TY - JOUR
T1 - A Unified Walking Model for Dimeric Motor Proteins
AU - Sasaki, Kazuo
AU - Kaya, Motoshi
AU - Higuchi, Hideo
N1 - Funding Information:
This study was supported by Grant-in-Aid for Scientific Research on Innovative Areas (H.H.; 23107002 ), Grant-in-Aid for Scientific Research (A) (H.H.; 23247022 ), Grant-in-Aid for Scientific Research (B) (K.S. and H.H.; 16H04773 ), Grant-in-Aid and for Scientific Research (C) (K.S.; 17K05562 ).
Publisher Copyright:
© 2018 Biophysical Society
PY - 2018/11/20
Y1 - 2018/11/20
N2 - Dimeric motor proteins, kinesin-1, cytoplasmic dynein-1, and myosin-V, move stepwise along microtubules and actin filaments with a regular step size. The motors take backward as well as forward steps. The step ratio r and dwell time τ which are the ratio of the number of backward steps to the number of forward steps and the time between consecutive steps, respectively, were observed to change with the load. To understand the movement of motor proteins, we constructed a unified and simple mathematical model to explain the load dependencies of r and of τ measured for the above three types of motors quantitatively. Our model consists of three states, and the forward and backward steps are represented by the cycles of transitions visiting different pairs of states among the three, implying that a backward step is not the reversal of a forward step. Each of r and τ is given by a simple expression containing two exponential functions. The experimental data for r and τ for dynein available in the literature are not sufficient for a quantitative analysis, which is in contrast to those for kinesin and myosin-V. We reanalyze the data to obtain r and τ of native dynein to make up the insufficient data to fit them to the model. Our model successfully describes the behavior of r and τ for all of the motors in a wide range of loads from large assisting loads to superstall loads.
AB - Dimeric motor proteins, kinesin-1, cytoplasmic dynein-1, and myosin-V, move stepwise along microtubules and actin filaments with a regular step size. The motors take backward as well as forward steps. The step ratio r and dwell time τ which are the ratio of the number of backward steps to the number of forward steps and the time between consecutive steps, respectively, were observed to change with the load. To understand the movement of motor proteins, we constructed a unified and simple mathematical model to explain the load dependencies of r and of τ measured for the above three types of motors quantitatively. Our model consists of three states, and the forward and backward steps are represented by the cycles of transitions visiting different pairs of states among the three, implying that a backward step is not the reversal of a forward step. Each of r and τ is given by a simple expression containing two exponential functions. The experimental data for r and τ for dynein available in the literature are not sufficient for a quantitative analysis, which is in contrast to those for kinesin and myosin-V. We reanalyze the data to obtain r and τ of native dynein to make up the insufficient data to fit them to the model. Our model successfully describes the behavior of r and τ for all of the motors in a wide range of loads from large assisting loads to superstall loads.
UR - http://www.scopus.com/inward/record.url?scp=85055913351&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85055913351&partnerID=8YFLogxK
U2 - 10.1016/j.bpj.2018.09.032
DO - 10.1016/j.bpj.2018.09.032
M3 - Article
C2 - 30396511
AN - SCOPUS:85055913351
SN - 0006-3495
VL - 115
SP - 1981
EP - 1992
JO - Biophysical Journal
JF - Biophysical Journal
IS - 10
ER -