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

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...

Full description

Saved in:

Bibliographic Details
Published in:	The Journal of clinical investigation Vol. 128; no. 12; pp. 5219 - 5221
Main Authors:	Hulsurkar, Mohit, Quick, Ann P, Wehrens, Xander Ht
Format:	Journal Article
Language:	English
Published:	United States American Society for Clinical Investigation 03-12-2018
Subjects:	Ankyrins Calcium-Calmodulin-Dependent Protein Kinase Type 2 Myocytes, Cardiac Signal Transduction Spectrin STAT3 Transcription Factor
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Commentary-3 content type line 23
ISSN:	0021-9738 1558-8238
DOI:	10.1172/JCI124778