Abstract
The SUMOylation pathway is involved in the regulation of numerous and diverse cellular functions, nuclear as well as extra-nuclear. Thus, it is not surprising that SUMO pathway components are implicated in diseases as diverse as cystic fibrosis, cancer and neurodegenerative diseases. Therefore, the components of the SUMOylation pathway should provide valid therapeutic targets for manipulation. While the related ubiquitylation system encompasses a vast number of enzymes as potential drug targets, there are only a handful of components that comprise the SUMOylation cascade. Whereas this alleviates the problem of target redundancy, it may complicate the potential to achieve drug specificity. The development of small molecule inhibitors aimed at SUMO pathway components is in its early stages. This review provides an outline of the pathway and summarizes drug development efforts targeted at individual SUMOylation pathway components, with an emphasis on how CFTR protein processing may be affected.
Keywords: SAE1/SAE2, Ubc9, SUMO E3, Hsp27, SUMO, SUMOpeptidases, SUMO interaction motif (SIM).
Current Drug Targets
Title:SUMOylation Modulates CFTR Biogenesis: Is the Pathway Druggable?
Volume: 16 Issue: 9
Author(s): Annette Ahner and Raymond A. Frizzell
Affiliation:
Keywords: SAE1/SAE2, Ubc9, SUMO E3, Hsp27, SUMO, SUMOpeptidases, SUMO interaction motif (SIM).
Abstract: The SUMOylation pathway is involved in the regulation of numerous and diverse cellular functions, nuclear as well as extra-nuclear. Thus, it is not surprising that SUMO pathway components are implicated in diseases as diverse as cystic fibrosis, cancer and neurodegenerative diseases. Therefore, the components of the SUMOylation pathway should provide valid therapeutic targets for manipulation. While the related ubiquitylation system encompasses a vast number of enzymes as potential drug targets, there are only a handful of components that comprise the SUMOylation cascade. Whereas this alleviates the problem of target redundancy, it may complicate the potential to achieve drug specificity. The development of small molecule inhibitors aimed at SUMO pathway components is in its early stages. This review provides an outline of the pathway and summarizes drug development efforts targeted at individual SUMOylation pathway components, with an emphasis on how CFTR protein processing may be affected.
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Cite this article as:
Ahner Annette and Frizzell A. Raymond, SUMOylation Modulates CFTR Biogenesis: Is the Pathway Druggable?, Current Drug Targets 2015; 16 (9) . https://dx.doi.org/10.2174/1389450116666150531152236
DOI https://dx.doi.org/10.2174/1389450116666150531152236 |
Print ISSN 1389-4501 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-5592 |
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