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Kar3 interaction with Cik1 alters motor structure and function.

Hsiao Mei Annie Chu1, Mikyung Yun, David E Anderson

  • 1Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA.

The EMBO Journal
|August 19, 2005
PubMed
Summary
This summary is machine-generated.

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Kar3, a kinesin motor protein, forms dimers with Cik1, a nonmotor protein. This dimerization enhances Kar3

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biophysics

Background:

  • Kar3 (kinesin-14 motor) and Cik1 (nonmotor protein) in Saccharomyces cerevisiae are crucial for mitosis and karyogamy.
  • Previous studies suggested Kar3 and Cik1 interaction via Kar3's coiled coil, but in vivo homodimers were unobserved.

Purpose of the Study:

  • To investigate the in vitro dimerization of Kar3 with Cik1.
  • To elucidate the structural changes and functional consequences of Kar3-Cik1 complex formation.

Main Methods:

  • Analytical ultracentrifugation to determine Kar3 dimerization in vitro.
  • Rotary-shadow electron microscopy (EM) to visualize motor domain structure.
  • Circular dichroism (CD) spectroscopy to analyze helical structure of nonmotor regions.

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Main Results:

  • Kar3 forms dimers in vitro, with motor domains appearing as paired particles.
  • The Kar3/Cik1 nonmotor region exhibits increased helicity and a distinct stalk structure compared to Kar3 alone.
  • The Kar3/Cik1 complex moves 2-5 times faster on microtubules than Kar3 alone, destabilizing lagging ends.

Conclusions:

  • Dimerization with Cik1 induces significant structural changes in Kar3.
  • These structural alterations modulate Kar3 motor velocity and microtubule destabilization activity.
  • The Kar3/Cik1 association likely regulates Kar3 function in vivo during mitosis and karyogamy.