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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kudryashov DS,Chibalina MV,Birukov KG,Lukas TJ,Sellers JR,Van Eldik LJ,Watterson DM,Shirinsky VP

doi

10.1016/s0014-5793(99)01591-4

keywords:

subject

Has Abstract

pub_date

1999-12-10 00:00:00

pages

67-71

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(99)01591-4

journal_volume

463

pub_type

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