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The kinesin KIF1C and microtubule plus ends regulate podosome dynamics in macrophages

Petra Kopp1, Reiner Lammers, Martin Aepfelbacher

  • 1Institut für Prophylaxe und Epidemiologie der Kreislaufkrankheiten, Ludwig-Maximilians-Universität, 80336 Munich, Germany.

Molecular Biology of the Cell
|March 24, 2006
PubMed

Insights

Microtubule plus ends regulate podosome turnover in human macrophages. The kinesin KIF1C motor protein binds myosin IIA, linking actin and tubulin cytoskeletons for podosome dynamics.

Area of Science:

  • Cell Biology
  • Cytoskeletal Dynamics
  • Molecular Motors

Background:

  • Podosomes are dynamic actin-rich structures crucial for monocytic cell migration and invasion.
  • The role of microtubules in regulating podosome turnover was previously unclear.
  • Understanding the molecular mechanisms linking microtubules and podosomes is essential.

Purpose of the Study:

  • To elucidate the molecular basis of microtubule-dependent podosome regulation.
  • To identify specific motor proteins involved in this process.
  • To investigate the interaction between the actin and tubulin cytoskeletons at podosomes.

Main Methods:

  • Utilized primary human macrophages.
  • Investigated microtubule plus end interactions with podosomes.
  • Identified and characterized the kinesin KIF1C motor protein.
  • Employed mutation constructs and gene silencing (siRNA/shRNA) for KIF1C depletion.
  • Performed protein interaction studies to identify binding partners.

Main Results:

  • Microtubule plus end contact influences podosome fate in macrophages.
  • Kinesin KIF1C, a Kinesin-3 family member, localizes to podosome turnover sites.
  • KIF1C depletion leads to reduced podosome dynamics and deficiency.
  • KIF1C directly binds to nonmuscle myosin IIA via its PTPD-binding domain.
  • This interaction establishes a link between actin and tubulin cytoskeletons.

Conclusions:

  • Kinesin KIF1C is a key regulator of podosome dynamics in human macrophages.
  • KIF1C mediates the interaction between microtubules and the actin cytoskeleton at podosomes.
  • This study reveals a novel function for KIF1C in human cells and implicates kinesins in podosome regulation.

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