Unique sequence of a high molecular weight myosin light chain kinase is involved in interaction with actin cytoskeleton

Dmitry S. Kudryashov; Margarita V. Chibalina; Konstantin G. Birukov; Thomas J. Lukas; James R. Sellers; Linda J. Van Eldik; D. Martin Watterson; Vladimir P. Shirinsky

doi:10.1016/S0014-5793(99)01591-4

Unique sequence of a high molecular weight myosin light chain kinase is involved in interaction with actin cytoskeleton

Dmitry S. Kudryashov
, Margarita V. Chibalina
, Konstantin G. Birukov
, Thomas J. Lukas
, James R. Sellers
, Linda J. Van Eldik
, D. Martin Watterson
, Vladimir P. Shirinsky

Research output: Contribution to journal › Article › peer-review

38 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	67-71
Number of pages	5
Journal	FEBS Letters
Volume	463
Issue number	1-2
DOIs	https://doi.org/10.1016/S0014-5793(99)01591-4
State	Published - Dec 10 1999

Bibliographical note

Funding 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.).

Funding

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.).

Funders	Funder number
National Institutes of Health (NIH)	RR13810
Howard Hughes Medical Institute	75195
National Institute of General Medical Sciences	R01GM030861

Keywords

Calmodulin
Cytoskeleton
Microfilament
Myosin light chain kinase

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(99)01591-4

Cite this

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title = "Unique sequence of a high molecular weight myosin light chain kinase is involved in interaction with actin cytoskeleton",

abstract = "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.",

keywords = "Calmodulin, Cytoskeleton, Microfilament, Myosin light chain kinase",

author = "Kudryashov, \{Dmitry S.\} and Chibalina, \{Margarita V.\} and Birukov, \{Konstantin G.\} and Lukas, \{Thomas J.\} and Sellers, \{James R.\} and \{Van Eldik\}, \{Linda J.\} and Watterson, \{D. Martin\} and Shirinsky, \{Vladimir P.\}",

note = "Funding 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.). ",

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doi = "10.1016/S0014-5793(99)01591-4",

language = "English",

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AU - Kudryashov, Dmitry S.

AU - Chibalina, Margarita V.

AU - Birukov, Konstantin G.

AU - Lukas, Thomas J.

AU - Sellers, James R.

AU - Van Eldik, Linda J.

AU - Watterson, D. Martin

AU - Shirinsky, Vladimir P.

N1 - Funding 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.).

PY - 1999/12/10

Y1 - 1999/12/10

N2 - 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.

AB - 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.

KW - Calmodulin

KW - Cytoskeleton

KW - Microfilament

KW - Myosin light chain kinase

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Unique sequence of a high molecular weight myosin light chain kinase is involved in interaction with actin cytoskeleton

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

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