Related Experiment Video
Updated: Apr 27, 2026

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein
Published on: January 16, 2020
The role of PDE6D in trafficking KRAS
Luna Van Nimmen1, Hanne Peeters1, Shehab Ismail1
1Department of Chemistry, Biochemistry, Molecular and Structural Biology Division, The Mechanistic Molecular Biochemistry Group, KU Leuven, 3001 Heverlee, Belgium.
None:
Lipid-modified membrane-associated proteins can bind reversibly to cellular membranes, and their steady-state localization reflects a balance between membrane-bound and cytosolic pools. For many small GTPases of the Rho and Rab families, this balance is regulated by GDP dissociation inhibitors (GDIs), which control membrane association by shielding the prenyl group and coupling localization to the nucleotide state. In contrast, Ras proteins were long thought to lack a comparable regulatory system. The prenyl-binding protein PDE6D has emerged as a GDI-like factor for prenylated Ras proteins. Here, we discuss the role of PDE6D in KRAS trafficking and spatial organization, and examine its potential as a target for pharmacological inhibition of oncogenic KRAS signaling.
Related Concept Videos
Small GTPases - Ras and Rho
Three regulatory proteins control their activity:
The Ras Gene
Ras is a...
Amplifying Signals via Enzymatic Cascade
MAPK Signaling Cascades
GPCR Desensitization
PI3K/mTOR/AKT Signaling Pathway

