Kinesin proteins: A phylum of motors for microtubule‐based motility

@article{Moore1996KinesinPA,
  title={Kinesin proteins: A phylum of motors for microtubule‐based motility},
  author={Jonathan D. Moore and Sharyn A. Endow},
  journal={BioEssays},
  year={1996},
  volume={18}
}
The cellular processes of transport, division and, possibly, early development all involve microtubule‐based motors. Recent work shows that, unexpectedly, many of these cellular functions are carried out by different types of kinesin and kinesin‐related motor proteins. The kinesin proteins are a large and rapidly growing family of microtubule‐motor proteins that share a 340‐amino‐acid motor domain. Phylogenetic analysis of the conserved motor domains groups the kinesin proteins into a number of… 

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...

References

SHOWING 1-10 OF 74 REFERENCES

Molecular phylogeny of the kinesin family of microtubule motor proteins.

Phylogenetic analysis of the motor regions of the kinesin proteins reveals at least five clearly defined groups that are likely to identify kinesins with different roles in basic cellular processes.

The Neurospora organelle motor: a distant relative of conventional kinesin with unconventional properties.

This work reports the identification, biochemical and immunological characterization, and molecular cloning of a cytoplasmic motor in a "lower" eukaryote, the Ascomycete fungus Neurospora crassa, and identifies Nkin as a distant relative of the family of conventional kinesins.

Suppression of a myosin defect by a kinesin-related gene

The identification of a suppressor (SMY1) that (surprisingly) encodes a predicted polypeptide sharing sequence similarity with the motor portion of proteins in the kinesin superfamily is reported.

Identification of kinesin in sea urchin eggs, and evidence for its localization in the mitotic spindle

The identification and isolation of a kinesin-like protein from the cytoplasm of sea urchin eggs is described and proposed that it may be a mechanochemical factor for some form of motility associated with the mitotic spindle.

A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles

The gene that encodes this antigen contains a domain with strong sequence similarity to the motor domain of kinesin-like proteins, and the product of this gene, expressed in bacteria, can cross-bridge antiparallel microtubules in vitro, and in the presence of Mg–ATP,microtubules slide over one another in a fashion reminiscent of microtubule movements during spindle elongation.

Kinesin family in murine central nervous system

Cloned and characterized five different members (KIF1-5), that encode the microtubule-associated motor domain homologous to kinesin heavy chain, in murine brain tissue and revealed that KIF1, KIF3, and KIF5 are expressed almost exclusively in Murine brain, whereas KIF2 and Kif4 are expressed in brain as well as in other tissues.

Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ncd protein.

It is found that the conserved domain of both proteins has microtubule motor activity, although the efficiency with which ATP hydrolysis is coupled to microtubules movement declines dramatically with increasing truncation.

Evidence for kinesin-related proteins in the mitotic apparatus using peptide antibodies.

It is reported that, unlike antibodies to conventional kinesin, the peptide antibodies to the kines in motor domain immunofluorescently label spindles and kinetochores in mitotic tissue culture cells, suggesting that kinesIn-like proteins may have important roles in chromosome movement and mitosis.
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