Myosin light chain kinase: pulling the strings of epithelial tight junction function.
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.
Department of Pathology, University of Chicago, Chicago, Illinois, USA.
Kevin E
KE
Cunningham
Jerrold R
JR
Turner
D000818:Animals; D003424:Crohn Disease / Q000201:enzymology / Q000503:physiopathology; D018450:Disease Progression; D006801:Humans; D007413:Intestinal Mucosa / Q000201:enzymology / Q000502:physiology*; D009219:Myosin-Light-Chain Kinase / Q000378:metabolism*; D019108:Tight Junctions / Q000201:enzymology / Q000502:physiology*; D014409:Tumor Necrosis Factor-alpha / Q000502:physiology
D014409:Tumor Necrosis Factor-alpha; D009219:Myosin-Light-Chain Kinase