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Journal articles on the topic 'Molecular motors'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 March 2023

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1

Kassem, Salma, Thomas van Leeuwen, Anouk S. Lubbe, Miriam R. Wilson, Ben L. Feringa, and David A. Leigh. "Artificial molecular motors." Chemical Society Reviews 46, no. 9 (2017): 2592–621. http://dx.doi.org/10.1039/c7cs00245a.

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Artificial molecular motors take inspiration from motor proteins, nature's solution for achieving directional molecular level motion. An overview is given of the principal designs of artificial molecular motors and their modes of operation. We identify some key challenges remaining in the field.

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2

Schliwa, Manfred, and Günther Woehlke. "Molecular motors." Nature 422, no. 6933 (April 2003): 759–65. http://dx.doi.org/10.1038/nature01601.

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3

Trybus, Kathleen M., and Vladimir I. Gelfand. "Molecular motors." Molecular Biology of the Cell 24, no. 6 (March 15, 2013): 672. http://dx.doi.org/10.1091/mbc.e12-12-0873.

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4

Cross, R. A., and N. J. Carter. "Molecular motors." Current Biology 10, no. 5 (March 2000): R177—R179. http://dx.doi.org/10.1016/s0960-9822(00)00368-7.

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5

KLUMPP, STEFAN, MELANIE J. I. MÜLLER, and REINHARD LIPOWSKY. "COOPERATIVE TRANSPORT BY SMALL TEAMS OF MOLECULAR MOTORS." Biophysical Reviews and Letters 01, no. 04 (October 2006): 353–61. http://dx.doi.org/10.1142/s1793048006000288.

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Molecular motors power directed transport of cargoes within cells. Even if a single motor is sufficient to transport a cargo, motors often cooperate in small teams. We discuss the cooperative cargo transport by several motors theoretically and explore some of its properties. In particular we emphasize how motor teams can drag cargoes through a viscous environment.

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6

NI, CHEN, and JUN-ZHONG WANG. "STM STUDIES ON MOLECULAR ROTORS AND MOTORS." Surface Review and Letters 25, Supp01 (December 2018): 1841004. http://dx.doi.org/10.1142/s0218625x18410044.

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Molecular motor is a nanoscale machine that consumes energy to produce work via the unidirectional and controlled movement. They are universal in nature and essential to numerous processes of life. When mounted onto solid surfaces, scanning tunneling microscopy (STM) is a powerful technique to characterize the molecular rotors and motors due to the atomic-scale resolution coupled with its ability to track the motion of molecular rotor and motor over time. Moreover, the molecular rotors and motors can be powered by STM tip through injecting tunneling electrons. This review addresses recent advances in the STM studies of the structure, motion, and manipulation of molecular rotors and motors. The developments of surface-mounted azimuthal and altitudinal rotor and motors, large-scale array of molecular rotors, as well as the molecular motors with translational motion will be addressed.

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7

Berger, Florian, Corina Keller, Melanie J. I. Müller, Stefan Klumpp, and Reinhard Lipowsky. "Co-operative transport by molecular motors." Biochemical Society Transactions 39, no. 5 (September 21, 2011): 1211–15. http://dx.doi.org/10.1042/bst0391211.

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Intracellular transport is often driven co-operatively by several molecular motors, which may belong to one or several motor species. Understanding how these motors interact and what co-ordinates and regulates their movements is a central problem in studies of intracellular transport. A general theoretical framework for the analysis of such transport processes is described, which enables us to explain the behaviour of intracellular cargos by the transport properties of individual motors and their interactions. We review recent advances in the theoretical description of motor co-operativity and discuss related experimental results.

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8

Lin, Tsai-Shun, and Chien-Jung Lo. "2P154 Investigating stators assembly of flagellar motors in Escherichia coli(11. Molecular motor,Poster)." Seibutsu Butsuri 53, supplement1-2 (2013): S184. http://dx.doi.org/10.2142/biophys.53.s184_4.

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9

Spector, Alexander A. "Effectiveness, Active Energy Produced by Molecular Motors, and Nonlinear Capacitance of the Cochlear Outer Hair Cell." Journal of Biomechanical Engineering 127, no. 3 (January 5, 2005): 391–99. http://dx.doi.org/10.1115/1.1894233.

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Cochlear outer hair cells are crucial for active hearing. These cells have a unique form of motility, named electromotility, whose main features are the cell’s length changes, active force production, and nonlinear capacitance. The molecular motor, prestin, that drives outer hair cell electromotility has recently been identified. We reveal relationships between the active energy produced by the outer hair cell molecular motors, motor effectiveness, and the capacitive properties of the cell membrane. We quantitatively characterize these relationships by introducing three characteristics: effective capacitance, zero-strain capacitance, and zero-resultant capacitance. We show that zero-strain capacitance is smaller than zero-resultant capacitance, and that the effective capacitance is between the two. It was also found that the differences between the introduced capacitive characteristics can be expressed in terms of the active energy produced by the cell’s molecular motors. The effectiveness of the cell and its molecular motors is introduced as the ratio of the motors’ active energy to the energy of the externally applied electric field. It is shown that the effectiveness is proportional to the difference between zero-strain and zero-resultant capacitance. We analyze the cell and motor’s effectiveness within a broad range of cellular parameters and estimate it to be within a range of 12%–30%.

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10

Pooler, Daisy R. S., Anouk S. Lubbe, Stefano Crespi, and Ben L. Feringa. "Designing light-driven rotary molecular motors." Chemical Science 12, no. 45 (2021): 14964–86. http://dx.doi.org/10.1039/d1sc04781g.

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Various families of light-driven rotary molecular motors and the key aspects of motor design are discussed. Comparisons are made between the strengths and weaknesses of each motor. Challenges, applications, and future prospects are explored.

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11

Endow, S. A. "Molecular motors--a paradigm for mutant analysis." Journal of Cell Science 113, no. 8 (April 15, 2000): 1311–18. http://dx.doi.org/10.1242/jcs.113.8.1311.

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Molecular motors perform essential functions in the cell and have the potential to provide insights into the basis of many important processes. A unique property of molecular motors is their ability to convert energy from ATP hydrolysis into work, enabling the motors to bind to and move along cytoskeletal filaments. The mechanism of energy conversion by molecular motors is not yet understood and may lead to the discovery of new biophysical principles. Mutant analysis could provide valuable information, but it is not obvious how to obtain mutants that are informative for study. The analysis presented here points out several strategies for obtaining mutants by selection from molecular or genetic screens, or by rational design. Mutants that are expected to provide important information about the motor mechanism include ATPase mutants, which interfere with the nucleotide hydrolysis cycle, and uncoupling mutants, which unlink basic motor activities and reveal their interdependence. Natural variants can also be exploited to provide unexpected information about motor function. This general approach to uncovering protein function by analysis of informative mutants is applicable not only to molecular motors, but to other proteins of interest.

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12

Kistemaker, Jos C. M., Anouk S. Lubbe, and Ben L. Feringa. "Exploring molecular motors." Materials Chemistry Frontiers 5, no. 7 (2021): 2900–2906. http://dx.doi.org/10.1039/d0qm01091j.

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The introduction of mechanical functions and controlled motion based on molecular motors and machines offers tremendous opportunities towards the design of dynamic molecular systems and responsive materials.

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13

Jülicher, Frank, Armand Ajdari, and Jacques Prost. "Modeling molecular motors." Reviews of Modern Physics 69, no. 4 (October 1, 1997): 1269–82. http://dx.doi.org/10.1103/revmodphys.69.1269.

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14

Molloy, J. E., and C. Veigel. "Editorial: Molecular motors." IEE Proceedings - Nanobiotechnology 150, no. 3 (2003): 93. http://dx.doi.org/10.1049/ip-nbt:20031216.

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15

Iino, Ryota, Kazushi Kinbara, and Zev Bryant. "Introduction: Molecular Motors." Chemical Reviews 120, no. 1 (January 8, 2020): 1–4. http://dx.doi.org/10.1021/acs.chemrev.9b00819.

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16

Davis, Anthony P. "Synthetic molecular motors." Nature 401, no. 6749 (September 1999): 120–21. http://dx.doi.org/10.1038/43576.

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17

Magnasco, Marcelo O. "Molecular combustion motors." Physical Review Letters 72, no. 16 (April 18, 1994): 2656–59. http://dx.doi.org/10.1103/physrevlett.72.2656.

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18

Jülicher, Frank, and Jacques Prost. "Cooperative Molecular Motors." Physical Review Letters 75, no. 13 (September 25, 1995): 2618–21. http://dx.doi.org/10.1103/physrevlett.75.2618.

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19

Soppina, Virupakshi, and Kristen J. Verhey. "The family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors." Molecular Biology of the Cell 25, no. 14 (July 15, 2014): 2161–70. http://dx.doi.org/10.1091/mbc.e14-01-0696.

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The kinesin-3 family (KIF) is one of the largest among the kinesin superfamily and an important driver of a variety of cellular transport events. Whereas all kinesins contain the highly conserved kinesin motor domain, different families have evolved unique motor features that enable different mechanical and functional outputs. A defining feature of kinesin-3 motors is the presence of a positively charged insert, the K-loop, in loop 12 of their motor domains. However, the mechanical and functional output of the K-loop with respect to processive motility of dimeric kinesin-3 motors is unknown. We find that, surprisingly, the K-loop plays no role in generating the superprocessive motion of dimeric kinesin-3 motors (KIF1, KIF13, and KIF16). Instead, we find that the K-loop provides kinesin-3 motors with a high microtubule affinity in the motor's ADP-bound state, a state that for other kinesins binds only weakly to the microtubule surface. A high microtubule affinity results in a high landing rate of processive kinesin-3 motors on the microtubule surface. We propose that the family-specific K-loop contributes to efficient kinesin-3 cargo transport by enhancing the initial interaction of dimeric motors with the microtubule track.

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20

Esaki, Seiji, Yoshiharu Ishii, and Toshio Yanagida. "1P273 Cooperativity causes plasticity in molecular motors(9. Molecular motor (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)." Seibutsu Butsuri 46, supplement2 (2006): S215. http://dx.doi.org/10.2142/biophys.46.s215_1.

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21

Bakewell, David J. G., and Dan V. Nicolau. "Protein Linear Molecular Motor-Powered Nanodevices." Australian Journal of Chemistry 60, no. 5 (2007): 314. http://dx.doi.org/10.1071/ch06456.

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Myosin–actin and kinesin–microtubule linear protein motor systems and their application in hybrid nanodevices are reviewed. Research during the past several decades has provided a wealth of understanding about the fundamentals of protein motors that continues to be pursued. It has also laid the foundations for a new branch of investigation that considers the application of these motors as key functional elements in laboratory-on-a-chip and other micro/nanodevices. Current models of myosin and kinesin motors are introduced and the effects of motility assay parameters, including temperature, toxicity, and in particular, surface effects on motor protein operation, are discussed. These parameters set the boundaries for gliding and bead motility assays. The review describes recent developments in assay motility confinement and unidirectional control, using micro- and nano-fabricated structures, surface patterning, microfluidic flow, electromagnetic fields, and self-assembled actin filament/microtubule tracks. Current protein motor assays are primitive devices, and the developments in governing control can lead to promising applications such as sensing, nano-mechanical drivers, and biocomputation.

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22

LIPOWSKY, REINHARD, JANINA BEEG, RUMIANA DIMOVA, STEFAN KLUMPP, STEFFEN LIEPELT, MELANIE J. I. MÜLLER, and ANGELO VALLERIANI. "ACTIVE BIO-SYSTEMS: FROM SINGLE MOTOR MOLECULES TO COOPERATIVE CARGO TRANSPORT." Biophysical Reviews and Letters 04, no. 01n02 (April 2009): 77–137. http://dx.doi.org/10.1142/s1793048009000946.

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Living cells contain a large number of molecular motors that convert the chemical energy released from nucleotide hydrolysis into mechanical work. This review focusses on stepping motors that move along cytoskeletal filaments. The behavior of these motors involves three distinct nonequilibrium processes that cover a wide range of length and time scales: (i) Directed stepping of single motors bound to a filament; (ii) Composite motor walks of single motors consisting of directed stepping interrupted by diffusive motion; and (iii) Cooperative transport by teams of several motors. On the molecular scale, the energy conversion of these motors leads to single steps along the filaments with a step size of about 10 nm. The corresponding chemomechanical coupling is governed by several distinct motor cycles, which represent the dominant pathways for different values of nucleotide concentrations and load force. For the kinesin motor, the competition of two such cycles determines the stall force, at which the motor velocity vanishes and the motor reverses the direction of its motion. Because of thermal noise, the stepping motors unbind from the filaments after a certain run time and run length. For kinesin, the run time is about 1 s and the run length is about 1 μm for high ATP concentration and low load force. On length scales that are large compared to the run length, a single motor undergoes composite walks consisting of directed stepping interrupted by diffusive motion. The relative importance of bound and unbound motor states depends on the binding and unbinding rates of the motors. The effective transport velocity and diffusion coefficient of the motors are determined by the geometry of the compartments, in which the motors move. The effective diffusion coefficient can be enhanced by several orders of magnitude if the motors undergo active diffusion by interacting with certain filament patterns. In vivo, stepping motors are responsible for the transport of vesicles and other types of intracellular cargo particles that shuttle between the different cell compartments. This cargo transport is usually performed by teams of motors. If all motors belong to the same molecular species, the cooperative action of the motors leads to uni-directional transport with a strongly increased run length and to a characteristic force dependence of the velocity distributions. If two antagonistic species of motors pull on the cargo, they perform a stochastic tug-of-war, which is characterized by a subtle force balance between the two motor teams and leads to seven distinct patterns of uni- and bi-directional transport. So far, all experimental observations on bi-directional transport are consistent with such a tug-of-war. Finally, the traffic of interacting motors is also briefly discussed. Depending on their mutual interactions and the compartment geometry, the motors form various spatio-temporal patterns such as traffic jams, and undergo nonequilibrium phase transitions between such transport patterns.

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23

Feng, Yuanning, Marco Ovalle, James S. W. Seale, Christopher K. Lee, Dong Jun Kim, R. Dean Astumian, and J. Fraser Stoddart. "Molecular Pumps and Motors." Journal of the American Chemical Society 143, no. 15 (April 8, 2021): 5569–91. http://dx.doi.org/10.1021/jacs.0c13388.

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24

Yildiz, Ahmet. "How Molecular Motors Move." Science 311, no. 5762 (February 10, 2006): 792–93. http://dx.doi.org/10.1126/science.1125068a.

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25

LESLIE, R. J. "Molecular Motors: Cell Movement." Science 244, no. 4912 (June 30, 1989): 1599. http://dx.doi.org/10.1126/science.244.4912.1599.

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26

Schliwa, Manfred. "Molecular motors join forces." Nature 397, no. 6716 (January 1999): 204–5. http://dx.doi.org/10.1038/16577.

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27

Tyreman, M. J. A., and J. E. Molloy. "Molecular motors: nature's nanomachines." IEE Proceedings - Nanobiotechnology 150, no. 3 (2003): 95. http://dx.doi.org/10.1049/ip-nbt:20031172.

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28

Michaelis, Jens, Adam Muschielok, Joanna Andrecka, Wolfgang Kügel, and Jeffrey R. Moffitt. "DNA based molecular motors." Physics of Life Reviews 6, no. 4 (December 2009): 250–66. http://dx.doi.org/10.1016/j.plrev.2009.09.001.

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29

Cross, R. A. "Molecular Motors: Dynein's Gearbox." Current Biology 14, no. 9 (May 2004): R355—R356. http://dx.doi.org/10.1016/j.cub.2004.04.026.

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30

Santamaria-Holek, Ivan, and Jared López Alamilla. "Determining Molecular Motors Processivity." Biophysical Journal 102, no. 3 (January 2012): 367a. http://dx.doi.org/10.1016/j.bpj.2011.11.2004.

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31

Meech, Robert, and Matthew Holley. "Ion-age molecular motors." Nature Neuroscience 4, no. 8 (August 2001): 771–73. http://dx.doi.org/10.1038/90461.

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32

Spudich, James A. "How molecular motors work." Nature 372, no. 6506 (December 1994): 515–18. http://dx.doi.org/10.1038/372515a0.

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33

Marrucci, L., D. Paparo, and M. Kreuzer. "Fluctuating-friction molecular motors." Journal of Physics: Condensed Matter 13, no. 46 (November 5, 2001): 10371–82. http://dx.doi.org/10.1088/0953-8984/13/46/309.

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34

Vilfan, A., E. Frey, and F. Schwabl. "Elastically coupled molecular motors." European Physical Journal B 3, no. 4 (July 1998): 535–46. http://dx.doi.org/10.1007/s100510050343.

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35

Gyoeva, F. K. "Interaction of Molecular Motors." Molecular Biology 39, no. 4 (July 2005): 614–22. http://dx.doi.org/10.1007/s11008-005-0077-x.

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36

Schalley, Christoph A., and Fritz Vögtle. "International Workshop „Molecular Motors”︁." Nachrichten aus der Chemie 50, no. 2 (February 2002): 201. http://dx.doi.org/10.1002/nadc.20020500232.

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37

Brady, S. T. "Molecular motors and fast axonal transport." Proceedings, annual meeting, Electron Microscopy Society of America 52 (1994): 22–23. http://dx.doi.org/10.1017/s0424820100167846.

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When video microscopy was first used to study fast axonal transport in isolated axoplasm from squid giant axons, a torrent of membrane traffic was seen to move in both directions. Images of membrane bounded organelles (MBOs) moving along individual microtubules (MTs) in axoplasm opened the way for characterization of the microscopic properties of fast axonal transport and led to the characterization of two molecular motors involved in fast axonal transport. The pharmacology of MBO movement ruled out previously identified molecular motors and a biochemical dissection of fast axonal transport in axoplasm demonstrated the existence of a new class of molecular motors. Subsequently, the polypeptides comprising a new class of molecular motor, kinesin, were discovered initiating a new era in the study of molecular motors and intracellular motility.The effects of ATP analogues on fast axonal transport led to dicovery of kinesin. When the nonhydrolyzable ATP analogue, adenylyl 5′-imidodiphosphate (AMP-PNP), was perfused into isolated axoplasm, all MBOs moving in both anterograde and retrograde directions stopped moving and remained attached to MTs. Unlike the effects of AMP-PNP on myosin and dynein, inhibition by AMP-PNP was rapid even in the presence of equimolar ATP, but was reversed by excess ATP.

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38

Abe, Yuta, Takeshi Itabashi, Yuta Shimamoto, Tarun M. Capoor, and Shin'ichi Ishiwata. "3P152 Behavior of molecular motors in cytoplasmic extracts(Molecular motors,Oral Presentations)." Seibutsu Butsuri 47, supplement (2007): S241. http://dx.doi.org/10.2142/biophys.47.s241_1.

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39

Feizabadi, Mitra Shojania, Ramiz S. Alejilat, Alexis B. Duffy, Jane C. Breslin, and Ibukunoluwa I. Akintola. "A Confirmation for the Positive Electric Charge of Bio-Molecular Motors through Utilizing a Novel Nano-Technology Approach In Vitro." International Journal of Molecular Sciences 21, no. 14 (July 13, 2020): 4935. http://dx.doi.org/10.3390/ijms21144935.

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Molecular motors are microtubule-based proteins which contribute to many cell functions, such as intracellular transportation and cell division. The details of the nature of the mutual interactions between motors and microtubules still needs to be extensively explored. However, electrostatic interaction is known as one of the key factors making motor-microtubule association possible. The association rate of molecular motors to microtubules is a way to observe and evaluate the charge of the bio-motors in vivo. Growing evidence indicates that microtubules with distinct structural compositions in terms of beta tubulin isotypes carry different charges. Therefore, the electrostatic-driven association rate of motors–microtubules, which is a base for identifying the charge of motors, can be more likely influenced. Here, we present a novel method to experimentally confirm the charge of molecular motors in vitro. The offered nanotechnology-based approach can validate the charge of motors in the absence of any cellular components through the observation and analysis of the changes that biomolecular motors can cause on the dynamic of charged microspheres inside a uniform electric field produced by a microscope slide-based nanocapacitor. This new in vitro experimental method is significant as it minimizes the intracellular factors that may interfere the electric charge that molecular motors carry.

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40

Zhang, Long, Yunyan Qiu, Wei-Guang Liu, Hongliang Chen, Dengke Shen, Bo Song, Kang Cai, et al. "An electric molecular motor." Nature 613, no. 7943 (January 11, 2023): 280–86. http://dx.doi.org/10.1038/s41586-022-05421-6.

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AbstractMacroscopic electric motors continue to have a large impact on almost every aspect of modern society. Consequently, the effort towards developing molecular motors1–3 that can be driven by electricity could not be more timely. Here we describe an electric molecular motor based on a [3]catenane4,5, in which two cyclobis(paraquat-p-phenylene)6 (CBPQT4+) rings are powered by electricity in solution to circumrotate unidirectionally around a 50-membered loop. The constitution of the loop ensures that both rings undergo highly (85%) unidirectional movement under the guidance of a flashing energy ratchet7,8, whereas the interactions between the two rings give rise to a two-dimensional potential energy surface (PES) similar to that shown by FOF1 ATP synthase9. The unidirectionality is powered by an oscillating10 voltage11,12 or external modulation of the redox potential13. Initially, we focused our attention on the homologous [2]catenane, only to find that the kinetic asymmetry was insufficient to support unidirectional movement of the sole ring. Accordingly, we incorporated a second CBPQT4+ ring to provide further symmetry breaking by interactions between the two mobile rings. This demonstration of electrically driven continual circumrotatory motion of two rings around a loop in a [3]catenane is free from the production of waste products and represents an important step towards surface-bound14 electric molecular motors.

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41

Feng, Mudong, and Michael K. Gilson. "Mechanistic analysis of light-driven overcrowded alkene-based molecular motors by multiscale molecular simulations." Physical Chemistry Chemical Physics 23, no. 14 (2021): 8525–40. http://dx.doi.org/10.1039/d0cp06685k.

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Ground-state and excited-state molecular dynamics simulations shed light on the rotation mechanism of small, light-driven molecular motors and predict motor performance. How fast can they rotate; how much torque and power can they generate?

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42

Toyabe, Shoiti, Takashi Sagawa, Masahito Ueda, Eiro Muneyuki, and Masaki Sano. "3P183 Information-heat engine as a model system of molecular motors(Molecular motor,The 48th Annual Meeting of the Biophysical Society of Japan)." Seibutsu Butsuri 50, supplement2 (2010): S177. http://dx.doi.org/10.2142/biophys.50.s177_2.

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43

Spudich, James A. "Molecular motors: forty years of interdisciplinary research." Molecular Biology of the Cell 22, no. 21 (November 2011): 3936–39. http://dx.doi.org/10.1091/mbc.e11-05-0447.

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A mere forty years ago it was unclear what motor molecules exist in cells that could be responsible for the variety of nonmuscle cell movements, including the “saltatory cytoplasmic particle movements” apparent by light microscopy. One wondered whether nonmuscle cells might have a myosin-like molecule, well known to investigators of muscle. Now we know that there are more than a hundred different molecular motors in eukaryotic cells that drive numerous biological processes and organize the cell's dynamic city plan. Furthermore, in vitro motility assays, taken to the single-molecule level using techniques of physics, have allowed detailed characterization of the processes by which motor molecules transduce the chemical energy of ATP hydrolysis into mechanical movement. Molecular motor research is now at an exciting threshold of being able to enter into the realm of clinical applications.

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44

Xie, Ping. "Molecular Mechanism of Processive Stepping of Kinesin Motors." Symmetry 13, no. 10 (September 27, 2021): 1799. http://dx.doi.org/10.3390/sym13101799.

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Kinesin-1 is a motor protein that can step processively on microtubule by hydrolyzing ATP molecules, playing an essential role in intracellular transports. To better understand the mechanochemical coupling of the motor stepping cycle, numerous structural, biochemical, single molecule, theoretical modeling and numerical simulation studies have been undertaken for the kinesin-1 motor. Recently, a novel ultraresolution optical trapping method was employed to study the mechanics of the kinesin-1 motor and new results were supplemented to its stepping dynamics. In this commentary, the new single molecule results are explained well theoretically with one of the models presented in the literature for the mechanochemical coupling of the kinesin-1 motor. With the model, various prior experimental results for dynamics of different families of N-terminal kinesin motors have also been explained quantitatively.

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45

KIERFELD, JAN, PAVEL KRAIKIVSKI, and REINHARD LIPOWSKY. "FILAMENT ORDERING AND CLUSTERING BY MOLECULAR MOTORS IN MOTILITY ASSAYS." Biophysical Reviews and Letters 01, no. 04 (October 2006): 363–74. http://dx.doi.org/10.1142/s1793048006000318.

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We study the cooperative behavior of cytoskeletal filaments in motility assays, in which immobilized motor proteins bind the filaments to a surface and actively pull them along this surface. Because of the repulsive interaction of filaments, the motor-driven dynamics of filaments leads to a nonequilibrium phase transition which generalizes the isotropicnematic phase transition of the corresponding equilibrium system, the hard-rod fluid. Langevin dynamics simulations and analytical theory show that the motor activity enhances the tendency for nematic ordering. At high detachment forces of motors, we observe the formation of filament clusters because of blocking effects; at low detachment forces, cluster formation can be controlled by the density of inactive motors.

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46

Norris, Stephen R., Virupakshi Soppina, Aslan S. Dizaji, Kristin I. Schimert, David Sept, Dawen Cai, Sivaraj Sivaramakrishnan, and Kristen J. Verhey. "A method for multiprotein assembly in cells reveals independent action of kinesins in complex." Journal of Cell Biology 207, no. 3 (November 3, 2014): 393–406. http://dx.doi.org/10.1083/jcb.201407086.

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Teams of processive molecular motors are critical for intracellular transport and organization, yet coordination between motors remains poorly understood. Here, we develop a system using protein components to generate assemblies of defined spacing and composition inside cells. This system is applicable to studying macromolecular complexes in the context of cell signaling, motility, and intracellular trafficking. We use the system to study the emergent behavior of kinesin motors in teams. We find that two kinesin motors in complex act independently (do not help or hinder each other) and can alternate their activities. For complexes containing a slow kinesin-1 and fast kinesin-3 motor, the slow motor dominates motility in vitro but the fast motor can dominate on certain subpopulations of microtubules in cells. Both motors showed dynamic interactions with the complex, suggesting that motor–cargo linkages are sensitive to forces applied by the motors. We conclude that kinesin motors in complex act independently in a manner regulated by the microtubule track.

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47

Ibusuki, Ryota, Tatsuya Morishita, Akane Furuta, Shintaro Nakayama, Maki Yoshio, Hiroaki Kojima, Kazuhiro Oiwa, and Ken’ya Furuta. "Programmable molecular transport achieved by engineering protein motors to move on DNA nanotubes." Science 375, no. 6585 (March 11, 2022): 1159–64. http://dx.doi.org/10.1126/science.abj5170.

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Intracellular transport is the basis of microscale logistics within cells and is powered by biomolecular motors. Mimicking transport for in vitro applications has been widely studied; however, the inflexibility in track design and control has hindered practical applications. Here, we developed protein-based motors that move on DNA nanotubes by combining a biomolecular motor dynein and DNA binding proteins. The new motors and DNA-based nanoarchitectures enabled us to arrange the binding sites on the track, locally control the direction of movement, and achieve multiplexed cargo transport by different motors. The integration of these technologies realized microscale cargo sorters and integrators that automatically transport molecules as programmed in DNA sequences on a branched DNA nanotube. Our system should provide a versatile, controllable platform for future applications.

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Tafoya, Sara, and Carlos Bustamante. "Molecular switch-like regulation in motor proteins." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1749 (May 7, 2018): 20170181. http://dx.doi.org/10.1098/rstb.2017.0181.

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Motor proteins are powered by nucleotide hydrolysis and exert mechanical work to carry out many fundamental biological tasks. To ensure their correct and efficient performance, the motors' activities are allosterically regulated by additional factors that enhance or suppress their NTPase activity. Here, we review two highly conserved mechanisms of ATP hydrolysis activation and repression operating in motor proteins—the glutamate switch and the arginine finger—and their associated regulatory factors. We examine the implications of these regulatory mechanisms in proteins that are formed by multiple ATPase subunits. We argue that the regulatory mechanisms employed by motor proteins display features similar to those described in small GTPases, which require external regulatory elements, such as dissociation inhibitors, exchange factors and activating proteins, to switch the protein's function ‘on’ and ‘off'. Likewise, similar regulatory roles are taken on by the motor's substrate, additional binding factors, and even adjacent subunits in multimeric complexes. However, in motor proteins, more than one regulatory factor and the two mechanisms described here often underlie the machine's operation. Furthermore, ATPase regulation takes place throughout the motor's cycle, which enables a more complex function than the binary ‘active' and ‘inactive' states. This article is part of a discussion meeting issue ‘Allostery and molecular machines'.

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Tayar, Alexandra M., Michael F. Hagan, and Zvonimir Dogic. "Active liquid crystals powered by force-sensing DNA-motor clusters." Proceedings of the National Academy of Sciences 118, no. 30 (July 20, 2021): e2102873118. http://dx.doi.org/10.1073/pnas.2102873118.

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Cytoskeletal active nematics exhibit striking nonequilibrium dynamics that are powered by energy-consuming molecular motors. To gain insight into the structure and mechanics of these materials, we design programmable clusters in which kinesin motors are linked by a double-stranded DNA linker. The efficiency by which DNA-based clusters power active nematics depends on both the stepping dynamics of the kinesin motors and the chemical structure of the polymeric linker. Fluorescence anisotropy measurements reveal that the motor clusters, like filamentous microtubules, exhibit local nematic order. The properties of the DNA linker enable the design of force-sensing clusters. When the load across the linker exceeds a critical threshold, the clusters fall apart, ceasing to generate active stresses and slowing the system dynamics. Fluorescence readout reveals the fraction of bound clusters that generate interfilament sliding. In turn, this yields the average load experienced by the kinesin motors as they step along the microtubules. DNA-motor clusters provide a foundation for understanding the molecular mechanism by which nanoscale molecular motors collectively generate mesoscopic active stresses, which in turn power macroscale nonequilibrium dynamics of active nematics.

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WANG, ZIQING, CAIHUA ZHANG, and GUODONG WANG. "MOLECULAR MOTORS CONTROL LENGTH OF ANTIPARALLEL MICROTUBULE OVERLAPS." Modern Physics Letters B 26, no. 04 (February 10, 2012): 1150027. http://dx.doi.org/10.1142/s0217984911500278.

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Using Monte Carlo simulation, we studied the controlling length of antiparallel microtubule overlaps by motors in the presence of PRC1. Two models for the inhibition mechanism of microtubule dynamics are developed. The comparison of the simulation results and the experimental data shows that the inhibition of microtubule dynamics is probably not due to a direct inhibition of polymerization and depolymerization of microtubule by the motor at plus end of microtubule but rather caused by global structural changes in the microtubule due to the presence of bound motor on the microtubule.

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