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PDC  -  phosducin

Bos taurus

Synonyms: PHD, RPR1
 
 
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Disease relevance of PDC

 

High impact information on PDC

  • This protein is very similar or identical to phosducin, a protein previously thought to be specific for retina and pineal gland [6].
  • These results suggest that Ca2+ can regulate the light response at the level of Gt activation through its effect on the phosphorylation state of Pd [7].
  • In visual signal transduction, unphosphorylated Pd blocks the interaction of light-activated rhodopsin with its G protein (Gt) by binding to the beta gamma subunits of Gt and preventing their association with the Gt alpha subunit [7].
  • The phosphoprotein phosducin (Pd) regulates many guanine nucleotide binding protein (G protein)-linked signaling pathways [7].
  • In this study, we show widespread tissue distribution of phosducin by the amplification of its cDNA and the detection of two different transcripts in Northern analyses in liver, lung, heart, brain, and retina [8].
 

Biological context of PDC

  • Phosphorylation of phosducin by Ca(2+)/calmodulin-dependent protein kinase II, which inhibits phosducin-Tbetagamma complex formation, completely restored Tbetagamma ubiquitylation and degradation [9].
  • Importantly, G beta gamma binding to Pdc was enhanced by Ca(2+) chelation and the binding kinetics closely paralleled those of Ser-54 dephosphorylation, indicating that Ser-54 phosphorylation controls G(t)beta gamma binding in vivo [10].
  • Phosducin (Pdc) is a G protein beta gamma dimer (G beta gamma) binding protein, highly expressed in retinal photoreceptor and pineal cells, yet whose physiological role remains elusive [10].
  • To directly examine the phosphorylation of Pdc in intact retina, we prepared antibodies specific to the three principal phosphorylation sites (Ser-54, Ser-73, and Ser-106) and measured the kinetics of phosphorylation/dephosphorylation during light/dark adaptation and the subsequent effects on G(t)beta gamma binding [10].
  • Sequence analysis of a cDNA clone for bovine retinal phosducin confirmed that the MEKA clone deviation resulted from an unidentified cDNA guanosine nucleotide, a shifted reading frame and a premature stop codon [11].
 

Anatomical context of PDC

  • Amino acid and cDNA sequence of bovine phosducin, a soluble phosphoprotein from photoreceptor cells [11].
  • Vertebrate photoreceptor cells contain a soluble phosphoprotein, phosducin, which complexes with the beta, gamma subunits of the GTP-binding protein, transducin [11].
  • Sensitization of SJL/J mice with non-self-PDC has been shown to result in induction of autoreactive T-cell responses to PDC sharing characteristics with those seen in patients with PBC [12].
  • METHODS: Serum and saliva from 12 patients with PBC were tested for AMA by immunoblotting on bovine heart mitochondria, and by an automated microassay based on inhibition of the enzymatic activity of PDC [13].
  • Thus, factors that determine the phosphorylation state of Pd in rod outer segments are important in controlling the number of Gts available for activation by rhodopsin [7].
 

Associations of PDC with chemical compounds

 

Regulatory relationships of PDC

 

Analytical, diagnostic and therapeutic context of PDC

  • In vitro, phosducin is phosphorylated by either exogenous or endogenous protein kinase A. 32P-Labeled rat retina phosducin was isolated by immunoprecipitation either after phosphorylation by protein kinase A in the presence of [gamma-32P]ATP or after incubation of retinas in darkness with 32Pi [14].
  • By the Western blot analysis anti-MEKA protein serum reacted with a soluble 32 kDa protein from bovine retina and 33 kDa for chick, but not with proteins from other tissues [1].
  • Thus, according to whether preparations of PDC are boiled or not, two conformationally alternative forms of the PDC-E2 protein can be revealed by immunoblotting [17].
  • Furthermore, direct measurements of interaction between G beta gamma and fragments of phosducin, using surface plasmon resonance technology, confirmed the assignment of binding activity to the 63-amino acid fragment and the importance of the tryptophan residue [18].
  • Neither Phd nor PhLOP1 affected CRX binding to its consensus DNA element in electrophoretic mobility shift assays [19].

References

  1. Isolation of a novel retina-specific clone (MEKA cDNA) encoding a photoreceptor soluble protein. Kuo, C.H., Akiyama, M., Miki, N. Brain Res. Mol. Brain Res. (1989) [Pubmed]
  2. Immunoreactivity of antimitochondrial autoantibodies in Japanese patients with primary biliary cirrhosis. Omagari, K., Rowley, M.J., Jois, J.A., Feeney, S.J., Komatsu, K., Maeda, T., Onishi, S., Yamazaki, K., Suzuki, K., Galperin, C., Mackay, I.R. J. Gastroenterol. (1996) [Pubmed]
  3. Carnitine palmitoyltransferase I in liver of periparturient dairy cows: effects of prepartum intake, postpartum induction of ketosis, and periparturient disorders. Dann, H.M., Drackley, J.K. J. Dairy Sci. (2005) [Pubmed]
  4. Effect of oxythiamine on adrenal thiamine pyrophosphate-dependent enzyme activities. Strumilo, S.A., Senkevich, S.B., Vinogradov, V.V. Biomed. Biochim. Acta (1984) [Pubmed]
  5. Rethinking the role of phosducin: light-regulated binding of phosducin to 14-3-3 in rod inner segments. Nakano, K., Chen, J., Tarr, G.E., Yoshida, T., Flynn, J.M., Bitensky, M.W. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  6. Phosducin is a protein kinase A-regulated G-protein regulator. Bauer, P.H., Müller, S., Puzicha, M., Pippig, S., Obermaier, B., Helmreich, E.J., Lohse, M.J. Nature (1992) [Pubmed]
  7. Regulation of phosducin phosphorylation in retinal rods by Ca2+/calmodulin-dependent adenylyl cyclase. Willardson, B.M., Wilkins, J.F., Yoshida, T., Bitensky, M.W. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  8. Phosducin is a ubiquitous G-protein regulator. Danner, S., Lohse, M.J. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  9. Ubiquitylation of the transducin betagamma subunit complex. Regulation by phosducin. Obin, M., Lee, B.Y., Meinke, G., Bohm, A., Lee, R.H., Gaudet, R., Hopp, J.A., Arshavsky, V.Y., Willardson, B.M., Taylor, A. J. Biol. Chem. (2002) [Pubmed]
  10. Site-specific phosphorylation of phosducin in intact retina. Dynamics of phosphorylation and effects on G protein beta gamma dimer binding. Lee, B.Y., Thulin, C.D., Willardson, B.M. J. Biol. Chem. (2004) [Pubmed]
  11. Amino acid and cDNA sequence of bovine phosducin, a soluble phosphoprotein from photoreceptor cells. Lee, R.H., Fowler, A., McGinnis, J.F., Lolley, R.N., Craft, C.M. J. Biol. Chem. (1990) [Pubmed]
  12. Bacterial motif DNA as an adjuvant for the breakdown of immune self-tolerance to pyruvate dehydrogenase complex. Jones, D.E., Palmer, J.M., Burt, A.D., Walker, C., Robe, A.J., Kirby, J.A. Hepatology (2002) [Pubmed]
  13. Antimitochondrial autoantibodies in saliva and sera from patients with primary biliary cirrhosis. Ikuno, N., Mackay, I.R., Jois, J., Omagari, K., Rowley, M.J. J. Gastroenterol. Hepatol. (2001) [Pubmed]
  14. Protein kinase A phosphorylates retinal phosducin on serine 73 in situ. Lee, R.H., Brown, B.M., Lolley, R.N. J. Biol. Chem. (1990) [Pubmed]
  15. Immunology, biosynthesis and in vivo assembly of the branched-chain 2-oxoacid dehydrogenase complex from bovine kidney. Clarkson, G.H., Lindsay, J.G. Eur. J. Biochem. (1991) [Pubmed]
  16. The phosphorylation state of phosducin determines its ability to block transducin subunit interactions and inhibit transducin binding to activated rhodopsin. Yoshida, T., Willardson, B.M., Wilkins, J.F., Jensen, G.J., Thornton, B.D., Bitensky, M.W. J. Biol. Chem. (1994) [Pubmed]
  17. Antibody to two forms of dihydrolipoamide acetyltransferase (PDC-E2) in primary biliary cirrhosis. Chen, Q.Y., Rowley, M.J., Mackay, I.R. Liver (1993) [Pubmed]
  18. The N terminus of phosducin is involved in binding of beta gamma subunits of G protein. Xu, J., Wu, D., Slepak, V.Z., Simon, M.I. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  19. Modulation of CRX transactivation activity by phosducin isoforms. Zhu, X., Craft, C.M. Mol. Cell. Biol. (2000) [Pubmed]
 
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