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Related Experiment Videos

Kinesin's second step.

Lisa M Klumpp1, Andreas Hoenger, Susan P Gilbert

  • 1Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.

Proceedings of the National Academy of Sciences of the United States of America
|February 27, 2004
PubMed
Summary
This summary is machine-generated.

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Researchers identified kinesin mutants that stall on microtubules. Phosphate release from the rear head signals the front head to bind ATP, enabling continued movement and revealing a conserved motor control mechanism.

Area of Science:

  • Molecular motor function
  • Cellular transport mechanisms
  • Biochemistry of kinesin

Background:

  • Processive motors like kinesin move along microtubules by hydrolyzing ATP.
  • Understanding the regulation of ATP binding and hydrolysis is crucial for motor function.

Purpose of the Study:

  • To identify the regulatory signal for ATP binding in kinesin's forward head.
  • To elucidate the mechanism enabling continued processive movement.

Main Methods:

  • Utilized dimeric kinesin mutants that stall after one ATP turnover.
  • Analyzed the sequence of events leading to ATP binding in the forward head.

Main Results:

  • Phosphate release from the rearward head precedes detachment.

Related Experiment Videos

  • Detachment of the rearward head triggers ATP binding site accessibility in the forward head.

    • Conclusions:

    • The rearward head's behavior regulates the forward head's activity.
    • This regulatory mechanism may be conserved across different processive motor proteins.