Modulation of myosin filament activation by telokin in smooth muscle

Sobieszek, Apolinary; Andruchov, Oleg; Grabarek, Zenon; Kulikova, Natalia; Liebetrau, Claudia; Matusovsky, Oleg S.

doi:10.1016/j.bpc.2004.07.038

Cited by 15 publications

(6 citation statements)

References 45 publications

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“…It has also been suggested that MLCK moves on myosin filaments in a myosin-assisted manner (69, 70). This idea arose from kinetic studies of the rate of phosphorylation of SMM in solution with known low amounts of added MLCK-CaM.…”

Section: Mlck Enzyme Activitymentioning

confidence: 99%

Biochemistry of smooth muscle myosin light chain kinase

Hong

Haldeman

Jackson

et al. 2011

Archives of Biochemistry and Biophysics

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The smooth muscle isoform of myosin light chain kinase (MLCK) is a Ca2+-calmodulin-activated kinase that is found in many tissues. It is particularly important for regulating smooth muscle contraction by phosphorylation of myosin. This review summarizes selected aspects of recent biochemical work on MLCK that pertains to its function in smooth muscle. In general, the focus of the review is on new findings, unresolved issues, and areas with the potential for high physiological significance that need further study. The review includes a concise summary of the structure, substrates, and enzyme activity, followed by a discussion of the factors that may limit the effective activity of MLCK in the muscle. The interactions of each of the many domains of MLCK with the proteins of the contractile apparatus, and the multi-domain interactions of MLCK that may control its behaviors in the cell are summarized. Finally, new in vitro approaches to studying the mechanism of phosphorylation of myosin are introduced.

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Section: Mlck Enzyme Activitymentioning

confidence: 99%

Biochemistry of smooth muscle myosin light chain kinase

Hong

Haldeman

Jackson

et al. 2011

Archives of Biochemistry and Biophysics

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“…Performing the intermediate extraction of MLCK with KES results in distinct crude actomyosin and subsequent types of myosin. The content of co-purified or endogenous CaM/MLCK complex is 3-4-fold lower with the MLCK extraction step than without it [38].…”

Section: Purification Of Cam Mlck and Mlcpmentioning

confidence: 91%

“…CaM acts as an activator of the MLCK, and TL acts as an inhibitor. TL slows down the phosphorylation produced by MLCK and accelerates the inhibitory effect of MLCP, both located on the myosin filaments [38]. TL also reduces the affinity of MLCK for myosin filaments, thereby reducing the myosin phosphorylation rate but not the level of phosphorylation [38].…”

Section: Myosin Filament Assembly and Copurification Of The Regulator...mentioning

confidence: 99%

“…TL slows down the phosphorylation produced by MLCK and accelerates the inhibitory effect of MLCP, both located on the myosin filaments [38]. TL also reduces the affinity of MLCK for myosin filaments, thereby reducing the myosin phosphorylation rate but not the level of phosphorylation [38]. In the absence of Ca 2+ or at its nanomolar range of concentration, CaM/MLCK becomes inactivated [39,40].…”

Section: Myosin Filament Assembly and Copurification Of The Regulator...mentioning

confidence: 99%

“…MLCP co-purifies with myosin but at an approximately 20-50-fold lower stoichiometric ratio than MLCK [23]. Detailed molar ratios of the endogenous MLCK, CaM, and MLCP in the native-like filamentous myosin preparations can be found in Table 1 of Sobieszek et al [38].…”

Section: Quantification Of the Endogenous Kinase Complex In Myosinmentioning

confidence: 99%

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Purification of Myosin from Bovine Tracheal Smooth Muscle, Filament Formation and Endogenous Association of Its Regulatory Complex

Wang

Sobieszek

Seow

et al. 2023

Cells

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Dynamic regulation of myosin filaments is a crucial factor in the ability of airway smooth muscle (ASM) to adapt to a wide length range. Increased stability or robustness of myosin filaments may play a role in the pathophysiology of asthmatic airways. Biochemical techniques for the purification of myosin and associated regulatory proteins could help elucidate potential alterations in myosin filament properties of asthmatic ASM. An effective myosin purification approach was originally developed for chicken gizzard smooth muscle myosin. More recently, we successfully adapted the procedure to bovine tracheal smooth muscle. This method yields purified myosin with or without the endogenous regulatory complex of myosin light chain kinase and myosin light chain phosphatase. The tight association of the regulatory complex with the assembled myosin filaments can be valuable in functional experiments. The purification protocol discussed here allows for enzymatic comparisons of myosin regulatory proteins. Furthermore, we detail the methodology for quantification and removal of the co-purified regulatory enzymes as a tool for exploring potentially altered phenotypes of the contractile apparatus in diseases such as asthma.

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Self-assembly of smooth muscle myosin filaments: adaptation of filament length by telokin and Mg·ATP

Sobieszek

2022

Eur Biophys J

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Modulation of myosin filament activation by telokin in smooth muscle

Cited by 15 publications

References 45 publications

Biochemistry of smooth muscle myosin light chain kinase

Biochemistry of smooth muscle myosin light chain kinase

Purification of Myosin from Bovine Tracheal Smooth Muscle, Filament Formation and Endogenous Association of Its Regulatory Complex

Self-assembly of smooth muscle myosin filaments: adaptation of filament length by telokin and Mg·ATP

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