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KIF14 binds tightly to microtubules and adopts a rigor-like conformation

Kritica Arora1, Lama Talje2, Ana B Asenjo3

  • 1Department of Biomedical and Molecular Sciences, Queen's University, 18 Stuart St., Rm. 652, Kingston, ON K7L 3 N6, Canada.

Journal of Molecular Biology
|June 21, 2014
PubMed

Insights

KIF14, a motor protein crucial for cell division, binds microtubules tightly without typical nucleotide changes. Its unique structure suggests a role in stabilizing essential structures during cytokinesis.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • KIF14 is a mitotic kinesin motor protein vital for cytokinesis and implicated in development and cancer.
  • Understanding KIF14's motor function is key to its roles in cell division and disease.

Purpose of the Study:

  • To investigate the biophysical and structural properties of the mouse KIF14 motor domain.
  • To elucidate the mechanism of KIF14 interaction with microtubules.

Main Methods:

  • Biochemical assays to measure ATPase activity and microtubule binding affinity.
  • X-ray crystallography to determine the structure of the KIF14 motor domain.
  • Cryo-electron microscopy to analyze the KIF14-microtubule complex.

Main Results:

  • Mouse KIF14 motor domain exhibits strong microtubule binding independent of nucleotide state.
  • KIF14 possesses robust ATPase activity but displays very slow motility.
  • Crystal structure reveals an open ATP-binding pocket and a twisted central β-sheet, resembling a rigor-like state.
  • Distinct KIF14-microtubule binding configuration observed via cryo-EM.

Conclusions:

  • KIF14's unique motor properties, including its rigor-like state and distinct microtubule binding, are adapted for stabilizing midbody microtubules.
  • These findings provide insights into KIF14's essential function in cytokinesis and its potential as a therapeutic target.
Keywords:
KIF14crystal structurekinesinmicrotubulesmotor protein

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