SUMO Wrestling with Type 1 Diabetes

Overview

Journal J Mol Med (Berl)

Specialty General Medicine

Date 2005 Apr 5

PMID 15806321

Citations 34

Authors

Manyu Li

Dehuang Guo

Carlos M Isales

Decio L Eizirik

Mark Atkinson

Jin-Xiong She

Cong-Yi Wang

Affiliations

Soon will be listed here.

Abstract

Post-translational modification of proteins by phosphorylation, methylation, acetylation, or ubiquitylation represent central mechanisms through which various biological processes are regulated. Reversible covalent modification (i.e., sumoylation) of proteins by the small ubiquitin-like modifier (SUMO) has also emerged as an important mechanism contributing to the dynamic regulation of protein function. Sumoylation has been linked to the pathogenesis of a variety of disorders including Alzheimer's disease (AD), Huntington's disease (HD), and type 1 diabetes (T1D). Advances in our understanding of the role of sumoylation suggested a novel regulatory mechanism for the regulation of immune responsive gene expression. In this review, we first update recent advances in the field of sumoylation, then specifically evaluate its regulatory role in several key signaling pathways for immune response and discuss its possible implication in T1D pathogenesis.

Citing Articles

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Wang J, Zhang R, Wu C, Wang L, Liu P, Li P Front Pharmacol. 2024; 15:1432724.

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Ubiquitin-conjugating enzyme E2 for regulating autophagy in diabetic cardiomyopathy: A mini-review.

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Regulation of insulin secretion by the post-translational modifications.

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Holoman N, Aiello J, Trobenter T, Tarchick M, Kozlowski M, Makowski E J Neurosci. 2021; 41(14):3275-3299.

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Loss of ubiquitin-conjugating enzyme E2 (Ubc9) in macrophages exacerbates multiple low-dose streptozotocin-induced diabetes by attenuating M2 macrophage polarization.

Wang F, Sun F, Luo J, Yue T, Chen L, Zhou H Cell Death Dis. 2019; 10(12):892.

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