Year: 2026
Type: article
Abstract: 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.
Source: Biological Chemistry
Authors: Luna Van Nimmen, Hanne Peeters, Shehab Ismail
Institution: KU Leuven
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid:
Funder: Fonds Wetenschappelijk Onderzoek
OpenAlex ID: W7155604263