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¹ Department of Cell and Molecular Biology, R.H. Lurie Comprehensive Cancer Center and Center for Genetic Medicine, Northwestern University Medical School, Chicago, IL 60611
² Department of Physiology, Indiana University School of Medicine, Indianapolis, IN 46202
³ Department of Molecular Biology and Biochemistry, Rutgers University, Nelson Labs, Busch Campus, Piscataway, NJ 08855

Address correspondence to Rex L. Chisholm, Department of Cell and Molecular Biology, 303 E. Chicago Ave., Northwestern University Medical School, Chicago, IL 60611. Tel.: (312) 503-4151. Fax: (312) 503-5994. E-mail: r-chisholm{at}nwu.edu

Approaches with high spatial and temporal resolution are required to understand the regulation of nonmuscle myosin II in vivo. Using fluorescence resonance energy transfer we have produced a novel biosensor allowing simultaneous determination of myosin light chain kinase (MLCK) localization and its [Ca²⁺]₄/calmodulin-binding state in living cells. We observe transient recruitment of diffuse MLCK to stress fibers and its in situ activation before contraction. MLCK is highly active in the lamella of migrating cells, but not at the retracting tail. This unexpected result highlights a potential role for MLCK-mediated myosin contractility in the lamella as a driving force for migration. During cytokinesis, MLCK was enriched at the spindle equator during late metaphase, and was maximally activated just before cleavage furrow constriction. As furrow contraction was completed, active MLCK was redistributed to the poles of the daughter cells. These results show MLCK is a myosin regulator in the lamella and contractile ring, and pinpoints sites where myosin function may be mediated by other kinases.

Key Words: myosin light chain kinase; myosin light chains; phosphorylation; cell division; FRET

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