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Related Experiment Videos

Individual phosphoinositide 3-kinase C2alpha domain activities independently regulate clathrin function.

Ibragim Gaidarov1, Yanqiu Zhao, James H Keen

  • 1Department of Biochemistry and Molecular Biology and the Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.

The Journal of Biological Chemistry
|October 11, 2005
PubMed
Summary

Phosphoinositide 3-kinase C2alpha (PI3K-C2alpha) binds clathrin, affecting its distribution and function. This protein impacts clathrin-mediated transport and membrane budding through protein interactions and lipid kinase activity.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Class II phosphoinositide 3-kinases (PI3K) have unclear cellular roles.
  • PI3K-C2alpha localizes to clathrin-coated membranes in the trans-Golgi network and plasma membrane.
  • Clathrin binding to PI3K-C2alpha activates its lipid kinase activity.

Purpose of the Study:

  • Investigate the role of PI3K-C2alpha in clathrin dynamics.
  • Determine how PI3K-C2alpha affects clathrin-mediated transport.
  • Elucidate the mechanisms by which PI3K-C2alpha modulates clathrin function.

Main Methods:

  • Expression of PI3K-C2alpha and its clathrin binding domain in cells.
  • Ultrastructural visualization of clathrin-coated structures.
  • Analysis of clathrin-mediated transport from the plasma membrane and trans-Golgi network.

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Main Results:

  • PI3K-C2alpha expression alters clathrin distribution and function.
  • Intracellular accumulation of clathrin-coated structures and inhibited transport were observed.
  • The isolated clathrin binding domain of PI3K-C2alpha can drive clathrin lattice assembly.
  • Both protein-protein interaction and lipid kinase activity independently modulate clathrin.

Conclusions:

  • PI3K-C2alpha influences clathrin dynamics through protein-protein interactions and lipid production.
  • The protein affects clathrin at sites of membrane budding and targeting.
  • PI3K-C2alpha plays a significant role in regulating clathrin-mediated cellular processes.