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Gene Review

ywhab-a  -  tyrosine 3-monooxygenase/tryptophan 5...

Xenopus laevis

 
 
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Disease relevance of Ywhab

  • Here we report the crystal structures of the zeta isoform of 14-3-3 in complex with two peptide ligands: a Raf-derived phosphopeptide (pS-Raf-259, LSQRQRSTpSTPNVHMV) and an unphosphorylated peptide derived from phage display (R18, PHCVPRDLSWLDLEANMCLP) that inhibits binding of exoenzyme S and Raf-1 [1].
  • The holoenzyme contains the catalytic subunit Hat1, the retinoblastoma associated protein RbAp48, and members of the phosphoserine binding family of 14-3-3 proteins [2].
 

High impact information on Ywhab

  • We show here that DNA-responsive checkpoints also activate PP2A/B56delta phosphatase complexes to dephosphorylate Cdc25 at a site distinct from Ser287 (T138), the phosphorylation of which is required for 14-3-3 release [3].
  • These observations identify PP2A/B56delta as a central checkpoint effector and suggest a mechanism for controlling 14-3-3 interactions to promote mitosis [3].
  • Our data suggest that creation of a 14-3-3 "sink," consisting of phosphorylated 14-3-3 binding intermediate filament proteins, including keratins, coupled with reduced Cdc25-14-3-3 affinity, contribute to Cdc25 activation [3].
  • Role for the PP2A/B56delta Phosphatase in Regulating 14-3-3 Release from Cdc25 to Control Mitosis [3].
  • Expression of 14-3-3 proteins in Xenopus oocytes enhanced Raf-1 activity and promoted Raf-1-dependent oocyte maturation [4].
 

Biological context of Ywhab

  • Our analyses identify two aPKC phosphorylation sites in xPar-1, which are essential for 14-3-3 binding and for proper gastrulation movements [5].
  • Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25 [6].
  • Negative regulation of the Cdc25C protein phosphatase by phosphorylation on Ser 216, the 14-3-3-binding site, is an important regulatory mechanism used by cells to block mitotic entry under normal conditions and after DNA damage [7].
  • PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation [8].
  • Fusicoccin signaling reveals 14-3-3 protein function as a novel step in left-right patterning during amphibian embryogenesis [9].
 

Anatomical context of Ywhab

  • The aPKC phosphorylation-dependent binding of xPar-1 to 14-3-3 does not markedly affect the kinase activity of xPar-1, but induces relocation of xPar-1 from the plasma membranes to the cytoplasm [5].
  • Similarly, the full-length B-Raf 14-3-3 binding mutant inhibited nerve growth factor-stimulated PC12 cell differentiation [10].
  • Together, these results provide conclusive evidence that protein 14-3-3 is present in mature spermatozoa and that PP1gamma2 is one of its binding partners [11].
 

Associations of Ywhab with chemical compounds

  • Here we show that two members of Par proteins, 14-3-3 (Par-5) and atypical PKC (aPKC), regulate the serine/threonine kinase Par-1 to control Xenopus gastrulation [5].
  • Here we report that Cdc25 in the G2-arrested oocyte is bound to 14-3-3 proteins and that progesterone treatment abrogates this binding [12].
  • Three candidate proteins found in the mammalian pineal, protein 14-3-3, malate dehydrogenase, and recoverin, do not comigrate with p30 [13].
  • A number of Raf-associated proteins have recently been identified, including members of the 14-3-3 family of phosphoserine-binding proteins [10].
  • 14-3-3 protein is known to activate tyrosine and tryptophan hydroxylases, to modulate the protein kinase C activity, to stimulate secretion, and to show phospholipase A2 activity per se [14].
 

Other interactions of Ywhab

 

Analytical, diagnostic and therapeutic context of Ywhab

References

  1. 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. Petosa, C., Masters, S.C., Bankston, L.A., Pohl, J., Wang, B., Fu, H., Liddington, R.C. J. Biol. Chem. (1998) [Pubmed]
  2. Purification and properties of the Xenopus Hat1 acetyltransferase: association with the 14-3-3 proteins in the oocyte nucleus. Imhof, A., Wolffe, A.P. Biochemistry (1999) [Pubmed]
  3. Role for the PP2A/B56delta Phosphatase in Regulating 14-3-3 Release from Cdc25 to Control Mitosis. Margolis, S.S., Perry, J.A., Forester, C.M., Nutt, L.K., Guo, Y., Jardim, M.J., Thomenius, M.J., Freel, C.D., Darbandi, R., Ahn, J.H., Arroyo, J.D., Wang, X.F., Shenolikar, S., Nairn, A.C., Dunphy, W.G., Hahn, W.C., Virshup, D.M., Kornbluth, S. Cell (2006) [Pubmed]
  4. Activation of Raf-1 by 14-3-3 proteins. Fantl, W.J., Muslin, A.J., Kikuchi, A., Martin, J.A., MacNicol, A.M., Gross, R.W., Williams, L.T. Nature (1994) [Pubmed]
  5. The polarity-inducing kinase Par-1 controls Xenopus gastrulation in cooperation with 14-3-3 and aPKC. Kusakabe, M., Nishida, E. EMBO J. (2004) [Pubmed]
  6. Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25. Kumagai, A., Dunphy, W.G. Genes Dev. (1999) [Pubmed]
  7. Dual phosphorylation controls Cdc25 phosphatases and mitotic entry. Bulavin, D.V., Higashimoto, Y., Demidenko, Z.N., Meek, S., Graves, P., Phillips, C., Zhao, H., Moody, S.A., Appella, E., Piwnica-Worms, H., Fornace, A.J. Nat. Cell Biol. (2003) [Pubmed]
  8. PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation. Margolis, S.S., Walsh, S., Weiser, D.C., Yoshida, M., Shenolikar, S., Kornbluth, S. EMBO J. (2003) [Pubmed]
  9. Fusicoccin signaling reveals 14-3-3 protein function as a novel step in left-right patterning during amphibian embryogenesis. Bunney, T.D., De Boer, A.H., Levin, M. Development (2003) [Pubmed]
  10. Disruption of the 14-3-3 binding site within the B-Raf kinase domain uncouples catalytic activity from PC12 cell differentiation. MacNicol, M.C., Muslin, A.J., MacNicol, A.M. J. Biol. Chem. (2000) [Pubmed]
  11. Protein 14-3-3zeta binds to protein phosphatase PP1gamma2 in bovine epididymal spermatozoa. Huang, Z., Myers, K., Khatra, B., Vijayaraghavan, S. Biol. Reprod. (2004) [Pubmed]
  12. Maintenance of G2 arrest in the Xenopus oocyte: a role for 14-3-3-mediated inhibition of Cdc25 nuclear import. Yang, J., Winkler, K., Yoshida, M., Kornbluth, S. EMBO J. (1999) [Pubmed]
  13. Forskolin and camptothecin induce a 30 kDa protein associated with melatonin production in Y79 human retinoblastoma cells. Janavs, J.L., Florez, J.C., Pierce, M.E., Takahashi, J.S. J. Neurosci. (1995) [Pubmed]
  14. Synergistic activation by Ras and 14-3-3 protein of a mitogen-activated protein kinase kinase kinase named Ras-dependent extracellular signal-regulated kinase kinase stimulator. Shimizu, K., Kuroda, S., Yamamori, B., Matsuda, S., Kaibuchi, K., Yamauchi, T., Isobe, T., Irie, K., Matsumoto, K., Takai, Y. J. Biol. Chem. (1994) [Pubmed]
  15. G2 arrest in Xenopus oocytes depends on phosphorylation of cdc25 by protein kinase A. Duckworth, B.C., Weaver, J.S., Ruderman, J.V. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  16. Differential role of 14-3-3 family members in Xenopus development. Lau, J.M., Wu, C., Muslin, A.J. Dev. Dyn. (2006) [Pubmed]
  17. 14-3-3 Mediates phosphorylation-dependent inhibition of the interaction between the ubiquitin E3 ligase Nedd4-2 and epithelial Na+ channels. Nagaki, K., Yamamura, H., Shimada, S., Saito, T., Hisanaga, S., Taoka, M., Isobe, T., Ichimura, T. Biochemistry (2006) [Pubmed]
 
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