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Myristoylation cannot functionally replace the isoprenylation of Rab5

G Li1, M A Barbieri, P D Stahl

  • 1Department of Cell Biology & Physiology, Washington University School of Medicine, St. Louis, Missouri 63110.

Archives of Biochemistry and Biophysics
|January 10, 1995
PubMed
Summary

N-terminal myristoylation cannot replace C-terminal isoprenylation for the small GTPase Rab5 to function in endocytosis. Myristoylation of Rab5 actually interferes with its normal biological activity and membrane association.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • C-terminal isoprenylation is crucial for small GTPase Rab5 membrane association and endocytosis regulation.
  • The role of alternative lipid modifications in Rab5 function remains unclear.

Purpose of the Study:

  • To investigate if N-terminal myristoylation can substitute for C-terminal isoprenylation in Rab5.
  • To assess the impact of myristoylation on Rab5 membrane binding and biological activity.

Main Methods:

  • Construction and expression of Rab5 mutants with varying lipid modifications (isoprenylation, myristoylation, or neither) using a Sindbis virus vector in BHK-21 cells.
  • Analysis of Rab5 mutant membrane association via lipid modification.
  • Assessment of biological activity, specifically the stimulation of endocytosis.

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Main Results:

  • Wild-type Rab5, isoprenylated and membrane-associated, was biologically active in endocytosis.
  • Rab5 with both isoprenylation and myristoylation showed increased membrane affinity but reduced activity.
  • Rab5 lacking lipid modifications was not membrane-associated or active.
  • Myristoylation alone significantly increased membrane association but did not restore Rab5 activity.

Conclusions:

  • N-terminal myristoylation cannot functionally replace C-terminal isoprenylation for Rab5.
  • Myristoylation of Rab5 can interfere with its normal function and membrane association.
  • Specific lipid modifications are essential for Rab5's role in endocytosis.