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Kinesin-1

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https://www.readbyqxmd.com/read/29337076/opposing-kinesin-and-myosin-i-motors-drive-membrane-deformation-and-tubulation-along-engineered-cytoskeletal-networks
#1
Betsy B McIntosh, Serapion Pyrpassopoulos, Erika L F Holzbaur, E Michael Ostap
Microtubule and actin filament molecular motors such as kinesin-1 and myosin-Ic (Myo1c) transport and remodel membrane-bound vesicles; however, it is unclear how they coordinate to accomplish these tasks. We introduced kinesin-1- and Myo1c-bound giant unilamellar vesicles (GUVs) into a micropatterned in vitro cytoskeletal matrix modeled after the subcellular architecture where vesicular sorting and membrane remodeling are observed. This array was composed of sparse microtubules intersecting regions dense with actin filaments, and revealed that Myo1c-dependent tethering of GUVs enabled kinesin-1-driven membrane deformation and tubulation...
January 9, 2018: Current Biology: CB
https://www.readbyqxmd.com/read/29329502/energetic-costs-precision-and-transport-efficiency-of-molecular-motors
#2
Wonseok Hwang, Changbong Hyeon
An efficient molecular motor would deliver cargos to the target site at a high speed and in a punctual manner while consuming a minimal amount of energy. According to a recently formulated thermodynamic principle, referred to as the thermodynamic uncertainty relation, the travel distance of a motor and its variance are, however, constrained by the free energy being consumed. Here we use the principle underlying the uncertainty relation to quantify the transport efficiency of molecular motors for varying ATP concentration ([ATP]) and applied load (f)...
January 12, 2018: Journal of Physical Chemistry Letters
https://www.readbyqxmd.com/read/29318877/reversibly-bound-kinesin-1-motor-proteins-propelling-microtubules-demonstrate-dynamic-recruitment-of-active-building-blocks
#3
Amy Tsui-Chi Lam, Stanislav Tsitkov, Yifei Zhang, Henry Hess
Biological materials and systems often dynamically self-assemble and disassemble, forming temporary structures as needed and allowing for dynamic responses to stimuli and changing environmental conditions. However, this dynamic interplay of localized component recruitment and release has been difficult to achieve in artificial molecular-scale systems, which are usually designed to have long-lasting, stable bonds. Here, we report the experimental realization of a molecular-scale system that dynamically assembles and disassembles its building blocks while retaining functionality...
January 10, 2018: Nano Letters
https://www.readbyqxmd.com/read/29296987/generic-maps-of-optimality-reveal-two-chemomechanical-coupling-regimes-for-motor-proteins-from-f1-atpase-and-kinesin-to-myosin-and-cytoplasmic-dynein
#4
Zhisong Wang
Many motor proteins achieve high efficiency for chemomechanical conversion, and single-molecule force-resisting experiments are a major tool to detect the chemomechanical coupling of efficient motors. Here, we introduce several quantitative relations that involve only parameters extracted from force-resisting experiments and offer new benchmarks beyond mere efficiency to judge the chemomechanical optimality or deficit of evolutionary remote motors on the same footing. The relations are verified by the experimental data from F1-ATPase, kinesin-1, myosin V and cytoplasmic dynein, which are representative members of four motor protein families...
January 3, 2018: Integrative Biology: Quantitative Biosciences From Nano to Macro
https://www.readbyqxmd.com/read/29295928/cargo-navigation-across-3d-microtubule-intersections
#5
Jared P Bergman, Matthew J Bovyn, Florence F Doval, Abhimanyu Sharma, Manasa V Gudheti, Steven P Gross, Jun F Allard, Michael D Vershinin
The eukaryotic cell's microtubule cytoskeleton is a complex 3D filament network. Microtubules cross at a wide variety of separation distances and angles. Prior studies in vivo and in vitro suggest that cargo transport is affected by intersection geometry. However, geometric complexity is not yet widely appreciated as a regulatory factor in its own right, and mechanisms that underlie this mode of regulation are not well understood. We have used our recently reported 3D microtubule manipulation system to build filament crossings de novo in a purified in vitro environment and used them to assay kinesin-1-driven model cargo navigation...
January 2, 2018: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/29229862/a-small-molecule-activator-of-kinesin-1-drives-remodeling-of-the-microtubule-network
#6
Thomas S Randall, Yan Y Yip, Daynea J Wallock-Richards, Karin Pfisterer, Anneri Sanger, Weronika Ficek, Roberto A Steiner, Andrew J Beavil, Maddy Parsons, Mark P Dodding
The microtubule motor kinesin-1 interacts via its cargo-binding domain with both microtubules and organelles, and hence plays an important role in controlling organelle transport and microtubule dynamics. In the absence of cargo, kinesin-1 is found in an autoinhibited conformation. The molecular basis of how cargo engagement affects the balance between kinesin-1's active and inactive conformations and roles in microtubule dynamics and organelle transport is not well understood. Here we describe the discovery of kinesore, a small molecule that in vitro inhibits kinesin-1 interactions with short linear peptide motifs found in organelle-specific cargo adaptors, yet activates kinesin-1's function of controlling microtubule dynamics in cells, demonstrating that these functions are mechanistically coupled...
December 11, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/29211997/challenges-in-estimating-the-motility-parameters-of-single-processive-motor-proteins
#7
Felix Ruhnow, Linda Kloβ, Stefan Diez
Cytoskeletal motor proteins are essential to the function of a wide range of intracellular mechano-systems. The biophysical characterization of their movement along their filamentous tracks is therefore of large importance. Toward this end, single-molecule, in vitro stepping-motility assays are commonly used to determine motor velocity and run length. However, comparing results from such experiments has proved difficult due to influences from variations in the experimental conditions and the data analysis methods...
December 5, 2017: Biophysical Journal
https://www.readbyqxmd.com/read/29202578/label-free-detection-of-microvesicles-and-proteins-by-the-bundling-of-gliding-microtubules
#8
Samata Chaudhuri, Till Korten, Slobodanka Korten, Gloria Milani, Tobia Lana, Geertruy Te Kronnie, Stefan Diez
Development of miniaturized devices for the rapid and sensitive detection of analyte is crucial for various applications across healthcare, pharmaceutical, environmental, and other industries. Here, we report on the detection of unlabeled analyte by using fluorescently-labeled, antibody-conjugated microtubules in a kinesin-1 gliding motility assay. The detection principle is based on the formation of fluorescent supramolecular assemblies of microtubule bundles and spools in the presence of multivalent analytes...
December 5, 2017: Nano Letters
https://www.readbyqxmd.com/read/29198755/differentiation-between-oppositely-oriented-microtubules-controls-polarized-neuronal-transport
#9
Roderick P Tas, Anaël Chazeau, Bas M C Cloin, Maaike L A Lambers, Casper C Hoogenraad, Lukas C Kapitein
Microtubules are essential for polarized transport in neurons, but how their organization guides motor proteins to axons or dendrites is unclear. Because different motors recognize distinct microtubule properties, we used optical nanoscopy to examine the relationship between microtubule orientations, stability, and modifications. Nanometric tracking of motors to super-resolve microtubules and determine their polarity revealed that in dendrites, stable and acetylated microtubules are mostly oriented minus-end out, while dynamic and tyrosinated microtubules are oriented oppositely...
November 28, 2017: Neuron
https://www.readbyqxmd.com/read/29140986/correction-kinesin-1-promotes-chondrocyte-maintenance-during-skeletal-morphogenesis
#10
Adrian Santos-Ledo, Marina Garcia-Macia, Philip D Campbell, Marta Gronska, Florence L Marlow
[This corrects the article DOI: 10.1371/journal.pgen.1006918.].
November 2017: PLoS Genetics
https://www.readbyqxmd.com/read/29112332/unbinding-of-kinesin-from-microtubule-in-the-strongly-bound-states-enhances-under-assisting-forces
#11
Hamidreza Khataee, Solmaz Naseri, Yongmin Zhong, Alan Wee-Chung Liew
The ability to predict the cellular dynamics of intracellular transport has enormous potential to impact human health. A key transporter is kinesin-1, an ATP-driven molecular motor that shuttles cellular cargos along microtubules (MTs). The dynamics of kinesins depends critically on their unbinding rate from MT, which varies depending on the force direction applied on the motor, i.e. the force-unbinding rate relation is asymmetric. However, it remains unclear how changing the force direction from resisting (applied against the motion direction) to assisting (applied in the motion direction) alters the kinesin's unbinding and stepping...
November 7, 2017: Molecular Informatics
https://www.readbyqxmd.com/read/29093025/phosphorylation-of-klc1-modifies-interaction-with-jip1-and-abolishes-the-enhanced-fast-velocity-of-app-transport-by-kinesin-1
#12
Kyoko Chiba, Ko-Yi Chien, Yuriko Sobu, Saori Hata, Shun Kato, Tadashi Nakaya, Yasushi Okada, Angus C Nairn, Masataka Kinjo, Hidenori Taru, Rong Wang, Toshiharu Suzuki
In neurons, amyloid β-protein precursor (APP) is transported by binding to kinesin-1, mediated by JNK-interacting protein 1b (JIP1b), which generates the enhanced fast velocity (EFV) and efficient high frequency (EHF) of APP anterograde transport. Previously we showed that EFV requires a conventional interaction between JIP1b C-terminal region and kinesin light chain 1 (KLC1) tetratricopeptide repeat, whereas EHF requires a novel interaction between the central region of JIP1b and the coiled-coil domain of KLC1...
November 1, 2017: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/29093024/phosphorylation-of-multiple-sites-within-an-acidic-region-of-alcadein-%C3%AE-is-required-for-kinesin-1-association-and-golgi-exit-of-alcadein-%C3%AE-cargo
#13
Yuriko Sobu, Keiko Furukori, Kyoko Chiba, Angus C Nairn, Masataka Kinjo, Saori Hata, Toshiharu Suzuki
Alcadein α (Alcα) is a major cargo of kinesin-1 that is subjected to anterograde transport in neuronal axons. Two tryptophan- and aspartic acid-containing (WD) motifs located in its cytoplasmic domain directly bind the tetratricopeptide repeat (TPR) motifs of kinesin light chain (KLC), which activate kinesin-1 and recruit kinesin-1 to Alcα cargo. We found that phosphorylation of three serine residues in the acidic region located between the two WD motifs is required for interaction with KLC. Phosphorylation of these serine residues may alter the disordered structure of the acidic region to induce the direct association with KLC...
November 1, 2017: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/29077261/tau-directs-intracellular-trafficking-by-regulating-the-forces-exerted-by-kinesin-and-dynein-teams
#14
Abdullah R Chaudhary, Florian Berger, Christopher L Berger, Adam G Hendricks
Organelles, proteins, and mRNA are transported bidirectionally along microtubules by plus-end directed kinesin and minus-end directed dynein motors. Microtubules are decorated by microtubule-associated proteins (MAPs) that organize the cytoskeleton, regulate microtubule dynamics and modulate the interaction between motor proteins and microtubules to direct intracellular transport. Tau is a neuronal MAP that stabilizes axonal microtubules and crosslinks them into bundles. Dysregulation of tau leads to a range of neurodegenerative diseases known as tauopathies including Alzheimer's disease (AD)...
October 27, 2017: Traffic
https://www.readbyqxmd.com/read/29046869/staphylococcus-aureus-alpha-toxin-induces-the-formation-of-dynamic-tubules-labeled-with-lc3-within-host-cells-in-a-rab7-and-rab1b-dependent-manner
#15
María M López de Armentia, María C Gauron, María I Colombo
Staphylococcus aureus is a pathogen that causes severe infectious diseases that eventually lead to septic and toxic shock. S. aureus infection is characterized by the production of virulence factors, including enzymes and toxins. After internalization S. aureus resides in a phagosome labeled with Rab7 protein. Here, we show that S. aureus generates tubular structures marked with the small GTPases Rab1b and Rab7 and by the autophagic protein LC3 at early times post-infection. As shown by live cell imaging these tubular structures are highly dynamic, extend, branch and grow in length...
2017: Frontiers in Cellular and Infection Microbiology
https://www.readbyqxmd.com/read/29035202/localised-dynactin-protects-growing-microtubules-to-deliver-oskar-mrna-to-the-posterior-cortex-of-the-drosophila-oocyte
#16
Ross Nieuwburg, Dmitry Nashchekin, Maximilian Jakobs, Andrew P Carter, Philipp Khuc Trong, Raymond E Goldstein, Daniel St Johnston
The localisation of oskar mRNA to the posterior of the Drosophila oocyte defines where the abdomen and germ cells form in the embryo. Kinesin 1 transports oskar mRNA to the oocyte posterior along a polarised microtubule cytoskeleton that grows from non-centrosomal microtubule organising centres (ncMTOCs) along the anterior/lateral cortex. Here, we show that the formation of this polarised microtubule network also requires the posterior regulation of microtubule growth. A missense mutation in the dynactin Arp1 subunit causes most oskar mRNA to localise in the posterior cytoplasm rather than cortically...
October 16, 2017: ELife
https://www.readbyqxmd.com/read/29033361/binding-of-pld2-generated-phosphatidic-acid-to-kif5b-promotes-mt1-mmp-surface-trafficking-and-lung-metastasis-of-mouse-breast-cancer-cells
#17
Ziqing Wang, Feng Zhang, Jingquan He, Ping Wu, Li Wei Rachel Tay, Ming Cai, Weiqi Nian, Yuanyuan Weng, Li Qin, Jeffrey T Chang, Laura B McIntire, Gilbert Di Paolo, Jianming Xu, Junmin Peng, Guangwei Du
Little is known about the cellular events promoting metastasis. We show that knockout of phospholipase D2 (PLD2), which generates the signaling lipid phosphatidic acid (PA), inhibits lung metastases in the mammary tumor virus (MMTV)-Neu transgenic mouse breast cancer model. PLD2 promotes local invasion through the regulation of the plasma membrane targeting of MT1-MMP and its associated invadopodia. A liposome pull-down screen identifies KIF5B, the heavy chain of the motor protein kinesin-1, as a new PA-binding protein...
October 23, 2017: Developmental Cell
https://www.readbyqxmd.com/read/28986254/enhanced-stability-of-kinesin-1-as-a-function-of-temperature
#18
K Chase, F Doval, M Vershinin
Kinesin-1 is a mechanochemical enzyme which mediates long distance intracellular cargo transport along microtubules in a wide variety of eukaryotic cells. Kinesin is also relatively easy to purify and shows robust function in vitro, leading to numerous proposals for using the kinesin-1/microtubule system for nanoscale transport in engineered devices. However, kinesin in vitro shows signs of degradation at ∼30 °C which severely limits its usability in biomimetic engineering. Notably, kinesin-1 functions robustly in animal cells at body temperatures as high as 40 °C which suggests that kinesin functioning can be stabilized beyond what is observed in vitro...
November 25, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28980869/regulation-of-autophagic-lysosome-reformation-by-kinesin-1-clathrin-and-phosphatidylinositol-4-5-bisphosphate
#19
Xu Liu, Daniel J Klionsky
No abstract text is available yet for this article.
October 5, 2017: Autophagy
https://www.readbyqxmd.com/read/28978447/acetylated-microtubules-are-preferentially-bundled-leading-to-enhanced-kinesin-1-motility
#20
Linda Balabanian, Christopher L Berger, Adam G Hendricks
The motor proteins kinesin and dynein transport organelles, mRNA, proteins, and signaling molecules along the microtubule cytoskeleton. In addition to serving as tracks for transport, the microtubule cytoskeleton directs intracellular trafficking by regulating the activity of motor proteins through the organization of the filament network, microtubule-associated proteins, and tubulin posttranslational modifications. However, it is not well understood how these factors influence motor motility, and in vitro assays and live cell observations often produce disparate results...
October 3, 2017: Biophysical Journal
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