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 Lettjournal_title
FEBS lettersauthors
Kudryashov DS,Chibalina MV,Birukov KG,Lukas TJ,Sellers JR,Van Eldik LJ,Watterson DM,Shirinsky VPdoi
10.1016/s0014-5793(99)01591-4keywords:
subject
Has Abstractpub_date
1999-12-10 00:00:00pages
67-71issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01591-4journal_volume
463pub_type
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