Myosin light chain kinase (MLCK) is the key regulator of cell motility and smooth muscle contraction in higher vertebrates. We searched for the features of the high molecular weight MLCK (MLCK-210) associated with its unique N-terminal sequence not found in a more ubiquitous lower molecular weight MLCK (MLCK-108). MLCK-210 demonstrates stronger association with the Triton-insoluble cytoskeletons than MLCK-108, suggesting the role for this sequence in subcellular targeting. Indeed, the expressed unique domain of MLCK-210 binds and bundles F-actin in vitro and colocalises with the microfilaments in transfected cells reproducing endogenous MLCK-210 distribution. Thus, MLCK-210 features an extensive actin binding interface and, perhaps, acts as an actin cytoskeleton stabiliser.
|Number of pages||5|
|State||Published - Dec 10 1999|
Bibliographical noteFunding Information:
We thank Drs T. Vlasik and V. Spirov (Cardiology Research Center, Moscow, Russia) for producing 2F4 monoclonal antibody for us and J.P. Schavocky (Northwestern University, Chicago, IL, USA) for his technical assistance. We are grateful to Dr A. Bresnick (Albert Einstein College of Medicine, Bronx, NY, USA) for providing a plasmid containing chicken MLCK-210-GFP construct and to Dr A. Vorotnikov (Cardiology Research Center, Moscow, Russia) for critical comments and help with the manuscript. This work was supported in part by HHMI International Scholar award 75195 (V.P.S.) and NIH Grants GM30861 and RR13810 (D.M.W.).
- Myosin light chain kinase
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
- Cell Biology