Universal and Unique Features of Kinesin Motors: Insights from a Comparison of Fungal and Animal Conventional Kinesins
- 1 July 1999
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry
- Vol. 380 (7-8) , 915-921
- https://doi.org/10.1515/bc.1999.113
Abstract
Kinesins are microtubule motors that use the energy derived from the hydrolysis of ATP to move unidirectionally along microtubules. The founding member of this still growing superfamily is conventional kinesin, a dimeric motor that moves processively towards the plus end of microtubules. Within the family of conventional kinesins, two groups can be distinguished to date, one derived from animal species, and one originating from filamentous fungi. So far no conventional kinesin has been reported from plant cells. Fungal and animal conventional kinesins differ in several respects, both in terms of their primary sequence and their physiological properties. Thus all fungal conventional kinesins move at velocities that are 4–5 times higher than those of animal conventional kinesins, and all of them appear to lack associated light chains. Both groups of motors are characterized by a number of group-specific sequence features which are considered here with respect to their functional importance. Animal and fungal conventional kinesins also share a number of sequence characteristics which point to common principles of motor function. The overall domain organization is remarkably similar. A C-terminal sequence motif common to all kinesins, which constitutes the only region of high homology outside the motor domain, suggests common principles of cargo association in both groups of motors. Consideration of the differences of, and similarities between, fungal and animal kinesins offers novel possibilities for experimentation (e. g., by constructing chimeras) that can be expected to contribute to our understanding of motor function.Keywords
This publication has 47 references indexed in Scilit:
- Kin I Kinesins Are Microtubule-Destabilizing EnzymesPublished by Elsevier ,1999
- The C-Terminal Region of the Stalk Domain of Ubiquitous Human Kinesin Heavy Chain Contains the Binding Site for Kinesin Light ChainBiochemistry, 1998
- Determinants of Kinesin Motor PolarityScience, 1998
- Proteolytic mapping of kinesin/ncd-microtubule interface: nucleotide-dependent conformational changes in the loops L8 and L12The EMBO Journal, 1998
- The Directional Preference of Kinesin Motors Is Specified by an Element outside of the Motor Catalytic DomainCell, 1997
- Molecular Requirements for Bi-directional Movement of Phagosomes Along MicrotubulesThe Journal of cell biology, 1997
- In search of membrane receptors for microtubule-based motors — is kinectin a kinesin receptor?Trends in Cell Biology, 1996
- Conserved Structures and Diversity of Functions of RNA-Binding ProteinsScience, 1994
- Effects of Kinesin Mutations on Neuronal FunctionsScience, 1992
- A novel brain ATPase with properties expected for the fast axonal transport motorNature, 1985