Caldesmon binds to smooth muscle myosin and myosin rod and crosslinks thick filaments to actin filaments

1992 ◽  
Vol 13 (2) ◽  
pp. 206-218 ◽  
Author(s):  
Steven Marston ◽  
Katalin Pinter ◽  
Pauline Bennett
Keyword(s):  
Smooth Muscle ◽  
Actin Filaments ◽  
Smooth Muscle Myosin ◽  
Thick Filaments ◽  
Muscle Myosin ◽  
Myosin Rod

scholarly journals Light chain phosphorylation regulates the movement of smooth muscle myosin on actin filaments.

1985 ◽  
Vol 101 (5) ◽  
pp. 1897-1902 ◽  
Author(s):  
J R Sellers ◽  
J A Spudich ◽  
M P Sheetz
Keyword(s):  
Smooth Muscle ◽  
Actin Filaments ◽  
Smooth Muscles ◽  
Smooth Muscle Myosin ◽  
Vitro Assay ◽  
Skeletal Muscle Myosin ◽  
Myosin Filaments ◽  
Muscle Myosin ◽  
Rate Of Movement

In smooth muscles there is no organized sarcomere structure wherein the relative movement of myosin filaments and actin filaments has been documented during contraction. Using the recently developed in vitro assay for myosin-coated bead movement (Sheetz, M.P., and J.A. Spudich, 1983, Nature (Lond.)., 303:31-35), we were able to quantitate the rate of movement of both phosphorylated and unphosphorylated smooth muscle myosin on ordered actin filaments derived from the giant alga, Nitella. We found that movement of turkey gizzard smooth muscle myosin on actin filaments depended upon the phosphorylation of the 20-kD myosin light chains. About 95% of the beads coated with phosphorylated myosin moved at velocities between 0.15 and 0.4 micron/s, depending upon the preparation. With unphosphorylated myosin, only 3% of the beads moved and then at a velocity of only approximately 0.01-0.04 micron/s. The effects of phosphorylation were fully reversible after dephosphorylation with a phosphatase prepared from smooth muscle. Analysis of the velocity of movement as a function of phosphorylation level indicated that phosphorylation of both heads of a myosin molecule was required for movement and that unphosphorylated myosin appears to decrease the rate of movement of phosphorylated myosin. Mixing of phosphorylated smooth muscle myosin with skeletal muscle myosin which moves at 2 microns/s resulted in a decreased rate of bead movement, suggesting that the more slowly cycling smooth muscle myosin is primarily determining the velocity of movement in such mixtures.

scholarly journals Muscle myosins form folded monomers, dimers, and tetramers during filament polymerization in vitro

2020 ◽  
Vol 117 (27) ◽  
pp. 15666-15672
Author(s):  
Xiong Liu ◽  
Shi Shu ◽  
Edward D. Korn
Keyword(s):  
Electron Microscopy ◽  
Smooth Muscle ◽  
Muscle Contraction ◽  
Actin Filaments ◽  
Critical Concentration ◽  
Smooth Muscle Myosin ◽  
Myosin Filaments ◽  
Muscle Myosin

Muscle contraction depends on the cyclical interaction of myosin and actin filaments. Therefore, it is important to understand the mechanisms of polymerization and depolymerization of muscle myosins. Muscle myosin 2 monomers exist in two states: one with a folded tail that interacts with the heads (10S) and one with an unfolded tail (6S). It has been thought that only unfolded monomers assemble into bipolar and side-polar (smooth muscle myosin) filaments. We now show by electron microscopy that, after 4 s of polymerization in vitro in both the presence (smooth muscle myosin) and absence of ATP, skeletal, cardiac, and smooth muscle myosins form tail-folded monomers without tail–head interaction, tail-folded antiparallel dimers, tail-folded antiparallel tetramers, unfolded bipolar tetramers, and small filaments. After 4 h, the myosins form thick bipolar and, for smooth muscle myosin, side-polar filaments. Nonphosphorylated smooth muscle myosin polymerizes in the presence of ATP but with a higher critical concentration than in the absence of ATP and forms only bipolar filaments with bare zones. Partial depolymerization in vitro of nonphosphorylated smooth muscle myosin filaments by the addition of MgATP is the reverse of polymerization.

scholarly journals The Crystal Structure of the N-terminal 15 Heptads of Smooth Muscle Myosin Rod Offers Insights into the Inhibited State of Myosin

2010 ◽  
Vol 98 (3) ◽  
pp. 414a
Author(s):  
Usha B. Nair ◽  
Patricia M. Fagnant ◽  
Susan Lowey ◽  
Mark A. Rould ◽  
Kathleen M. Trybus
Keyword(s):  
Crystal Structure ◽  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Muscle Myosin ◽  
Myosin Rod

scholarly journals The Kinetics Underlying the Velocity of Smooth Muscle Myosin Filament Sliding on Actin Filaments in vitro

2015 ◽  
Vol 108 (2) ◽  
pp. 9a
Author(s):  
Brian D. Haldeman ◽  
Richard K. Brizendine ◽  
Diego Alcala ◽  
Kevin C. Facemyer ◽  
Josh E. Baker ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Actin Filaments ◽  
Smooth Muscle Myosin ◽  
Myosin Filament ◽  
Muscle Myosin

In Vitro Movement of Actin Filaments on Gizzard Smooth Muscle Myosin: Requirement of Phosphorylation of Myosin Light Chain and Effects of Tropomyosin and Caldesmon1

1991 ◽  
Vol 109 (6) ◽  
pp. 858-866 ◽  
Author(s):  
Tsuyoshi Okagaki ◽  
Sugie Higashi-Fujime ◽  
Ryoki Ishikawa ◽  
Hiromi Takano-Ohmuro ◽  
Kazuhiro Kohama
Keyword(s):  
Smooth Muscle ◽  
Light Chain ◽  
Actin Filaments ◽  
Myosin Light Chain ◽  
Smooth Muscle Myosin ◽  
Muscle Myosin

Unfolding Domains in Smooth Muscle Myosin Rod

Biochemistry ◽  
1995 ◽  
Vol 34 (20) ◽  
pp. 6770-6774 ◽  
Author(s):  
Lan King ◽  
John C. Seidel ◽  
Sherwin S. Lehrer
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Muscle Myosin ◽  
Myosin Rod

Bending of smooth muscle myosin rod

FEBS Letters ◽  
1984 ◽  
Vol 176 (1) ◽  
pp. 197-201 ◽  
Author(s):  
R.A. Cross
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Muscle Myosin ◽  
Myosin Rod

scholarly journals Actin-facilitated assembly of smooth muscle myosin induces formation of actomyosin fibrils

1992 ◽  
Vol 117 (6) ◽  
pp. 1223-1230 ◽  
Author(s):  
D Applegate ◽  
JD Pardee
Keyword(s):  
Smooth Muscle ◽  
Actin Filament ◽  
Active Sites ◽  
Atp Hydrolysis ◽  
Thick Filament ◽  
Smooth Muscle Myosin ◽  
Fiber Assembly ◽  
Thick Filaments ◽  
Filament Networks ◽  
Muscle Myosin

To identify regulatory mechanisms potentially involved in formation of actomyosin structures in smooth muscle cells, the influence of F-actin on smooth muscle myosin assembly was examined. In physiologically relevant buffers, AMPPNP binding to myosin caused transition to the soluble 10S myosin conformation due to trapping of nucleotide at the active sites. The resulting 10S myosin-AMPPNP complex was highly stable and thick filament assembly was suppressed. However, upon addition to F-actin, myosin readily assembled to form thick filaments. Furthermore, myosin assembly caused rearrangement of actin filament networks into actomyosin fibers composed of coaligned F-actin and myosin thick filaments. Severin-induced fragmentation of actin in actomyosin fibers resulted in immediate disassembly of myosin thick filaments, demonstrating that actin filaments were indispensable for mediating myosin assembly in the presence of AMPPNP. Actomyosin fibers also formed after addition of F-actin to nonphosphorylated 10S myosin monomers containing the products of ATP hydrolysis trapped at the active site. The resulting fibers were rapidly disassembled after addition of millimolar MgATP and consequent transition of myosin to the soluble 10S state. However, reassembly of myosin filaments in the presence of MgATP and F-actin could be induced by phosphorylation of myosin P-light chains, causing regeneration of actomyosin fiber bundles. The results indicate that actomyosin fibers can be spontaneously formed by F-actin-mediated assembly of smooth muscle myosin. Moreover, induction of actomyosin fibers by myosin light chain phosphorylation in the presence of actin filament networks provides a plausible hypothesis for contractile fiber assembly in situ.

scholarly journals Solubility-determining domain of smooth muscle myosin rod

FEBS Letters ◽  
1986 ◽  
Vol 200 (2) ◽  
pp. 355-360 ◽  
Author(s):  
R.A. Cross ◽  
J. Vandekerckhove
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Muscle Myosin ◽  
Myosin Rod
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