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Structures of kinesin and kinesin–microtubule interactions
Current Opinion in Cell Biology, 1999Several X-ray crystal structures of kinesin motor domains have recently been solved at high resolution ( approximately 0.2-0.3 nm), in both their monomeric and dimeric states. They show the folding of the polypeptide chain and different arrangements of subunits in the dimer.
Mandelkow, Eckhard, Hoenger, Andreas
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Current Opinion in Cell Biology, 2006
Kinesin-1 is a single-molecule walking machine, driven by ATP turnover. Recent optical trapping experiments show that pulling backwards on a walking kinesin-1 molecule causes the mechanical walking action to reverse, while the coupled chemical cycle of ATP turnover continues, apparently, to run forwards -- kinesin can moonwalk.
Nicholas J, Carter, Robert A, Cross
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Kinesin-1 is a single-molecule walking machine, driven by ATP turnover. Recent optical trapping experiments show that pulling backwards on a walking kinesin-1 molecule causes the mechanical walking action to reverse, while the coupled chemical cycle of ATP turnover continues, apparently, to run forwards -- kinesin can moonwalk.
Nicholas J, Carter, Robert A, Cross
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Biochemical Society Transactions, 2012
Kinesin-1 is a walking machine that takes ~8 nm steps along microtubules. Some aspects of the molecular mechanism of walking are now clear, but many are not. In the present paper, we discuss currently controversial points, focusing on the pathways by which kinesin takes occasional backsteps.
Nicholas J, Carter, Robert A, Cross
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Kinesin-1 is a walking machine that takes ~8 nm steps along microtubules. Some aspects of the molecular mechanism of walking are now clear, but many are not. In the present paper, we discuss currently controversial points, focusing on the pathways by which kinesin takes occasional backsteps.
Nicholas J, Carter, Robert A, Cross
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Kinesin-II, the heteromeric kinesin
Cellular and Molecular Life Sciences (CMLS), 1999The kinesins constitute a large family of motor proteins which are responsible for the distribution of numerous organelles, vesicles and macromolecular complexes throughout the cell. One class of these molecular motors, kinesin-II, is unique in that these proteins are typically found as heterotrimeric complexes containing two different, though related,
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Structure of a kinesin–tubulin complex and implications for kinesin motility
Nature Structural & Molecular Biology, 2013The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtubule-attached motile kinesins leads to cargo displacement. To better understand the nature of the conformational changes that lead to the power stroke that moves a kinesin's load along a microtubule, we determined the X-ray structure of human kinesin-1 ...
Gigant, Benoît +7 more
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Roles of mitotic kinesins, kinesin-5 and kinesin-6, in regulating neuronal migation
2022Mammalian brain development depends on migration of newborn neurons from their sites of origin to new locales. Migration of the neuron involves the extension of a leading process followed by somal translocation. According to the existing literature, cytoplasmic dynein and myosin-II, a microtubule-based motor and an actin-based motor, respectively ...
Aditi Falnikar +2 more
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Trends in Biochemical Sciences, 2001
Conventional kinesin has long been known to be a molecular motor that transports vesicular cargo, but only recently have we begun to understand how it functions in cells. Regulation of kinesin involves self-inhibition in which a head-to-tail interaction prevents microtubule binding.
K J, Verhey, T A, Rapoport
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Conventional kinesin has long been known to be a molecular motor that transports vesicular cargo, but only recently have we begun to understand how it functions in cells. Regulation of kinesin involves self-inhibition in which a head-to-tail interaction prevents microtubule binding.
K J, Verhey, T A, Rapoport
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Biochemistry, 2007
Several lines of experimental evidence suggest that the conventional kinesin 1 walks by an asymmetric hand-over-hand mechanism, although it is a homodimer. In the previous study, we examined several important force-dependent features of the hand-over-hand mechanism of kinesin. In this study, we focus on the asymmetry in the hand-over-hand mechanism. We
Qiang, Shao, Yi Qin, Gao
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Several lines of experimental evidence suggest that the conventional kinesin 1 walks by an asymmetric hand-over-hand mechanism, although it is a homodimer. In the previous study, we examined several important force-dependent features of the hand-over-hand mechanism of kinesin. In this study, we focus on the asymmetry in the hand-over-hand mechanism. We
Qiang, Shao, Yi Qin, Gao
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Trends in Cell Biology, 2002
Kinesins are motor proteins that move cargoes such as vesicles, organelles and chromosomes along microtubules. They are best known for their role in axonal transport and in mitosis. There is a diverse family of kinesins, members of which differ in composition and functions.
Mandelkow, Eckhard, Mandelkow, Eva-Maria
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Kinesins are motor proteins that move cargoes such as vesicles, organelles and chromosomes along microtubules. They are best known for their role in axonal transport and in mitosis. There is a diverse family of kinesins, members of which differ in composition and functions.
Mandelkow, Eckhard, Mandelkow, Eva-Maria
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The Mechanochemistry of Kinesin
Molecular and Chemical Neuropathology, 1990The mechanochemical protein kinesin is believed to play an important role in intracellular vesicle movements, including the anterograde motion of axoplasmic transport. This article reviews some of the pharmacological and biochemical information about kinesin, particularly with respect to the properties of nucleotide-dependent microtubule binding ...
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