The cellular modifier MOAG-4/SERF drives amyloid formation through charge complementation

How aging causes relatively common diseases such as Alzheimer’s and Parkinson’s is still a mystery. Since toxic structural changes in proteins are likely to be responsible, Pras et al. investigated biological mechanisms that could drive such changes. The authors made use of a modifying factor called SERF, a human protein that can accelerate structural changes and aggregation of several disease-related proteins. Through a peptide-binding screen, the authors found that SERF2 acts on negatively charged protein regions. Removing positive charge in SERF was sufficient to suppress protein aggregation and toxicity in models for disease. The authors propose that blocking charge-interactions with SERF or related cellular modifiers could be explored as an approach to treat age-related protein toxicity.

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