Literature DB >> 18802450

Processive kinesins require loose mechanical coupling for efficient collective motility.

Peter Bieling1, Ivo A Telley, Jacob Piehler, Thomas Surrey.   

Abstract

Processive motor proteins are stochastic steppers that perform actual mechanical steps for only a minor fraction of the time they are bound to the filament track. Motors usually work in teams and therefore the question arises whether the stochasticity of stepping can cause mutual interference when motors are mechanically coupled. We used biocompatible surfaces to immobilize processive kinesin-1 motors at controlled surface densities in a mechanically well-defined way. This helped us to study quantitatively how mechanical coupling between motors affects the efficiency of collective microtubule transport. We found that kinesin-1 constructs that lack most of the non-motor sequence slow each other down when collectively transporting a microtubule, depending on the number of interacting motors. This negative interference observed for a motor ensemble can be explained quantitatively by a mathematical model using the known physical properties of individual molecules of kinesin-1. The non-motor extension of kinesin-1 reduces this mutual interference, indicating that loose mechanical coupling between motors is required for efficient transport by ensembles of processive motors.

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Year:  2008        PMID: 18802450      PMCID: PMC2581844          DOI: 10.1038/embor.2008.169

Source DB:  PubMed          Journal:  EMBO Rep        ISSN: 1469-221X            Impact factor:   8.807


  27 in total

1.  Comparison of reflectometric interference spectroscopy with other instruments for label-free optical detection.

Authors:  C Hänel; G Gauglitz
Journal:  Anal Bioanal Chem       Date:  2001-12-12       Impact factor: 4.142

2.  Reconstitution of a microtubule plus-end tracking system in vitro.

Authors:  Peter Bieling; Liedewij Laan; Henry Schek; E Laura Munteanu; Linda Sandblad; Marileen Dogterom; Damian Brunner; Thomas Surrey
Journal:  Nature       Date:  2007-12-02       Impact factor: 49.962

3.  How kinesin waits between steps.

Authors:  Teppei Mori; Ronald D Vale; Michio Tomishige
Journal:  Nature       Date:  2007-11-14       Impact factor: 49.962

4.  Importance of a flexible hinge near the motor domain in kinesin-driven motility.

Authors:  M Grummt; G Woehlke; U Henningsen; S Fuchs; M Schleicher; M Schliwa
Journal:  EMBO J       Date:  1998-10-01       Impact factor: 11.598

5.  Molecular motors: structural adaptations to cellular functions.

Authors:  J Howard
Journal:  Nature       Date:  1997-10-09       Impact factor: 49.962

6.  The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain.

Authors:  R B Case; D W Pierce; N Hom-Booher; C L Hart; R D Vale
Journal:  Cell       Date:  1997-09-05       Impact factor: 41.582

7.  Movement of microtubules by single kinesin molecules.

Authors:  J Howard; A J Hudspeth; R D Vale
Journal:  Nature       Date:  1989-11-09       Impact factor: 49.962

8.  Direct observation of kinesin stepping by optical trapping interferometry.

Authors:  K Svoboda; C F Schmidt; B J Schnapp; S M Block
Journal:  Nature       Date:  1993-10-21       Impact factor: 49.962

9.  Microtubule movement by a biotinated kinesin bound to streptavidin-coated surface.

Authors:  E Berliner; H K Mahtani; S Karki; L F Chu; J E Cronan; J Gelles
Journal:  J Biol Chem       Date:  1994-03-18       Impact factor: 5.157

10.  Processivity of the motor protein kinesin requires two heads.

Authors:  W O Hancock; J Howard
Journal:  J Cell Biol       Date:  1998-03-23       Impact factor: 10.539

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  30 in total

1.  Obstacles on the microtubule reduce the processivity of Kinesin-1 in a minimal in vitro system and in cell extract.

Authors:  Ivo A Telley; Peter Bieling; Thomas Surrey
Journal:  Biophys J       Date:  2009-04-22       Impact factor: 4.033

2.  Watching the walk: observing chemo-mechanical coupling in a processive myosin motor.

Authors:  Enrique M De La Cruz; Adrian O Olivares
Journal:  HFSP J       Date:  2009-03-18

3.  Force-velocity relationship for multiple kinesin motors pulling a magnetic bead.

Authors:  Todd L Fallesen; Jed C Macosko; G Holzwarth
Journal:  Eur Biophys J       Date:  2011-07-07       Impact factor: 1.733

4.  Tunable dynamics of microtubule-based active isotropic gels.

Authors:  Gil Henkin; Stephen J DeCamp; Daniel T N Chen; Tim Sanchez; Zvonimir Dogic
Journal:  Philos Trans A Math Phys Eng Sci       Date:  2014-11-28       Impact factor: 4.226

5.  Cargo transport at microtubule crossings: evidence for prolonged tug-of-war between kinesin motors.

Authors:  Olaolu Osunbayo; Jacqualine Butterfield; Jared Bergman; Leslie Mershon; Vladimir Rodionov; Michael Vershinin
Journal:  Biophys J       Date:  2015-03-24       Impact factor: 4.033

6.  Intracellular cargo transport by single-headed kinesin motors.

Authors:  Kristin I Schimert; Breane G Budaitis; Dana N Reinemann; Matthew J Lang; Kristen J Verhey
Journal:  Proc Natl Acad Sci U S A       Date:  2019-03-08       Impact factor: 11.205

7.  Cargo Transport by Two Coupled Myosin Va Motors on Actin Filaments and Bundles.

Authors:  M Yusuf Ali; Andrej Vilfan; Kathleen M Trybus; David M Warshaw
Journal:  Biophys J       Date:  2016-11-15       Impact factor: 4.033

8.  Transport efficiency of membrane-anchored kinesin-1 motors depends on motor density and diffusivity.

Authors:  Rahul Grover; Janine Fischer; Friedrich W Schwarz; Wilhelm J Walter; Petra Schwille; Stefan Diez
Journal:  Proc Natl Acad Sci U S A       Date:  2016-11-01       Impact factor: 11.205

9.  The kinetics of mechanically coupled myosins exhibit group size-dependent regimes.

Authors:  Lennart Hilbert; Shivaram Cumarasamy; Nedjma B Zitouni; Michael C Mackey; Anne-Marie Lauzon
Journal:  Biophys J       Date:  2013-09-17       Impact factor: 4.033

10.  Microtubule organization by the antagonistic mitotic motors kinesin-5 and kinesin-14.

Authors:  Christian Hentrich; Thomas Surrey
Journal:  J Cell Biol       Date:  2010-05-03       Impact factor: 10.539

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