SUMO and Its Role in Human Diseases

Kevin D. Sarge, Ok Kyong Park-Sarge

Producción científica: Chapterrevisión exhaustiva

72 Citas (Scopus)

Resumen

The covalent attachment of small ubiquition-like modifier (SUMO) polypeptides, or sumoylation, is an important regulator of the functional properties of many proteins. Among these are many proteins implicated in human diseases including cancer and Huntington's, Alzheimer's, and Parkinson's diseases, as well as spinocerebellar ataxia 1 and amyotrophic lateral sclerosis. The results of two more recent studies identify two additional human disease-associated proteins that are sumoylated, amyloid precursor protein (APP), and lamin A. APP sumoylation modulates Aβ peptide levels, suggesting a potential role in Alzheimer's disease, and decreased lamin A sumoylation due to mutations near its SUMO site has been implicated in causing some forms of familial dilated cardiomyopathy.

Idioma originalEnglish
Título de la publicación alojadaInternational Review of Cell and Molecular Biology
Páginas167-183
Número de páginas17
DOI
EstadoPublished - 2011

Serie de la publicación

NombreInternational Review of Cell and Molecular Biology
Volumen288
ISSN (versión impresa)1937-6448

Nota bibliográfica

Funding Information:
The authors acknowledge the support of NIH grants GM61053 and GM64606 to K. D. S., which enabled us to perform our studies cited in this review.

Financiación

The authors acknowledge the support of NIH grants GM61053 and GM64606 to K. D. S., which enabled us to perform our studies cited in this review.

FinanciadoresNúmero del financiador
National Institutes of Health (NIH)GM64606
National Institute of General Medical SciencesR01GM061053

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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