Interdomain interactions in the KIF3 kinesin family motor. 2nd joint conference of the IEEE engineering in medicine and biology society and the biomedical engineering society

W. O. Hancock, Y. Zhang, Y. C. Lee

Research output: Contribution to journalConference articlepeer-review

Abstract

Kinesins comprise a family of molecular motors that transport intracellular cargo along microtubules. While the performance of conventional kinesin has received considerable attention, much less is known about the design features and performance of other kinesins. KIF3A/B is an especially intriguing kinesin because it contains two non-identical heads, a design that may confer added speed, affinity, strength, or some other ability. To test KIF3A/B function, we have expressed and purified full-length motors in a eukaryotic expression system and investigated their motility and biochemistry using in vitro assays. KIF3A/B moves microtubules at approximately 20% the speed of conventional kinesin. Individual KIF3A/B motors are able to support motility in the microtubule gliding assay, though the microtubule affinity is less than conventional kinesin. Hence, the design advantage of having two different motor domains appears to be neither the speed of movement nor the affinity for microtubules.

Original languageEnglish (US)
Pages (from-to)591-592
Number of pages2
JournalAnnual International Conference of the IEEE Engineering in Medicine and Biology - Proceedings
Volume1
StatePublished - 2002
EventProceedings of the 2002 IEEE Engineering in Medicine and Biology 24th Annual Conference and the 2002 Fall Meeting of the Biomedical Engineering Society (BMES / EMBS) - Houston, TX, United States
Duration: Oct 23 2002Oct 26 2002

All Science Journal Classification (ASJC) codes

  • Signal Processing
  • Health Informatics
  • Computer Vision and Pattern Recognition
  • Biomedical Engineering

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