Sumoylation and human disease pathogenesis

Research output: Contribution to journalReview articlepeer-review

121 Scopus citations


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 languageEnglish
Pages (from-to)200-205
Number of pages6
JournalTrends in Biochemical Sciences
Issue number4
StatePublished - 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


Dive into the research topics of 'Sumoylation and human disease pathogenesis'. Together they form a unique fingerprint.

Cite this