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

Identification of novel PDEδ interacting proteins.

Author information

1
Department of Chemical Biology, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Straße 11, 44227 Dortmund, Germany; Lehrbereich Chemische Biologie, Fakultät Chemie, Technische Universität Dortmund, Otto-Hahn-Straße 6, 44227 Dortmund, Germany.
2
Department of Chemical Biology, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Straße 11, 44227 Dortmund, Germany.
3
Department of Chemical Biology, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Straße 11, 44227 Dortmund, Germany; Lehrbereich Chemische Biologie, Fakultät Chemie, Technische Universität Dortmund, Otto-Hahn-Straße 6, 44227 Dortmund, Germany. Electronic address: herbert.waldmann@mpi-dortmund.mpg.de.
4
Department of Chemical Biology, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Straße 11, 44227 Dortmund, Germany. Electronic address: slava.ziegler@mpi-dortmund.mpg.de.

Abstract

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

PMID:
28935183
DOI:
10.1016/j.bmc.2017.08.033
[Indexed for MEDLINE]

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