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Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen.
He, Yanan; Chen, Yihong; Mooney, Steven M; Rajagopalan, Krithika; Bhargava, Ajay; Sacho, Elizabeth; Weninger, Keith; Bryan, Philip N; Kulkarni, Prakash; Orban, John.
Afiliação
  • He Y; From the W. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland 20850, the Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742.
  • Chen Y; From the W. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland 20850, the Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742.
  • Mooney SM; the Department of Urology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21287.
  • Rajagopalan K; the Department of Urology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21287.
  • Bhargava A; Shakti BioResearch, Woodbridge, Connecticut 06525, and.
  • Sacho E; the Department of Physics, North Carolina State University, Raleigh, North Carolina 27695.
  • Weninger K; the Department of Physics, North Carolina State University, Raleigh, North Carolina 27695.
  • Bryan PN; From the W. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland 20850.
  • Kulkarni P; the Department of Urology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21287, pkulkar4@ibbr.umd.edu.
  • Orban J; From the W. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland 20850, the Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, jorban@umd.edu.
J Biol Chem ; 290(41): 25090-102, 2015 Oct 09.
Article em En | MEDLINE | ID: mdl-26242913
Prostate-associated gene 4 (PAGE4) is an intrinsically disordered cancer/testis antigen that is up-regulated in the fetal and diseased human prostate. Knocking down PAGE4 expression results in cell death, whereas its overexpression leads to a growth advantage of prostate cancer cells (Zeng, Y., He, Y., Yang, F., Mooney, S. M., Getzenberg, R. H., Orban, J., and Kulkarni, P. (2011) The cancer/testis antigen prostate-associated gene 4 (PAGE4) is a highly intrinsically disordered protein. J. Biol. Chem. 286, 13985-13994). Phosphorylation of PAGE4 at Thr-51 is critical for potentiating c-Jun transactivation, an important factor in controlling cell growth, apoptosis, and stress response. Using NMR spectroscopy, we show that the PAGE4 polypeptide chain has local and long-range conformational preferences that are perturbed by site-specific phosphorylation at Thr-51. The population of transient turn-like structures increases upon phosphorylation in an ∼20-residue acidic region centered on Thr-51. This central region therefore becomes more compact and more negatively charged, with increasing intramolecular contacts to basic sequence motifs near the N and C termini. Although flexibility is decreased in the central region of phospho-PAGE4, the polypeptide chain remains highly dynamic overall. PAGE4 utilizes a transient helical structure adjacent to the central acidic region to bind c-Jun with low affinity in vitro. The binding interaction is attenuated by phosphorylation at Thr-51, most likely because of masking the effects of the more compact phosphorylated state. Therefore, phosphorylation of PAGE4 leads to conformational shifts in the dynamic ensemble, with large functional consequences. The changes in the structural ensemble induced by posttranslational modifications are similar conceptually to the conformational switching events seen in some marginally stable ("metamorphic") folded proteins in response to mutation or environmental triggers.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Neoplasias da Próstata / Antígenos de Neoplasias Idioma: En Ano de publicação: 2015 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Neoplasias da Próstata / Antígenos de Neoplasias Idioma: En Ano de publicação: 2015 Tipo de documento: Article