Identification of novel PDEδ interacting proteins

Bioorg Med Chem. 2018 May 1;26(8):1426-1434. doi: 10.1016/j.bmc.2017.08.033. Epub 2017 Aug 31.


Prenylation is a post-translational modification that increases the affinity of proteins for membranes and mediates protein-protein interactions. The retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta (PDEδ) is a prenyl binding protein that is essential for the shuttling of small GTPases between different membrane compartments and, thus, for their proper functioning. Although the prenylome comprises up to 2% of the mammalian proteome, only few prenylated proteins are known to interact with PDEδ. A proteome-wide approach was employed to map the PDEδ interactome among the prenylome and revealed RAB23, CDC42 and CNP as novel PDEδ interacting proteins. Moreover, PDEδ associates with the lamin A mutant progerin in a prenyl-dependent manner. These findings shed new light on the role of PDEδ in binding (and regulating) prenylated proteins in cells.

Keywords: Inhibitor; PDEδ; Prenylation; Protein-protein interactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism*
  • Cells, Cultured
  • Cyclic Nucleotide Phosphodiesterases, Type 6 / chemistry
  • Cyclic Nucleotide Phosphodiesterases, Type 6 / metabolism*
  • Dose-Response Relationship, Drug
  • Humans
  • Molecular Structure
  • Protein Binding
  • Structure-Activity Relationship


  • Carrier Proteins
  • Cyclic Nucleotide Phosphodiesterases, Type 6