Regulation of cAMP and cGMP signaling: New phosphodiesterases and new functions

Current Opinion in Cell Biology

Volumn 12, Issue 2, 2000, Pages 174-179

  Soderling, Scott H ^a   Beavo, Joseph A ^a  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTISENSE OLIGONUCLEOTIDE; CYCLIC AMP; CYCLIC GMP; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; INSULIN; PHOSPHODIESTERASE INHIBITOR; SILDENAFIL;

BODY GROWTH; ENZYME INHIBITION; ERECTILE DYSFUNCTION; FERTILITY; GENE DISRUPTION; GENE ISOLATION; HUMAN; INSULIN RELEASE; KNOCKOUT MOUSE; NONHUMAN; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION; T LYMPHOCYTE ACTIVATION;

EID: 0034009080     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)00073-3     Document Type: Review

References (41)

1. ••].
2. ••] identify and characterize a novel family of cAMP-binding guanine-nucleotide-exchange factors that activate the small G-protein Rap1.
3. •].
4. •] also identify the unique amino-terminal PAS that may bind other proteins and/or a small ligand.
5. Hayashi M., Matsushima K., Ohashi H., Tsunoda H., Murase S., Kawarada Y., Tanaka T. Molecular cloning and characterization of human PDE8B, a novel thyroid-specific isozyme of 3′,5′-cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 250:1998;751-756.
6. Fisher D.A., Smith J.F., Pillar J.S., St Denis S.H., Cheng J.B. Isolation and characterization of PDE9A, a novel human cGMP-specific phosphodiesterase. J Biol Chem. 273:1998;15559-15564. The gene sequence, structure and alternative splice variants of PDE9 are described.
7. •].
8. •].
9. •].
10. •].
11. •]. These studies demonstrate that PDE10 can hydrolyze both cAMP and cGMP, but may function as a cAMP-inhibited cGMP PDE. Additionally, PDE10 is shown to contain two amino-terminal GAF domains, which, in contrast to PDE2, PDE5 and PDE6, do not appear to have a high-affinity binding site for cGMP.
12. Linden H., Macino G. White collar 2, a partner in blue-light signal transduction, controlling expression of light-regulated genes in Neurospora crassa. EMBO J. 16:1997;98-109.
13. Huang Z.J., Edery I., Rosbash M. PAS is a dimerization domain common to Drosophila period and several transcription factors. Nature. 364:1993;259-262.
14. Gekakis N., Saez L., Delahaye-Brown A.M., Myers M.P., Sehgal A., Young M.W., Weitz C.J. Isolation of timeless by PER protein interaction: defective interaction between timeless protein and long-period mutant PERL. Science. 270:1995;811-815.
15. Fukunaga B.N., Probst M.R., Reisz-Porszasz S., Hankinson O. Identification of functional domains of the aryl hydrocarbon receptor. J Biol Chem. 270:1995;29270-29278.
16. Ni M., Tepperman J.M., Quail P.H. PIF3, a phytochrome-interacting factor necessary for normal photoinduced signal transduction, is a novel basic helix-loop-helix protein. Cell. 95:1998;657-667.
17. Gong W., Hao B., Mansy S.S., Gonzalez G., Gilles-Gonzalez M.A., Chan M.K. Structure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction. Proc Natl Acad Sci USA. 95:1998;15177-15182. This paper describes the crystal structure for the PAS domain of FixL, which is remarkably similar to that of PYP [18], with different ligands complexed within the 'palm' of the PAS 'hand'.
18. Borgstahl G.E., Williams D.R., Getzoff E.D. 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Biochemistry. 34:1995;6278-6287.
19. Pellequer J.L., Brudler R., Getzoff E.D. Biological sensors: more than one way to sense oxygen. Curr Biol. 9:1999;R416-R418. This paper reviews the structural features of the PAS domain. It contains an informative figure that aligns the structures of the FixL, PYP and HERG (human-ether-a-go-go potassium channel) PAS domains together to visually demonstrate that, in spite of limited sequence conservation, strong structural homology exists.
20. Aravind L., Ponting C.P. The GAF domain: an evolutionary link between diverse phototransducing proteins. Trends Biochem Sci. 22:1997;458-459.
21. Holz G.G., Habener J.F. Signal transduction crosstalk in the endocrine system: pancreatic beta- cells and the glucose competence concept. Trends Biochem Sci. 17:1992;388-393.
22. Zhao A.Z., Zhao H., Teague J., Fujimoto W., Beavo J.A. Attenuation of insulin secretion by insulin-like growth factor 1 is mediated through activation of phosphodiesterase 3B. Proc Natl Acad Sci USA. 94:1997;3223-3228.
23. Zhao A.Z., Bornfeldt K.E., Beavo J.A. Leptin inhibits insulin secretion by activation of phosphodiesterase 3B. J Clin Invest. 102:1998;869-873. This paper shows that both IGF-1 and leptin can reduce insulin secretion by activating PDE3B and thereby lowering cAMP levels. The authors also suggest that different cAMP pools regulated by localized PDEs regulate insulin secretion.
24. Lester L.B., Langeberg L.K., Scott J.D. Anchoring of protein kinase A facilitates hormone-mediated insulin secretion. Proc Natl Acad Sci USA. 94:1997;14942-14947.
25. Fraser I.D., Tavalin S.J., Lester L.B., Langeberg L.K., Westphal A.M., Dean R.A., Marrion N.V., Scott J.D. A novel lipid-anchored A-kinase Anchoring Protein facilitates cAMP-responsive membrane events. EMBO J. 17:1998;2261-2272.
26. Li L., Yee C., Beavo J.A. CD3- and CD28-dependent induction of PDE7 required for T cell activation. Science. 283:1999;848-851. This paper shows that PDE7A protein is upregulated by co-stimulation of T cells, and that this upregulation is likely to be a necessary requirement for the T-cell activation.
27. Jin S.L., Richard F.J., Kuo W., D'Ercole A.J., Conti M. Impaired growth and fertility of cAMP-specific phosphodiesterase PDE4D-deficient mice. Proc Natl Acad Sci USA. 96:1999;11998-12003. This study is the first publication of a PDE4 gene knockout in mouse. Although PDE4D is one of four similar cAMP PDEs (4A, 4B, 4C and 4D), these knockout mice do not appear to compensate for the loss of PDE4D by upregulation of other PDE4 members. Additionally, these mice show many interesting phenotypes including growth and fertility impairments.
28. Tsafriri A., Chun S.Y., Zhang R., Hsueh A.J.W., Conti M. Oocyte maturation involves compartmentalization and opposing changes of cAMP levels in follicular somatic and germ cells: studies using selective phosphodiesterase inhibitors. Dev Biol. 178:1996;393-402.
29. Zhou J., Kumar R., Matzuk M.M., Bondy C. Insulin-like growth factor 1 regulates gonadotropin responsiveness in the murine ovary. Mol Endocrinol. 11:1997;1924-1932.
30. Magoha G.A. Management of male erectile dysfunction: a review. East Afr Med J. 75:1998;623-627.
31. Chuang A.T., Strauss J.D., Murphy R.A., Steers W.D. Sildenafil, a type-5 CGMP phosphodiesterase inhibitor, specifically amplifies endogenous cGMP-dependent relaxation in rabbit corpus cavernosum smooth muscle in vitro. J Urol. 160:1998;257-261.
32. Moreland R.B., Goldstein I., Traish A. Sildenafil, a novel inhibitor of phosphodiesterase type 5 in human corpus cavernosum smooth muscle cells. Life Sci. 62:1998;309-318.
33. Ballard S.A., Gingell C.J., Tang K., Turner L.A., Price M.E., Naylor A.M. Effects of sildenafil on the relaxation of human corpus cavernosum tissue in vitro and on the activities of cyclic nucleotide phosphodiesterase isozymes. J Urol. 159:1998;2164-2171.
34. Carter A.J., Ballard S.A., Naylor A.M. Effect of the selective phosphodiesterase type 5 inhibitor sildenafil on erectile dysfunction in the anesthetized dog. J Urol. 160:1998;242-246. This paper demonstrates the effect of inhibiting PDE5 on penile erection. It suggests that PDE5 does not regulate basal cGMP, but rather cGMP in response to sexual stimulation.
35. O'Connell J.C., McCallum J.F., McPhee I., Wakefield J., Houslay E.S., Wishart W., Bolger G., Frame M., Houslay M.D. The SH3 domain of Src tyrosyl protein kinase interacts with the N- terminal splice region of the PDE4A cAMP-specific phosphodiesterase RPDE-6 (RNPDE4A5). Biochem J. 318:1996;255-261.
36. Yarwood S.J., Steele M.R., Scotland G., Houslay M.D., Bolger G.B. The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform. J Biol Chem. 274:1999;14909-14917. This paper, along with [35], demonstrates the specific interaction of PDE4 isozymes with cellular scaffolding proteins. These studies help to define the emerging theme in the PDE field that that spatially distinct targeting of PDEs is likely to be important for regulation of cellular function.
37. Marzesco A.M., Galli T., Louvard D., Zahraoui A. The rod cGMP phosphodiesterase delta subunit dissociates the small GTPase Rab13 from membranes. J Biol Chem. 273:1998;22340-22345. This study suggests that the function of the PDE6 delta subunit may not be limited to the solubilization of PDE6 in photoreceptors. It also suggests that the delta subunit may be targeted to subcellular compartments by a PDZ binding motif at the C-terminus.
38. Hoffmann R., Baillie G.S., MacKenzie S.J., Yarwood S.J., Houslay M.D. The MAP kinase ERK2 inhibits the cyclic AMP-specific phosphodiesterase HSPDE4D3 by phosphorylating it at Ser579. EMBO J. 18:1999;893-903. The authors demonstrate that PDE4D3 can be regulated by ERK2. This in turn suggests that the MAP kinase and cAMP signaling systems may crosstalk at the level of PDE4.
39. Korschen H.G., Beyermann M., Muller F., Heck M., Vanller M., Koch K.W., Kellner R., Wolfrum U., Bode C., Hofmann K.P., Kaupp U.B. Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors. Nature. 400:1999;761-766. This paper shows that glutamic-acid-rich proteins (GARPs) may bind to PDE6 in photoreceptors. GARP is shown to have a distinct subcellular localization and therefore may serve to regulate the localization of PDE6 within the photoreceptor membrane.
40. Morais J.H., Lee A., Cohen S.L., Chait B.T., Li M., Mackinnon R. Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain. Cell. 95:1998;649-655. The crystal structure of the amino-terminal HERG PAS domain, which probably regulates the gating properties of this potassium channel by an intra-molecular protein interaction, is presented. This structure is similar to the structures of the PAS domains of PYP and FixL. Additionally, mutagenesis suggests the HERG PAS domain can bind to other regions of the potassium channel by a hydrophobic patch located on the surface of the antiparallel β sheets. An analogous hydrophobic patch is found on the PDE8A PAS domain structure model (see Figure 2), suggesting that this may be a common protein interaction region.
41. Fawcett L., Baxendale R., Stacey P., McGrouther C., Harrow I., Soderling S.A., Helman J., Beavo J.A., Phillips S.C. Molecular cloning and characterization of a novel human phosphodiesterase gene family: PDE11A. Proc Natl Acad Sci USA. 2000;. in press. This isozyme hydrolyzes both cAMP and cGMP and contains a GAF domain. Little is known yet about its regulation.