Chemical-biological exploration of the limits of the Ras de- and repalmitoylating machinery

Chembiochem. 2012 May 7;13(7):1017-23. doi: 10.1002/cbic.201200078. Epub 2012 Apr 5.

Abstract

A dynamic de-/repalmitoylation cycle determines localization and activity of H- and N-Ras. This combined cellular de- and repalmitoylation machinery has been shown to be substrate tolerant--it accepts variation of amino acid sequence, structure and configuration. Here, semisynthetic Ras-proteins in which the C-terminal amino acids are replaced by peptoid residues are used to reveal the first limitations of substrate recognition by the de- and repalmitoylating machinery.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Dogs
  • Lipopeptides / chemistry*
  • Lipoylation*
  • Lysophospholipase / chemistry
  • Lysophospholipase / metabolism
  • Microscopy, Confocal
  • Molecular Sequence Data
  • Signal Transduction
  • Transfection
  • ras Proteins / chemistry*
  • ras Proteins / metabolism*

Substances

  • Lipopeptides
  • Lysophospholipase
  • ras Proteins