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Nonelectrostatic contributions to the binding of MARCKS-related protein to lipid bilayers

J J Ramsden1, G Vergères

  • 1Biozentrum, University of Basel, Klingelbergstrasse 70, Basel, 4056, Switzerland.

Archives of Biochemistry and Biophysics
|November 5, 1999
PubMed

Insights

The myristoyl moiety is crucial for MARCKS-related protein (MRP) binding to cell membranes. However, hydrophobic interactions within the effector domain also significantly contribute to MRP

Area of Science:

  • Biochemistry
  • Cell Biology
  • Membrane Biophysics

Background:

  • MARCKS-related protein (MRP) plays a role in cellular processes.
  • Understanding MRP's membrane interaction is key to its function.
  • Specific domains of MRP mediate its association with lipid bilayers.

Purpose of the Study:

  • To investigate the role of the myristoyl moiety and effector domain (ED) in MRP's membrane binding.
  • To elucidate the contributions of hydrophobic and electrostatic interactions to MRP-membrane association.
  • To characterize MRP binding to both neutral and acidic phospholipid bilayers.

Main Methods:

  • Utilized two-mode optical waveguide spectroscopy to monitor protein-membrane interactions.
  • Studied various MRP constructs lacking the myristoyl moiety, the ED, or both.
  • Examined binding to supported planar phospholipid bilayer membranes of varying charge.

Main Results:

  • The myristoyl moiety is important for MRP binding to both neutral and acidic membranes.
  • Unmyristoylated MRP shows significant binding to neutral membranes, mediated by hydrophobic interactions in the ED.
  • Complete removal of the myristoyl moiety and ED abolishes binding to acidic membranes but leaves minimal binding to neutral membranes.

Conclusions:

  • Hydrophobic interactions, independent of the myristoyl moiety, are critical for MRP association with membranes.
  • The effector domain's hydrophobic residues are primarily responsible for binding unmyristoylated MRP to neutral membranes.
  • Electrostatic repulsion counteracts residual binding when both myristoyl and ED are absent, especially with acidic membranes.

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