Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta

Definition:

Promotes the release of prenylated target proteins from cellular membranes. Modulates the activity of prenylated or palmitoylated Ras family members by regulating their subcellular location. Required for normal ciliary targeting of farnesylated target proteins, such as INPP5E. Modulates the subcellular location of target proteins by acting as a GTP specific dissociation inhibitor (GDI) (By similarity). Increases the affinity of ARL3 for GTP by several orders of magnitude. Stabilizes ARL3-GTP by decreasing the nucleotide dissociation rate (By similarity).

References:

[1]. Shehab A Ismail, et al. Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo. Nat Chem Biol. 2011 Oct 16;7(12):942-9. [Content Brief]

[2]. Gunther Zimmermann, et al. Small molecule inhibition of the KRAS-PDEδ interaction impairs oncogenic KRAS signalling. Nature. 2013 May 30;497(7451):638-42. [Content Brief]

[3]. Denise Wätzlich, et al. The interplay between RPGR, PDEδ and Arl2/3 regulate the ciliary targeting of farnesylated cargo. EMBO Rep. 2013 May;14(5):465-72. [Content Brief]

[4]. A M Marzesco, et al. The rod cGMP phosphodiesterase delta subunit dissociates the small GTPase Rab13 from membranes. J Biol Chem. 1998 Aug 28;273(35):22340-5. [Content Brief]

[5]. Sophie Thomas, et al. A homozygous PDE6D mutation in Joubert syndrome impairs targeting of farnesylated INPP5E protein to the primary cilium. Hum Mutat. 2014 Jan;35(1):137-46. [Content Brief]

[6]. M Linari, et al. The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner. FEBS Lett. 1999 Sep 10;458(1):55-9. [Content Brief]

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