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Dynamic interactions between microtubules and artificial membranes.

J M Caron1, R D Berlin

  • 1Department of Physiology, University of Connecticut Health Center, Farmington 06032.

Biochemistry
|June 16, 1987
PubMed
Summary

Microtubule protein readily adsorbs to liposomes above their transition temperature. This adsorbed tubulin can reassemble into microtubules on neutral vesicles, but not on acidic ones.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Biophysics

Background:

  • Microtubules are crucial cytoskeletal components involved in cell division and intracellular transport.
  • Tubulin, the protein subunit of microtubules, undergoes dynamic assembly and disassembly.
  • Liposomes, artificial vesicles, are used as model systems to study protein-lipid interactions.

Purpose of the Study:

  • To investigate the adsorption of microtubule protein to liposomes.
  • To determine the conditions affecting tubulin adsorption and subsequent microtubule assembly.
  • To explore the influence of liposome charge on tubulin-lipid interactions.

Main Methods:

  • Liposome preparation using phosphatidylcholine (neutral) and phosphatidylserine (acidic).
  • Incubation of microtubule protein with liposomes above the phospholipid transition temperature.
  • Assessment of tubulin adsorption onto liposomes.
  • Induction of microtubule assembly by altering buffer conditions.
  • Effect of colchicine preincubation on tubulin adsorption.

Main Results:

  • Extensive adsorption of microtubule protein to liposomes occurred above the phospholipid bilayer transition temperature.
  • Adsorption occurred on both neutral phosphatidylcholine (PC) and acidic phosphatidylserine (PS) vesicles.
  • Preincubation with colchicine did not affect microtubule protein adsorption.
  • 51-63% of tubulin adsorbed onto neutral PC vesicles could be desorbed to form microtubules.
  • No microtubule assembly occurred with microtubule protein preadsorbed onto acidic PS vesicles, indicating irreversible binding.

Conclusions:

  • Microtubule protein adsorption to liposomes is dependent on temperature and vesicle charge.
  • Neutral liposomes can serve as a platform for reversible tubulin adsorption and subsequent microtubule assembly.
  • Acidic liposomes promote irreversible binding of microtubule protein, preventing assembly.
  • These findings offer insights into the regulation of microtubule dynamics at membrane interfaces.

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