Is Desmin Propensity to Aggregate Part of its Protective Function?

Sonia R. Singh, Hikmet Kadioglu, Krishna Patel, Lucie Carrier, Giulio Agnetti

Research output: Contribution to journalReview articlepeer-review

5 Scopus citations


Desmin is the major protein component of the intermediate filaments (IFs) cytoskeleton in muscle cells, including cardiac. The accumulation of cleaved and misfolded desmin is a cellular hallmark of heart failure (HF). These desmin alterations are reversed by therapy, suggesting a causal role for the IFs in the development of HF. Though IFs are known to play a role in the protection from stress, a mechanistic model of how that occurs is currently lacking. On the other hand, the heart is uniquely suited to study the function of the IFs, due to its inherent, cyclic contraction. That is, HF can be used as a model to address how IFs afford protection from mechanical, and possibly redox, stress. In this review we provide a brief summary of the current views on the function of the IFs, focusing on desmin. We also propose a new model according to which the propensity of desmin to aggregate may have been selected during evolution as a way to dissipate excessive mechanical and possibly redox stress. According to this model, though desmin misfolding may afford protection from acute injury, the sustained or excessive accumulation of desmin aggregates could impair proteostasis and contribute to disease.

Original languageEnglish (US)
Article number1528
Issue number2
StatePublished - Feb 20 2020


  • desmin
  • heart failure
  • intermediate filaments
  • protein misfolding and aggregation

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology


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