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Myosin light chain kinase: pulling the strings of epithelial tight junction function
Author(s) -
Cunningham Kevin E.,
Turner Jerrold R.
Publication year - 2012
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2012.06526.x
Subject(s) - myosin light chain kinase , tight junction , paracellular transport , microbiology and biotechnology , myosin , myosin light chain phosphatase , barrier function , cell junction , rho associated protein kinase , phosphorylation , immunoglobulin light chain , chemistry , biology , permeability (electromagnetism) , biochemistry , immunology , cell , membrane , antibody
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.