cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A

Definition:

Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate. May play a critical role in regulating cAMP and cGMP levels in the striatum, a region of the brain that contributes to the control of movement and cognition.

References:

[1]. Huanchen Wang, et al. Structural insight into substrate specificity of phosphodiesterase 10. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5782-7. [Content Brief]

[2]. K Loughney, et al. Isolation and characterization of PDE10A, a novel human 3', 5'-cyclic nucleotide phosphodiesterase. Gene. 1999 Jun 24;234(1):109-17. [Content Brief]

[3]. Niccolò E Mencacci, et al. De Novo Mutations in PDE10A Cause Childhood-Onset Chorea with Bilateral Striatal Lesions. Am J Hum Genet. 2016 Apr 7;98(4):763-71. [Content Brief]

[4]. K Fujishige, et al. Cloning and characterization of a novel human phosphodiesterase that hydrolyzes both cAMP and cGMP (PDE10A). J Biol Chem. 1999 Jun 25;274(26):18438-45. [Content Brief]

[5]. Marco Gross-Langenhoff, et al. cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11. J Biol Chem. 2006 Feb 3;281(5):2841-6. [Content Brief]

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