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Role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, a review dedicated to Dr. Setsuro Ebashi
- Source :
-
Biochemical & Biophysical Research Communications . Apr2008, Vol. 369 Issue 1, p135-143. 9p. - Publication Year :
- 2008
-
Abstract
- Abstract: Myosin light-chain kinase (MLCK) of smooth muscle consists of an actin-binding domain at the N-terminal, the catalytic domain in the central portion, and the myosin-binding domain at the C-terminal. The kinase activity is mediated by the catalytic domain that phosphorylates the myosin light-chain of 20kDa (MLC20), activating smooth muscle myosin to interact with actin. Although the regulatory role of the kinase activity is well established, the role of non-kinase activity derived from actin-binding and myosin-binding domains remains unknown. This review is dedicated to Dr. Setsuro Ebashi, who devoted himself to elucidating the non-kinase activity of MLCK after establishing calcium regulation through troponin in skeletal and cardiac muscles. He proposed that the actin–myosin interaction of smooth muscle could be activated by the non-kinase activity of MLCK, a mechanism that is quite independent of MLC20 phosphorylation. The authors will extend his proposal for the role of non-kinase activity. In this review, we express MLCK and its fragments as recombinant proteins to examine their effects on the actin–myosin interaction in vitro. We also down-regulate MLCK in the cultured smooth muscle cells, and propose that MLC20 phosphorylation is not obligatory for the smooth muscle to contract. [Copyright &y& Elsevier]
- Subjects :
- *MUSCULOSKELETAL system
*MUSCLE proteins
*MUSCLE cells
*CONTRACTILITY (Biology)
Subjects
Details
- Language :
- English
- ISSN :
- 0006291X
- Volume :
- 369
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Biochemical & Biophysical Research Communications
- Publication Type :
- Academic Journal
- Accession number :
- 31396564
- Full Text :
- https://doi.org/10.1016/j.bbrc.2007.11.096