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Walking on two heads: the many talents of kinesin

Nature Reviews Molecular Cell Biology volume 1, pages 50–58 (2000)Cite this article

Abstract

The gallop of a race horse and the minute excursions of a cellular vesicle have one thing in common: they are based on the directional movement of proteins termed molecular motors — many trillions in the case of the horse, just a few in the case of the cell vesicle. These tiny machines take nanometre steps on a millisecond timescale to drive all biological movements. Over the past 15 years new biochemical and biophysical approaches have allowed us to take a giant step forward in understanding the molecular basis of motor mechanics.

Key Points

  • Most biological movements are accomplished by protein machines, termed molecular motors. The best-studied of these are the cytoskeletal motors, including myosin, which binds actin, and kinesin and dynein, which both bind microtubules. This review focuses primarily on kinesin.

  • The catalytic motor domain shows the highest homology between different cytoskeletal motors. It possesses a binding site for ATP and a binding site for the cytoskeletal element. There is little homology outside the catalytic domain. However, even though myosin and kinesin show no sequence similarity, their catalytic motor domains are closely related structurally.

  • Motors undergo conformational changes that are driven by ATP hydrolysis. This is translated into unidirectional movement by structural elements adjacent to the catalytic motor domain.

  • Within the kinesin superfamily, most motors move towards the plus end of microtubules. Non-claret disjunctional (Ncd), however, moves in the opposite direction, towards the minus end. Using artificial chimeric motors, the region responsible for determining the direction of movement has been mapped to the neck and neck linker regions

  • Kinesins take many steps along microtubules without falling off; this is termed ‘processivity’. This is achieved by precise coordination between the two kinesin heads, so that one head is always bound; this is tightly coupled to ATP hydrolysis. Single- headed motors can also be processive.

  • Regulation of kinesin activity is largely mediated by an intramolecular interaction between the head and tail, resulting in a compact conformation that inhibits the ATPase activity of the head. Cargo binding relieves this tail inhibition.

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Figure 1: Overview of three molecular motor ‘prototypes’.
Figure 2: Overview of the domain organization, heavy chain molecular weight, polarity of movement and velocity of the main kinesin families.
Figure 3: Domain organization of the conventional kinesin heavy-chain dimer, showing the crystal structure of the catalytic domains and the neck96.
Figure 4: Crystal structures of dimeric Ncd and conventional kinesin.
Figure 5: Processive catalysis of conventional kinesin.
Figure 6: Model for how cargo binding might be linked to motor activation.

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Acknowledgements

We thank U. Euteneuer and K. Hahlen for valuable comments. Work in the authors’ laboratory is supported by the Deutsche Forschungsgemeinschaft, the Volkswagen Stiftung, and the Fonds der Chemischen Industrie.

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Authors and Affiliations

  1. Adolf-Butenandt-Institut, Zellbiologie, University of Munich, Schillerstrasse 42, Munich, 80336, Germany

    Günther Woehlke & Manfred Schliwa

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DATABASE LINKS

myosin

dynein

kinesin

ncd

myosin VI

myosin V

KIF1A

FURTHER INFORMATION

Kinesin home page

Structure and function of microtubules

Online animation: Kinesin stepping

ENCYCLOPEDIA OF LIFE SCIENCES

Dynein and kinesin

Cytoskeleton

Intracellular transport

ATP-binding motifs

Glossary

P-LOOP-TYPE ATP-BINDING SITE

‘Phosphate-binding loop’; a nucleotide-binding consensus motif (GXXXXGKT/S) at the ATP-binding site.

CROSSBRIDGE CYCLE

The sequence of structural changes of a myosin head coordinated with the hydrolysis of one molecule of ATP.

DUTY RATIO

The fraction of time that a motor molecule remains attached to the track during one full ATP hydrolysis cycle.

GLIDING ASSAY

Optical assay for the movement of cytoskeletal filaments over a ‘lawn’ of motor molecules attached to a coverslip.

OPTICAL TRAP ASSAY

A focused laser beam that traps refractile particles (for example, polystyrene beads) with attached motor molecules, allowing determination of step size and force per step.

RETAINING FORCE

Force exerted by a laser trap on a motor-carrying bead, moving along a microtubule. molecule of ATP.

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Woehlke, G., Schliwa, M. Walking on two heads: the many talents of kinesin. Nat Rev Mol Cell Biol 1, 50–58 (2000). https://doi.org/10.1038/35036069

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