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Developing Practical Therapeutic Strategies that Target Protein SUMOylation

Author(s):

Olivia F. Cox and Paul W. Huber*   Pages 1 - 10 ( 10 )

Abstract:


Post-translational modification by small ubiquitin-like modifier (SUMO) has emerged as a global mechanism for the control and integration of a wide variety of biological processes through the regulation of protein activity, stability and intracellular localization. As SUMOylation is examined in greater detail, it has become clear that the process is at the root of several pathologies including heart, endocrine, and inflammatory disease, and various types of cancer. Moreover, it is certain that perturbation of this process, either globally or of a specific protein, accounts for many instances of congenital birth defects. In order to be successful, practical strategies to ameliorate conditions due to disruptions in this post-translational modification will need to consider the multiple components of the SUMOylation machinery and the extraordinary number of proteins that undergo this modification.

Keywords:

SUMO, SUMO ligase, SENP protease, heart development, heart failure, cancer, neurodegenerative disease, congenital birth defects, spina bifida, neural tube

Affiliation:

Department of Chemistry and Biochemistry, University of Notre Dame Notre Dame, Indiana 46556, Department of Chemistry and Biochemistry, University of Notre Dame Notre Dame, Indiana 46556



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