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Smooth Muscle Myosin Cross-bridge Interactions Modulate Actin Filament Sliding Velocity In Vitro

D. Warshaw, J. Desrosiers, S. Work, K. Trybus
Published 1990 · Biology, Medicine

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Although it is generally believed that phosphorylation of the regulatory light chain of myosin is required before smooth muscle can develop force, it is not known if the overall degree of phosphorylation can also modulate the rate at which cross-bridges cycle. To address this question, an in vitro motility assay was used to observe the motion of single actin filaments interacting with smooth muscle myosin copolymers composed of varying ratios of phosphorylated and unphosphorylated myosin. The results suggest that unphosphorylated myosin acts as a load to slow down the rate at which actin is moved by the faster cycling phosphorylated cross-bridges. Myosin that was chemically modified to generate a noncycling analogue of the "weakly" bound conformation was similarly able to slow down phosphorylated myosin. The observed modulation of actin velocity as a function of copolymer composition can be accounted for by a model based on mechanical interactions between cross-bridges.
This paper references
Detection of surface movements in smooth muscle cells: Digital video microscopy
S. S. Work (1988)
10.1021/BI00745A026
Characterization of modified myosin at low ionic strength. Enzymatic and spin-label studies.
D. B. Stone (1973)
The contractile mechanism in smooth muscle
F. S. Fay (1981)
10.1038/303031A0
Movement of myosin-coated fluorescent beads on actin cables in vitro
M. Sheetz (1983)
10.1021/BI00668A038
Mechanism of inhibition of relaxation by N-ethylmaleimide treatment of myosin.
S. Pemrick (1976)
10.1016/0076-6879(82)85020-9
[18] Purification of muscle actin
J. D. Pardee (1982)
Mechanism of the phosphorylation-dependent regulation of smooth muscle heavy meromyosin.
J. Sellers (1985)
10.1016/0076-6879(82)85057-X
Special instrumentation and techniques for kinetic studies of contractile systems.
H. White (1982)
10.1016/0010-4825(88)90056-X
Detection of surface movements on single smooth muscle cells: digital video microscopy.
S. Work (1988)
10.1073/PNAS.83.17.6272
Fluorescent actin filaments move on myosin fixed to a glass surface.
S. Kron (1986)
10.1073/PNAS.80.16.4909
Crosslinked myosin subfragment 1: a stable analogue of the subfragment-1.ATP complex.
J. Chalovich (1983)
10.1016/B978-0-12-195220-4.50006-4
1 – Vascular Smooth Muscle: Relations between Energy Metabolism and Mechanics
P. Hellstrand (1982)
Effects of Lowering Temperature and Extracellular Calcium
Mined Yamakawa (1990)
10.1113/jphysiol.1979.sp012804
The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres.
K. A. Edman (1979)
10.1016/S0091-679X(08)60661-5
Chapter 18 Purification of Muscle Actin
J. D. Pardee (1982)
10.1152/AJPCELL.1986.251.6.C945
Slowing of cross-bridge cycling in smooth muscle without evidence of an internal load.
T. Butler (1986)
10.1126/SCIENCE.6893872
Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle.
P. F. Dillon (1981)
10.1038/328536A0
Myosin subfragment-1 is sufficient to move actin filaments in vitro
Y. Toyoshima (1987)
Preparation of myosin and its subfragments from rabbit skeletal muscle.
S. Margossian (1982)
10.1021/BI00272A002
Binding of gizzard smooth muscle myosin subfragment 1 to actin in the presence and absence of adenosine 5'-triphosphate.
L. Greene (1983)
10.1152/AJPCELL.1988.255.1.C86
Regulation of shortening velocity by cross-bridge phosphorylation in smooth muscle.
C. Hai (1988)
10.1042/BJ1190031
An electrophoretic study of the low-molecular-weight components of myosin.
W. Perrie (1970)
10.1161/01.RES.45.5.661
Cellular Thin Filament Protein Contents and Force Generation in Porcine Arteries andVeins
D. M. Cohen (1979)
10.1083/JCB.109.6.2887
Filamentous smooth muscle myosin is regulated by phosphorylation
K. Trybus (1989)
10.1152/AJPCELL.1988.254.5.C605
Functional significance of myosin transitions in single fibers of developing soleus muscle.
P. Reiser (1988)
10.1085/JGP.82.2.157
Cross-bridge elasticity in single smooth muscle cells
D. Warshaw (1983)
10.1085/JGP.91.2.165
Cross-bridge kinetics, cooperativity, and negatively strained cross- bridges in vertebrate smooth muscle. A laser-flash photolysis study
A. Somlyo (1988)
Cross-bridge Interactions Modulate Actin Velocity
Warshaw
10.1146/ANNUREV.PA.25.040185.003113
The function of myosin and myosin light chain kinase phosphorylation in smooth muscle.
K. Kamm (1985)
10.1016/0306-3623(86)90238-7
Energetic aspects of muscle contraction.
R. Woledge (1985)
A microcolorimetric method for the deterruination of inorganic phosphorous
H. H. Taussky (1953)
10.1085/JGP.89.5.771
Force: velocity relationship in single isolated toad stomach smooth muscle cells
D. Warshaw (1987)
10.1083/JCB.101.5.1897
Light chain phosphorylation regulates the movement of smooth muscle myosin on actin filaments
J. Sellers (1985)
10.1146/ANNUREV.PH.47.030185.003213
High-energy phosphate metabolism in vascular smooth muscle.
T. Butler (1985)
10.1016/s0021-9258(18)66180-0
A microcolorimetric method for the determination of inorganic phosphorus.
H. Taussky (1953)
10.1016/S0006-3495(80)85126-5
Cross-bridge model of muscle contraction. Quantitative analysis.
Evan Eisenberg (1980)
Crosslinked myosin subfragmcnt-l: A stable analogue of the subfragment-I • ATP complex
J. M. Chaiovich (1983)
10.1038/326805A0
Sliding movement of single actin filaments on one-headed myosin filaments
Y. Harada (1987)
10.1038/334074A0
Force measurements by micromanipulation of a single actin filament by glass needles
A. Kishino (1988)
10.1085/JGP.76.5.609
Chemical energetics of force development, force maintenance, and relaxation in mammalian smooth muscle
M. Siegman (1980)
10.1016/s0021-9258(18)43018-9
Reversible phosphorylation of smooth muscle myosin, heavy meromyosin, and platelet myosin.
J. Sellers (1981)
10.1016/s0021-9258(19)57507-x
Vascular smooth muscle caldesmon.
T. Clark (1986)
10.1016/0076-6879(91)96035-P
Assays for actin sliding movement over myosin-coated surfaces.
S. Kron (1991)
10.1073/PNAS.79.23.7288
Evidence for cross-bridge attachment in relaxed muscle at low ionic strength.
B. Brenner (1982)
Purification of muscle actin.
J. D. Pardee (1982)
Crosslinked myosin subfragmcnt-l: A stable analogue of the subfragment-I @BULLET ATP complex
J M Chaiovich (1983)
10.1083/JCB.109.6.2879
Monoclonal antibodies detect and stabilize conformational states of smooth muscle myosin
K. Trybus (1989)
10.1101/SQB.1973.037.01.021
Actin Activation of Heavy Meromyosin and Subfragment-1 ATPases; Steady State Kinetics Studies
C. Moos (1973)
10.1152/AJPLEGACY.1976.231.5.1509
Rigor and resistance to stretch in vertebrate smooth muscle.
T. Butler (1976)
10.1016/s0021-9258(17)39767-3
Conformational states of smooth muscle myosin. Effects of light chain phosphorylation and ionic strength.
K. Trybus (1984)



This paper is referenced by
10.1016/S0091-679X(08)60167-3
Assay of microtubule movement driven by single kinesin molecules.
J. Howard (1993)
10.1016/S0091-679X(08)60159-4
Myosin-specific adaptations of the motility assay.
J. Sellers (1993)
10.1165/rcmb.2015-0180OC
Peripheral Airway Smooth Muscle, but Not the Trachealis, Is Hypercontractile in an Equine Model of Asthma.
O. Matusovsky (2016)
10.1016/B978-0-12-656970-4.50050-6
Contractility of Muscles
R. Paul (1995)
10.1083/jcb.200304023
A mutant heterodimeric myosin with one inactive head generates maximal displacement
N. Kad (2003)
10.1016/S0006-3495(97)78753-8
Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap.
W. Guilford (1997)
10.1002/CM.970220407
Actin-binding proteins regulate the work performed by myosin II motors on single actin filaments.
L. Janson (1992)
10.1161/01.RES.86.7.737
Single-molecule mechanics of R403Q cardiac myosin isolated from the mouse model of familial hypertrophic cardiomyopathy.
M. Tyska (2000)
10.1023/A:1014572003361
Cross-bridge cooperativity during isometric contraction and unloaded shortening of skeletal muscle
V. Barnett (2004)
10.1091/MBC.7.7.1123
Structure-function studies of the myosin motor domain: importance of the 50-kDa cleft.
K. Ruppel (1996)
10.1007/978-1-4684-6003-2_34
Regulation of the step-distance in shortening muscles.
A. Oplatka (1991)
10.1113/jphysiol.2011.222984
An integrated in vitro and in situ study of kinetics of myosin II from frog skeletal muscle
R. Elangovan (2012)
10.1016/S0022-2836(02)01469-9
Some motile properties of fast characean myosin.
J. Awata (2003)
10.1101/2020.01.21.913558
Single molecule analysis reveals the role of regulatory light chains in fine-tuning skeletal myosin-II function
Arnab Nayak (2020)
10.1161/01.RES.77.2.439
Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro.
P. Vanburen (1995)
, isoform expression in human tissues ( + ) Insert smooth muscle myosin heavy chain ( SMB )
R. Léguillette (2005)
10.1016/j.bpj.2013.07.054
The kinetics of mechanically coupled myosins exhibit group size-dependent regimes.
L. Hilbert (2013)
10.14288/1.0166427
Modeling biomechanical responses of cells to external forces
Tenghu Wu (2015)
10.1016/0955-0674(91)90171-T
Regulation of cytoplasmic and smooth muscle myosin.
J. Sellers (1991)
10.1007/s002490050147
Acting on actin: the electric motility assay
D. Riveline (1998)
10.1016/j.bbrc.2013.07.109
Competitive displacement of cofilin can promote actin filament severing.
W. A. Elam (2013)
10.1007/BF01874156
Limits to shortening in smooth muscle tissues
R. Meiss (2005)
10.1016/S0006-3495(02)75560-4
The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin molecules.
J. Baker (2002)
10.1016/j.cub.2020.06.041
Periodic Oscillations of Myosin-II Mechanically Proofread Cell-Cell Connections to Ensure Robust Formation of the Cardiac Vessel
S. Zhang (2020)
10.1073/pnas.0711531105
Myosin V and Kinesin act as tethers to enhance each others' processivity
M. Y. Ali (2008)
10.1101/2020.05.27.119065
Imaging ATP Consumption in Resting Skeletal Muscle: One Molecule at a Time
Shane R. Nelson (2020)
10.1016/j.bbagen.2014.07.024
The role of caldesmon and its phosphorylation by ERK on the binding force of unphosphorylated myosin to actin.
Horia N. Roman (2014)
10.1016/B978-0-12-381510-1.00083-1
Chapter 83 – Smooth Muscle Myocyte Ultrastructure and Contractility
A. Somlyo (2012)
10.1073/pnas.1413397111
Site-specific cation release drives actin filament severing by vertebrate cofilin
Hyeran Kang (2014)
10.1111/J.1432-1033.1995.123_1.X
The effect of cross-linking of the two heads of porcine aorta smooth muscle myosin on its conformation and enzymic activity.
T. Katoh (1995)
10.1007/BF00123828
Smooth, cardiac and skeletal muscle myosin force and motion generation assessed by cross-bridge mechanical interactions in vitro
D. Harris (2004)
10.1023/B:JURE.0000021394.48560.71
Does the myosin V neck region act as a lever?
J. Moore (2004)
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