Sumoylation and human disease pathogenesis

Kevin D. Sarge; Ok Kyong Park-Sarge

doi:10.1016/j.tibs.2009.01.004

Sumoylation and human disease pathogenesis

Kevin D. Sarge, Ok Kyong Park-Sarge

Research output: Contribution to journal › Review article › peer-review

125 Scopus citations

Abstract

Covalent modification by SUMO polypeptides, or sumoylation, is an important regulator of the functional properties of many proteins. Among these are several proteins implicated in human diseases including cancer, Huntington's, Alzheimer's, and Parkinson's diseases, as well as spinocerebellar ataxia 1 and amyotrophic lateral sclerosis. Recent reports reveal two new examples of human disease-associated proteins that are SUMO modified: amyloid precursor protein and lamin A. These findings point to a function for sumoylation in modulating amyloid-β peptide levels, indicating a potential role in Alzheimer's disease, and for decreased lamin A sumoylation as a causative factor in familial dilated cardiomyopathy.

Original language	English
Pages (from-to)	200-205
Number of pages	6
Journal	Trends in Biochemical Sciences
Volume	34
Issue number	4
DOIs	https://doi.org/10.1016/j.tibs.2009.01.004
State	Published - Apr 2009

Bibliographical note

Funding Information:
We apologize to colleagues whose work we could not cite directly owing to space constraints. The authors would like to acknowledge the support of NIH grants GM61053 and GM64606 to K.D.S.

ASJC Scopus subject areas

Biochemistry
Molecular Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.tibs.2009.01.004

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abstract = "Covalent modification by SUMO polypeptides, or sumoylation, is an important regulator of the functional properties of many proteins. Among these are several proteins implicated in human diseases including cancer, Huntington's, Alzheimer's, and Parkinson's diseases, as well as spinocerebellar ataxia 1 and amyotrophic lateral sclerosis. Recent reports reveal two new examples of human disease-associated proteins that are SUMO modified: amyloid precursor protein and lamin A. These findings point to a function for sumoylation in modulating amyloid-β peptide levels, indicating a potential role in Alzheimer's disease, and for decreased lamin A sumoylation as a causative factor in familial dilated cardiomyopathy.",

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AU - Park-Sarge, Ok Kyong

N1 - Funding Information: We apologize to colleagues whose work we could not cite directly owing to space constraints. The authors would like to acknowledge the support of NIH grants GM61053 and GM64606 to K.D.S.

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AB - Covalent modification by SUMO polypeptides, or sumoylation, is an important regulator of the functional properties of many proteins. Among these are several proteins implicated in human diseases including cancer, Huntington's, Alzheimer's, and Parkinson's diseases, as well as spinocerebellar ataxia 1 and amyotrophic lateral sclerosis. Recent reports reveal two new examples of human disease-associated proteins that are SUMO modified: amyloid precursor protein and lamin A. These findings point to a function for sumoylation in modulating amyloid-β peptide levels, indicating a potential role in Alzheimer's disease, and for decreased lamin A sumoylation as a causative factor in familial dilated cardiomyopathy.

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Sumoylation and human disease pathogenesis

Abstract

Bibliographical note

ASJC Scopus subject areas

UN SDGs

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