hospital, Ludwig-Maximilians-University of Munich, Munich, Germany

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C J Auernhammer Department of Internal Medicine IV, Campus Grosshadern, University-Hospital, Ludwig-Maximilians-University of Munich, Munich, Germany

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reactivate or increase p27 expression in cancers, respective GEP-NETs ( Table 4 ). The E3 ubiquitin ligase S-phase kinase-associated protein 2 (Skp2) is an important mediator of ubiquitination of various proteins including p27, rendering them to subsequent

Article Type:
Review Article
DOI:
https://doi.org/10.1530/EC-17-0286
Volume/Issue:
Volume 7: Issue 1
Open access
Magdalene K Montgomery Department of Pharmacology, UNSW Medicine, School of Medical Sciences, University of New South Wales, Kensington, Sydney, New South Wales 2052, Australia

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Nigel Turner Department of Pharmacology, UNSW Medicine, School of Medical Sciences, University of New South Wales, Kensington, Sydney, New South Wales 2052, Australia

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potential Pink1 accumulates on the outer mitochondrial membrane and communicates with the E3 ubiquitin ligase Parkin. Parkin rapidly translocates to mitochondria and signals the initiation of mitophagy by ubiquinating mitochondrial proteins (VDAC1, mitofusin

Article Type:
Review Article
DOI:
https://doi.org/10.1530/EC-14-0092
Volume/Issue:
Volume 4: Issue 1
Open access