Myosin light chain kinases

@article{Gallagher2004MyosinLC,
  title={Myosin light chain kinases},
  author={Patricia J. Gallagher and B. PAUL HERRING and James T Stull},
  journal={Journal of Muscle Research \& Cell Motility},
  year={2004},
  volume={18},
  pages={1-16}
}
A remarkable variety of extracellular signalling molecules effect signal transduction by receptormediated increases in cytosolic Ca2‡ concentration. This Ca2‡ response is a central event for the regulation or modulation of many cell processes, including those dependent upon actin-activation of the myosin II motor protein. In the case of striated muscles, Ca2‡ binds to the thin filament regulatory protein troponin allowing actin to activate sarcomeric myosin MgATPase, bringing about muscle… 

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Whether Ca2+ is required for tension maintenance of an agonist induced contraction using the membrane permeant form of the caged Ca-chelator, diazo2, is tested.

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The varied activities of these major signaling pathways endow SMCs with different contractile profiles such as phasic and tonic contractions to meet the diversified physiological requirements.

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A CaM-independent activation mechanism for smMLCK by mechanical release of the inhibitory elements is investigated via high throughput AFM single-molecule force spectroscopy, indicating restored substrate-binding capability due to mechanically induced removal of the auto-inhibitory regulatory region.

Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase.

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Smooth Muscle Myosin Phosphatase-associated Kinase Induces Ca2+ Sensitization via Myosin Phosphatase Inhibition*

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Using an antibody that specifically recognizes MYPT1 phosphorylated at Thr654(M130 numbering), it is determined that this calcium-independent contraction in β-escin-permeabilized rabbit ileal smooth muscle was correlated with an increase in MYPT 1 phosphorylation.

Biochemistry of smooth muscle myosin light chain kinase.

Regulation of myosin light chain kinase and telokin expression in smooth muscle tissues.

TLDR
Some of the recent studies that have described the transcriptional regulation of mylk1 gene products in smooth muscle tissues are highlighted and the implications of these findings for regulation of expression of other smooth muscle-specific genes are discussed.

Calponin (CaP) as a latch-bridge protein — a new concept in regulation of contractility in smooth muscles

  • P. Szymanski
  • Biology
    Journal of Muscle Research & Cell Motility
  • 2004
TLDR
It is proposed that CaP tethers thin and thick filaments and this CaP effect is exerted when its central part binds to F-actin, whereas the NH2-terminal half simultaneously interacts with phosphorylated MRLC.

Vectorial phosphorylation of filamentous smooth muscle myosin by calmodulin and myosin light chain kinase complex

  • A. Sobieszek
  • Biology, Chemistry
    Journal of Muscle Research & Cell Motility
  • 2004
TLDR
Phosphorylation progress curves obtained from mixtures of the native-like, and CaM- and MLCK-free filaments indicated that the CaM/MLCK complex preferentially phosphorylation its parent filaments and, as result, the whole myosin present was not maximally phosphorylated.
...

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