Isoprenylation of Monomeric GTPases in Human Trabecular Meshwork Cells

Methods Mol Biol. 2017:1609:217-229. doi: 10.1007/978-1-4939-6996-8_18.

Abstract

Small monomeric GTPases, including those belonging to the Rho family, regulate a diverse array of intracellular signaling pathways which affect vesicle transport/trafficking, endocytosis, cell cycle progression, cell contractility, and formation of stress fibers or focal adhesions. Functional activation of newly synthesized small monomeric GTPases is facilitated by a multistep post-translational process involving transferase-catalyzed addition of farnesyl or geranylgeranyl isoprenoids to conserved cysteine residues within a unique carboxy terminal CaaX motif. Here, using well-established and widely available contemporary methodologies, detailed protocols by which to semi-quantitatively evaluate the functional consequence of post-translational isoprenylation in human trabecular meshwork cells are described. We introduce the concept that isoprenylation alone is itself a key regulator of mammalian Rho GTPase expression and turnover.

Keywords: Farnesyl; Geranylgeranyl; Human; Monomeric GTPase; Trabecular meshwork.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, Non-U.S. Gov't
  • Research Support, N.I.H., Extramural

MeSH terms

  • Cells, Cultured
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Immunoblotting
  • Protein Prenylation
  • Trabecular Meshwork / cytology*
  • rho GTP-Binding Proteins / chemistry*
  • rho GTP-Binding Proteins / metabolism*

Substances

  • rho GTP-Binding Proteins