K.J. Böhm, Leibniz Institute for Age Research - Fritz Lipmann Institute, Jena, Germany

Kinesins are eukaryotic microtubule-associated motor proteins (also called mechanochemical proteins) which convert chemical energy released from nucleoside triphosphates (preferentially from ATP) into mechanical energy.

Within the last decade, numerous kinesin isoforms and related proteins, sharing a common motor domain of 340-350 amino acids (see Sakowicz et al., 1998; Stewart et al., 1993), have been described in animal and plant cells as well as in lower eukaryotic organisms, e.g., yeast and Aspergillus (for reviews see Goodson et al., 1994, Vale and Fletterick, 1997, Hirokawa, 1998).
A prominent member of the kinesin superfamily, currently including more than 600 sequences from a variety of species (see Marx et al. 2005), is the conventional kinesin (kinesin-1, see recent nomenclature published by LAWRENCE et al. 2004), which essentially contributes to anterograde vesicle transport in neuronal cells (Schnapp et al., 1992).  It is a plus end-directed molecular motor, whose ATPase is strongly promoted by microtubules (Kuznetsov and Gelfand, 1986; Huang and Hackney, 1994).


Dreblow K., Böhm KJ,: Mechanism of kinesin-dependent vesicle transport along a microtubule

(Copyright 2009. All rights reserved by the authors)

Kinesin-1 is a dimer (Hirose and Amos, 1999) consisting of two identical 120 to 130-kDa chains, commonly known as heavy chains. When kinesin is purified from brain homogenates, two light chains (60 to 70 kDa) were found to be associated with the dimers (Kull 2000). These light chains, which are involved in the kinesin binding to organelles, are not essential for motility generation (Howard 1997) and seem to have regulatory functions ((Verhey et al., 1998).

Kinesin-1 comprises three distinct domains:  the N-terminal motor domain, the central stalk domain, and the C-terminal fan-shaped tail, which is (presumably together with the stalk) implicated in cargo binding.
The motor domain, which is known to be a highly conserved region characteristic for very different members of the kinesin superfamily,  can be subdivided into the core motor domain, the adjacent neck linker and the neck region.
Its core domain, consisting of about 325 amino acids, contains both the microtubule-binding and the ATPase-active sites (Kull 2000).
The stalk region is described to be responsible for dimerization.

    Kinesin dimer (for a detailed scheme see Woehlke and Schliwa 2000)

The kinesin head domain has the shape of an arrow head with dimensions of approximately 7.5 nm x 4.5 nm x 4.5 nm. X-ray structural analysis revealed a central, eight-stranded beta-sheet with three alpha-helices on either side (Kull et al. 1996; Sack et al. 1997).

A characteristic feature of the two-headed kinesin-1 is its processivity, i.e., single kinesin molecules move along microtubules of several micrometers length without dissociating (Block et al., 1990; Crevel et al., 1997; Hancock and Howard, 1998). Both heads translocate by turns in 16-nm steps, resulting in an 8-nm centre-of-mass migration (Mandelkow and Johnson, 1998), one of them is always bound to the microtubule (Ray et al., 1993; Kozielski et al., 1998). Recently, it has been shown that also one-headed members of the kinesin superfamily, e.g., KIF1A, can realize movement in a processive fashion. This was explained by the existence of two microtubule-binding motifs in one head (Schief and Howard, 2001).

Intracellular movement and transport processes can be mimicked in vitro either by gliding of taxol-stabilized microtubules across kinesin-coated glass surfaces (Vale et al., 1985; von Massow et al., 1989; Schnapp et al., 1990) or by translocation of kinesin-coated polymer beads along immobilized microtubules (Kuo et al., 1991).


        Microtubule gliding across a kinesin-coated glass surface (Copyright 2009. K. Dreblow, KJ. Böhm, FLI Jena)         Video sequence of microtubules gliding across kinesin-coated glass surface

The velocity of motility generated by kinesin-1 is typically found between 0.4 µm/s and 0.9 µm/s (Vale et al., 1985; von Massow et al., 1989, Steinberg and Schliwa 1996, Böhm et al., 1997). For comparison, a kinesin from the fungus Neurospora was found to walk  at velocities up to 3.8 µm/s (Steinberg and Schliwa 1996). In contrast, the mitotic kinesin Eg5 moves at about 0.06 µm/s, only (Lockhart and Cross 1996). For  kinesin-1 it was shown that microtubule gliding can be accelerated by increasing the Mg2+ concentration at a constant ATP concentration (Böhm et al. 2000a) and by temperature elevation (Böhm et al. 2000b). At high temperatures velocities up to 3.7 µm/s were measured (Kawaguchi and Ishiwata 2001).

Microtubule gliding across a kinesin-coated glass surface in the presence of 5.0 M glycerol

In the presence of glycerol or other polyhydroxy compounds, a remarkable fraction of the microtubules gliding across a kinesin-coated glass surface did not follow a straight line but circular tracks (Böhm et al. 2001).

Further information on kinesin and other cytoskeleton motor proteins can be obtained from our recent review on Kinesin and nanoactuators. (Böhm KJ, Unger E, 2004)
See also the recent review of             Marx A, Muller J, Mandelkow E.: The structure of microtubule motor proteins.  Adv Protein Chem. 71 (2005) 299-344.


  • Böhm KJ: Kinesin-dependent motility generation as target mechanism of cadmium intoxication. Toxicol. Lett  (in press)
  • Dreblow K., Kalchishkova N., Böhm K.J.: Kinesin passing permanent blockages along its protofilament track. Biochem. Biophys. Res. Commun. 395, 490–495  (2010)
  • Dreblow K., Kalchishkova N., Böhm K.J.: Kinesin bypassing blockages on microtubule rails. Biophys. Rev. Lett.  4, 139-151 (2009)
  • Kalchishkova N., Böhm K.J.: On the relevance of the core helix αlpha 6 to kinesin activity generation. Biophys. Rev. Lett. 4, 63-75 (2009)
  • Kalchishkova N., Böhm KJ.: The role of kinesin neck linker and neck in velocity regulation. J. Mol. Biol.  382, 127-135 (2008)
  • BLOCK SM, GOLDSTEIN LS, SCHNAPP BJ, 1990. Bead movement by single kinesin molecules studied with optical tweezers. Nature 348: 348-352.
    BLOOM GS, WAGNER MC, PFISTER KK, BRADY ST, 1988. Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide. Biochem 27: 3409-3416.
    BÖHM KJ, STEINMETZER P, DANIEL A, VATER W, BAUM M, UNGER E, 1997. Kinesin-driven microtubule motility in the presence of alkaline-earth metal ions. Indication for calcium ion-dependent motility. Cell Motil Cytoskeleton 37: 226-231.
    Böhm KJ, Stracke R, Unger E, 2000a. Speeding up kinesin-driven microtubule gliding in vitro by variation of cofactor composition and physicochemical parameters. Cell Biol. Int., 24, 335-341.
    öhm KJ, Stracke R, Baum M, Zieren M, Unger E, 2000b. Effect of temperature on kinesin-driven microtubule gliding and kinesin ATPase activity. FEBS Letters 466, 59-62.
    Böhm KJ, Stracke R, Vater W, Unger E, 2001: Inhibition of kinesin-driven microtubule motility by polyhydroxy compounds. In: Micro- and Nanostructures of Biological Systems (eds. Hein
    H-J, Bischoff G) Shaker Verlag Aachen, pp. 153-165 (2001)
    Böhm KJ, Unger E, 2004. Kinesin and nanoactuators. In
    : Encyclopedia of Nanoscience and Nanotechnology (ed. Nalwa, HS) American Scientific Publishers vol.  4, pp. 345-357
    BRADY ST, 1991. Molecular motors in the nervous system. Neuron 7: 521-533.

    COHN SA, INGOLD AL, SCHOLEY JM, 1989. Quantitative analysis of sea urchin egg kinesin-driven microtubule motility. J Biol Chem: 264: 4290-4297.
    CORREIA JJ, GILBERT SP, MOYER ML, JOHNSON KA, 1995. Sedimentation studies on the kinesin motor domain constructs K401, K366, and K341. Biochemistry 34: 4898-4907.
    CREVEL IM, LOCKHART A, CROSS RA , 1997. Kinetic evidence for low chemical processivity in ncd and Eg5. J Mol Biol 273: 160-170.
    GOODSON HV, KANG SJ, ENDOW SA, 1994. Molecular phylogeny of the kinesin family of microtubule motor proteins. J Cell Sci 107: 1875-1884.
    HACKNEY DD, LEVITT JD, SUHAN J, 1992. Kinesin undergoes a 9 S to 6 S conformational transition. J Biol Chem 267: 8696-8701.
    HANCOCK WO, HOWARD J, 1998. Processivity of the motor protein kinesin requires two heads. J Cell Biol 140: 1395-1405.
    HARRISON BC, MARCHESE-RAGONA SP, GILBERT SP, CHENG N, STEVEN AC, JOHNSON KA, 1993. Decoration of the microtubule surface by one kinesin head per tubulin heterodimer. Nature 362: 73-75.
    HIROKAWA N, PFISTER KK, YORIFUJI H, WAGNER MC, BRADY ST, BLOOM GS, 1989. Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration. Cell 56: 867-878.
    HIROKAWA N, 1998. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279: 519-526.
    Hirose K,  Amos LA, 1999. Three-dimensional structure of motor molecules. Cell. Mol. Life Sci. 56, 184-199.
    Howard J, 1997. Molecular motors: structural adaptations to cellular functions. Nature 389, 561-567
    HOWARD J, HUDSPETH AJ, VALE RD, 1989. Movement of microtubules by single kinesin molecules. Nature 342: 154-158.
    HUANG TG, HACKNEY DD, 1994. Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterization. J Biol Chem 269: 16493-16501.

    HUNT AJ, GITTES F, HOWARD J, 1994. The force exerted by a single kinesin molecule against a viscous load. Biophys J 67: 766-781.
    Kawaguchi K, Ishiwata S, 2001. Thermal activation of single kinesin molecules with temperature pulse microscopy. Cell Motil. Cytoskel., 49, 41-47.
    KOZIELSKI F, ARNAL I, WADE RH, 1998. A model of the microtubule-kinesin complex based on electron cryomicroscopy and X-ray crystallography. Curr Biol 8: 191-198.
    KUO SC, GELLES J, STEUER E, SHEETZ MP, 1991. A model for kinesin movement from nanometer-level movements of kinesin and cytoplasmic dynein and force measurements. J Cell Sci Suppl 14: 135-138.  
    KULL FJ, 2000. Motor proteins of the kinesin superfamily: structure and mechanism. in Essays in Biochemistry. Molecular Motors edited Banting G, Higgins S.J.  Portland Press, London, pp. 61-73.
    Kull FJ, , Sablin EP , Lau R , Fletterick RJ , Vale RD, 1996. Crystal structure of the kinesin motor domain  reveals a structural similarity to myosin.
    Nature 380, 550 (1996).
    KUZNETSOV SA, GELFAND VI, 1986. Bovine brain kinesin is a microtubule-activated ATPase. Proc Natl Acad Sci USA 83: 8530-8534.

    LAWRENCE CJ, DAWE RK, CHRISTIE KR et al. 2004. A standardized kinesin nomenclature. J. Cell Biol. 167, 19-22
    Lockhart A, Cross RA, 1996. Kinetics and motility of the Eg5 microtubule motor. Biochemistry 35, 2365-2373
    The structural and mechanochemical cycle of kinesin. Trends Biochem Sci 23: 429-433.
    Marx A, Muller J, Mandelkow E, 2005. The structure of microtubule motor proteins. Adv Protein Chem. 71: 299-344. Review.
    PORTER ME, SCHOLEY JM, STEMPLE DL, VIGERS GP, VALE RD, SHEETZ MP, MCINTOSH JR, 1987. Characterization of the microtubule movement produced by sea urchin egg kinesin. J Biol Chem 262: 2794-2802.
    RAY S, MEYHÖFER E, MILLIGAN RA, HOWARD J, 1993. Kinesin follows the microtubule's protofilament axis. J Cell Biol 121: 1083-1093.
    Sack S, Müller J, Marx A, Thormählen M, Mandelkow E.-M, Brady ST, Mandelkow E, 1997. X-ray structure of motor and neck somains of rat brain kinesin. Biochemistry 36, 16155-16165 (1997).
    SAKOWICZ R, BERDELIS MS, RAY K, BLACKBURN CL, HOPMANN C, FAULKNER DJ, GOLDSTEIN LS, 1998. A marine natural product inhibitor of kinesin motors. Science 280: 292-295.
    SAXTON WM, PORTER ME, COHN SA, SCHOLEY JM, RAFF EC, MCINTOSH JR, 1988. Drosophila kinesin: characterization of microtubule motility and ATPase. Proc Natl Acad Sci USA 85: 1109-1113.
    SCHIEF WR, Howard J, 2001. Conformational changes during kinesin motility. Current Opin Cell Biol 13: 19-28
    SCHOLEY JM, HEUSER J, YANG JT, GOLDSTEIN LS, 1989. Identification of globular mechanochemical heads of kinesin.
    Nature 338: 355-357.

    SCHOLEY JM, VALE RD, 1994. Kinesin-based organelle transport. Microtubules. Alan R Liss, Inc, New York/Chichester/Brisbane/Toronto/Singapore, pp. 343-365.
    SCHNAPP BJ, CRISE B, SHEETZ MP, REESE TS, KHAN S, 1990. Delayed start-up of kinesin-driven microtubule gliding following inhibition by adenosine 5'-[beta,gamma-imido]triphosphate. Proc Natl Acad Sci USA 87: 10053-10057.
    SCHNAPP BJ, REESE TS, BECHTOLD R, 1992. Kinesin is bound with high affinity to squid axon organelles that move to the plus-end of microtubules. J Cell Biol 119: 389-399.
    STEINBERG G, SCHLIWA M, 1995. The Neurospora organelle motor: A distant relative of conventional kinesin with unconventional properties. Molec Biol Cell 6: 1605-1618.
    STEINBERG G, SCHLIWA M, 1996. Characterization of the biophysical and motility properties of kinesin from the fungus Neurospora crassa. J Biol Chem 271: 7516-7521.
    STEWART RJ, THALER JP, GOLDSTEIN LS, 1993. Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ncd protein. Proc Natl Acad Sci USA 90: 5209-5213.
    VALE RD, FLETTERICK RJ, 1997. The design plan of kinesin motors. Ann Rev Cell Dev Biol 13: 745-777.
    VALE RD, REESE TS, SHEETZ MP, 1985. Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell  42: 39-50.
    VERHEY KJ, LIZOTTE DL, ABRAMSON T, BARENBOIM L, SCHNAPP BJ, RAPOPORT TA, 1998. Light chain-dependent regulation of kinesin's interaction with microtubules. J Cell Biol 143: 1053-1066.
    Interaction between kinesin, microtubules, and microtubule-associated protein 2. Cell Motil Cytoskeleton 14: 562-571.
    Woehlke G, Schliwa M, 2000. Walking on two heads: the many talents of kinesin. Nat. Rev. Mol. Cell Biol. 1, 50-58



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