Myosin light chain kinase: pulling the strings of epithelial tight junction function
Version of Record online: 25 JUN 2012
© 2012 New York Academy of Sciences.
Annals of the New York Academy of Sciences
Volume 1258, Barriers and Channels Formed by Tight Junction Proteins II pages 34–42, July 2012
How to Cite
Cunningham, K. E. and Turner, J. R. (2012), Myosin light chain kinase: pulling the strings of epithelial tight junction function. Annals of the New York Academy of Sciences, 1258: 34–42. doi: 10.1111/j.1749-6632.2012.06526.x
- Issue online: 25 JUN 2012
- Version of Record online: 25 JUN 2012
- tight junction;
- myosin light chain kinase;
- inflammatory bowel disease
Dynamic regulation of paracellular permeability is essential for physiological epithelial function, while dysregulated permeability is common in disease. The recent elucidation of the molecular composition of the epithelial tight junction complex has been accompanied by characterization of diverse intracellular mediators of paracellular permeabiltiy. Myosin light chain kinase (MLCK), which induces contraction of the perijunctional actomyosin ring through myosin II regulatory light chain phosphorylation, has emerged as a key regulator of tight junction permeability. Examination of the regulation and role of MLCK in tight junction dysfunction has helped to define pathological processes and characterize the role of barrier loss in disease pathogenesis, and may provide future therapeutic targets to treat intestinal disease.