339 results found
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Structural basis for the assembly of the mitotic motor Kinesin-5 into bipolar tetramers

    Jessica E Scholey, Stanley Nithianantham ... Jawdat Al-Bassam
    The Bipolar Assembly domain of kinesin-5 comprises an anti-parallel four-helix bundle, which explains how kinesin-5 subunits assemble into bipolar tetramers with two motile ends that transmit forces while crosslinking and sliding adjacent microtubules during mitosis.
    1. Cell Biology
    2. Structural Biology and Molecular Biophysics

    The kinesin-5 tail domain directly modulates the mechanochemical cycle of the motor domain for anti-parallel microtubule sliding

    Tatyana Bodrug, Elizabeth M Wilson-Kubalek ... Jawdat Al-Bassam
    Biochemical, single molecule, cell and structural biology studies reveal an interaction between the kinesin-5 tail and motor domains regulating high-force production, which is critical for microtubule sliding motility.
    1. Cell Biology

    Intracellular functions and motile properties of bi-directional kinesin-5 Cin8 are regulated by neck linker docking

    Alina Goldstein-Levitin, Himanshu Pandey ... Larisa Gheber
    Precise hydrogen-bond stabilization of the neck linker docking onto the catalytic motor domain, is crucial for motor activity and intracellular functions of the bi-directional mitotic kinesin-5 Cin8.
    1. Cell Biology
    2. Physics of Living Systems

    Concerted action of kinesins KIF5B and KIF13B promotes efficient secretory vesicle transport to microtubule plus ends

    Andrea Serra-Marques, Maud Martin ... Anna Akhmanova
    The function and distribution of kinesin motors on exocytotic vesicles is dissected and visualized through a combination of gene knockout experiments, high-resolution microscopy and advanced data analysis.
    1. Cell Biology
    2. Genetics and Genomics

    Multiple motors cooperate to establish and maintain acentrosomal spindle bipolarity in C. elegans oocyte meiosis

    Gabriel Cavin-Meza, Michelle M Kwan, Sarah M Wignall
    Rapid depletion of dynein from oocytes yielded new insights into acentrosomal pole organization and also led to the first evidence that the kinesin-5 motor BMK-1 plays a role in microtubule organization during C. elegans meiosis.
    1. Cell Biology
    2. Computational and Systems Biology

    Mechanisms of chromosome biorientation and bipolar spindle assembly analyzed by computational modeling

    Christopher Edelmaier, Adam R Lamson ... Meredith D Betterton
    A computational model of fission yeast mitosis can interrogate mechanisms required for successful mitosis, the origin of spindle length fluctuations, and spindle force balance during assembly.
    1. Cell Biology

    Changes in seam number and location induce holes within microtubules assembled from porcine brain tubulin and in Xenopus egg cytoplasmic extracts

    Charlotte Guyomar, Clément Bousquet ... Denis Chrétien
    Tubulin engages unique lateral interactions without longitudinal ones during microtubule polymerization, leaving holes of a few subunits size potentially at the origin of tubulin exchange within their shaft.
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Motor Proteins: A surprising twist

    Nikta Fakhri, Christoph F Schmidt
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    1. Cell Biology

    Microtubule-mediated GLUT4 trafficking is disrupted in insulin-resistant skeletal muscle

    Jonas R Knudsen, Kaspar W Persson ... Thomas Elbenhardt Jensen
    Microtubule-dependent movement of the glucose transporter GLUT4 is important for insulin-stimulated muscle glucose uptake, involves the motor protein KIF5B, and is impaired in muscle from diet-induced obese mice.
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Cytoplasmic dynein crosslinks and slides anti-parallel microtubules using its two motor domains

    Marvin E Tanenbaum, Ronald D Vale, Richard J McKenney
    The motor domains of dynein are sufficient to crosslink microtubules and slide them antiparallel to each other.

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