Novel roles of SUMO in pancreatic β-cells: thinking outside the nucleus

被引:16
作者
Fox, Jocelyn E. Manning [1 ,2 ]
Hajmrle, Catherine [1 ,2 ]
MacDonald, Patrick E. [1 ,2 ]
机构
[1] Univ Alberta, Dept Pharmacol, Li Ka Shing Ctr, Edmonton, AB T6G 2E1, Canada
[2] Univ Alberta, Alberta Diabet Inst, Li Ka Shing Ctr, Edmonton, AB T6G 2E1, Canada
基金
加拿大健康研究院;
关键词
SUMO; SENP; beta-cell; diabetes; insulin; exocytosis; ion channels; UBIQUITIN-LIKE PROTEIN; INSULIN SECRETORY GRANULES; SENSITIVE K+ CHANNELS; KAPPA-B-ALPHA; TRANSCRIPTIONAL ACTIVATION; DESUMOYLATING ENZYMES; REDOX REGULATION; GENE-EXPRESSION; GLUCOSE; SUMOYLATION;
D O I
10.1139/Y11-134
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
The endocrine pancreas is critically important in the regulation of energy metabolism, with defective insulin secretion from pancreatic islet beta-cells a major contributing factor to the development of type 2 diabetes. Small ubiquitin-like modifier (SUMO) proteins have been demonstrated to covalently modify a wide range of target proteins, mediating a broad range of cellular processes. While the effects of SUMOylation on beta-cell gene transcription have been previously reviewed, recent reports indicate roles for SUMO outside of the nucleus. In this review we shall focus on the reported non-nuclear roles of SUMOylation in the regulation of beta-cells, including SUMOylation as a novel signaling pathway in the acute regulation of insulin secretion.
引用
收藏
页码:765 / 770
页数:6
相关论文
共 63 条
[1]   Molecular defects in insulin secretion in type-2 diabetes [J].
Ashcroft, FM ;
Rorsman, P .
REVIEWS IN ENDOCRINE & METABOLIC DISORDERS, 2004, 5 (02) :135-142
[2]   SUMO modification regulates inactivation of the voltage-gated potassium channel Kv1.5 [J].
Benson, Mark D. ;
Li, Qiu-Ju ;
Kieckhafer, Katherine ;
Dudek, David ;
Whorton, Matthew R. ;
Sunahara, Roger K. ;
Iniguez-Lluhi, Jorge A. ;
Martens, Jeffrey R. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (06) :1805-1810
[3]   Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1 [J].
Bernier-Villamor, V ;
Sampson, DA ;
Matunis, MJ ;
Lima, CD .
CELL, 2002, 108 (03) :345-356
[4]  
Boddy MN, 1996, ONCOGENE, V13, P971
[5]  
Chen A, 1998, BIOCHEM MOL BIOL INT, V46, P1161
[6]   SUMOylation Regulates Insulin Exocytosis Downstream of Secretory Granule Docking in Rodents and Humans [J].
Dai, Xiao-Qing ;
Plummer, Greg ;
Casimir, Marina ;
Kang, Youhou ;
Hajmrle, Catherine ;
Gaisano, Herbert Y. ;
Fox, Jocelyn E. Manning ;
MacDonald, Patrick E. .
DIABETES, 2011, 60 (03) :838-847
[7]   SUMOylation regulates Kv2.1 and modulates pancreatic β-cell excitability [J].
Dai, Xiao-Qing ;
Kolic, Jelena ;
Marchi, Paolo ;
Sipione, Simonetta ;
MacDonald, Patrick E. .
JOURNAL OF CELL SCIENCE, 2009, 122 (06) :775-779
[8]   SUMO-1 modification of IκBα inhibits NF-κB activation [J].
Desterro, JMP ;
Rodriguez, MS ;
Hay, RT .
MOLECULAR CELL, 1998, 2 (02) :233-239
[9]   Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1 [J].
Desterro, JMP ;
Rodriguez, MS ;
Kemp, GD ;
Hay, RT .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (15) :10618-10624
[10]   DeSUMOylating Enzymes-SENPs [J].
Drag, Marcin ;
Salvesen, Guv S. .
IUBMB LIFE, 2008, 60 (11) :734-742