STAT3: a link between CaMKII-βIV-spectrin and maladaptive remodeling?

J Clin Invest. 2018 Dec 3;128(12):5219-5221. doi: 10.1172/JCI124778. Epub 2018 Nov 12.


βIV-Spectrin, along with ankyrin and Ca2+/calmodulin-dependent kinase II (CaMKII), has been shown to form local signaling domains at the intercalated disc, while playing a key role in the regulation of Na+ and K+ channels in cardiomyocytes. In this issue of the JCI, Unudurthi et al. show that under chronic pressure overload conditions, CaMKII activation leads to βIV-spectrin degradation, resulting in the release of sequestered STAT3 from the intercalated discs. This in turn leads to dysregulation of STAT3-mediated gene transcription, maladaptive remodeling, fibrosis, and decreased cardiac function. Overall, this study presents interesting findings regarding the role of CaMKII and βIV-spectrin under physiological as well as pathological conditions.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Comment

MeSH terms

  • Ankyrins
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2*
  • Myocytes, Cardiac
  • STAT3 Transcription Factor
  • Signal Transduction
  • Spectrin*


  • Ankyrins
  • STAT3 Transcription Factor
  • Spectrin
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2