A rapid conformational rearrangement of STAT1 dimers is required for termination rather than for amplification of interferon-γ signaling

References

• Brivanlou AH, Darnell JE Jr.. Signal transduction and the control of gene expression. Science 2002; 295:813 - 8; http://dx.doi.org/10.1126/science.1066355; PMID: 11823631
   PubMed Web of Science ®Google Scholar
• Levy DE, Darnell JE Jr.. Stats: transcriptional control and biological impact. Nat Rev Mol Cell Biol 2002; 3:651 - 62; http://dx.doi.org/10.1038/nrm909; PMID: 12209125
   PubMed Web of Science ®Google Scholar
• Darnell JE Jr., Kerr IM, Stark GR. JAK-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 1994; 264:1415 - 21; http://dx.doi.org/10.1126/science.8197455; PMID: 8197455
   PubMed Web of Science ®Google Scholar
• Darnell JE Jr.. STATs and gene regulation. Science 1997; 277:1630 - 5; http://dx.doi.org/10.1126/science.277.5332.1630; PMID: 9287210
   PubMed Web of Science ®Google Scholar
• Ihle JN. The Stat family in cytokine signaling. Curr Opin Cell Biol 2001; 13:211 - 7; http://dx.doi.org/10.1016/S0955-0674(00)00199-X; PMID: 11248555
   PubMed Web of Science ®Google Scholar
• Shuai K, Schindler C, Prezioso VR, Darnell JE Jr.. Activation of transcription by IFN-gamma: tyrosine phosphorylation of a 91-kD DNA binding protein. Science 1992; 258:1808 - 12; http://dx.doi.org/10.1126/science.1281555; PMID: 1281555
   PubMed Web of Science ®Google Scholar
• Shuai K, Stark GR, Kerr IM, Darnell JE Jr.. A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma. Science 1993; 261:1744 - 6; http://dx.doi.org/10.1126/science.7690989; PMID: 7690989
   PubMed Web of Science ®Google Scholar
• Shuai K, Horvath CM, Huang LH, Qureshi SA, Cowburn D, Darnell JE Jr.. Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions. Cell 1994; 76:821 - 8; http://dx.doi.org/10.1016/0092-8674(94)90357-3; PMID: 7510216
   PubMed Web of Science ®Google Scholar
• Greenlund AC, Morales MO, Viviano BL, Yan H, Krolewski J, Schreiber RD. Stat recruitment by tyrosine-phosphorylated cytokine receptors: an ordered reversible affinity-driven process. Immunity 1995; 2:677 - 87; http://dx.doi.org/10.1016/1074-7613(95)90012-8; PMID: 7796299
   PubMed Web of Science ®Google Scholar
• Decker T, Kovarik P, Meinke A. GAS elements: a few nucleotides with a major impact on cytokine-induced gene expression. J Interferon Cytokine Res 1997; 17:121 - 34; http://dx.doi.org/10.1089/jir.1997.17.121; PMID: 9085936
   PubMed Web of Science ®Google Scholar
• Herrington J, Rui L, Luo G, Yu-Lee LY, Carter-Su C. A functional DNA binding domain is required for growth hormone-induced nuclear accumulation of Stat5B. J Biol Chem 1999; 274:5138 - 45; http://dx.doi.org/10.1074/jbc.274.8.5138; PMID: 9988763
   PubMed Web of Science ®Google Scholar
• Sehgal PB. Paradigm shifts in the cell biology of STAT signaling. Semin Cell Dev Biol 2008; 19:329 - 40; http://dx.doi.org/10.1016/j.semcdb.2008.07.003; PMID: 18691663
   PubMed Web of Science ®Google Scholar
• Speil J, Baumgart E, Siebrasse JP, Veith R, Vinkemeier U, Kubitscheck U. Activated STAT1 transcription factors conduct distinct saltatory movements in the cell nucleus. Biophys J 2011; 101:2592 - 600; http://dx.doi.org/10.1016/j.bpj.2011.10.006; PMID: 22261046
   PubMed Web of Science ®Google Scholar
• Schindler C, Shuai K, Prezioso VR, Darnell JE Jr.. Interferon-dependent tyrosine phosphorylation of a latent cytoplasmic transcription factor. Science 1992; 257:809 - 13; http://dx.doi.org/10.1126/science.1496401; PMID: 1496401
   PubMed Web of Science ®Google Scholar
• Horvath CM, Wen Z, Darnell JE Jr.. A STAT protein domain that determines DNA sequence recognition suggests a novel DNA-binding domain. Genes Dev 1995; 9:984 - 94; http://dx.doi.org/10.1101/gad.9.8.984; PMID: 7774815
   PubMed Web of Science ®Google Scholar
• Horvath CM, Stark GR, Kerr IM, Darnell JE Jr.. Interactions between STAT and non-STAT proteins in the interferon-stimulated gene factor 3 transcription complex. Mol Cell Biol 1996; 16:6957 - 64; PMID: 8943351
   PubMed Web of Science ®Google Scholar
• Meyer T, Begitt A, Lödige I, van Rossum M, Vinkemeier U. Constitutive and IFN-γ-induced nuclear import of STAT1 proceed through independent pathways. EMBO J 2002; 21:344 - 54; http://dx.doi.org/10.1093/emboj/21.3.344; PMID: 11823427
   PubMed Web of Science ®Google Scholar
• Marg A, Shan Y, Meyer T, Meissner T, Brandenburg M, Vinkemeier U. Nucleocytoplasmic shuttling by nucleoporins Nup153 and Nup214 and CRM1-dependent nuclear export control the subcellular distribution of latent Stat1. J Cell Biol 2004; 165:823 - 33; http://dx.doi.org/10.1083/jcb.200403057; PMID: 15210729
   PubMed Web of Science ®Google Scholar
• Meyer T, Marg A, Lemke P, Wiesner B, Vinkemeier U. DNA binding controls inactivation and nuclear accumulation of the transcription factor Stat1. Genes Dev 2003; 17:1992 - 2005; http://dx.doi.org/10.1101/gad.268003; PMID: 12923054
   PubMed Web of Science ®Google Scholar
• Sekimoto T, Imamoto N, Nakajima K, Hirano T, Yoneda Y. Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1. EMBO J 1997; 16:7067 - 77; http://dx.doi.org/10.1093/emboj/16.23.7067; PMID: 9384585
   PubMed Web of Science ®Google Scholar
• Fagerlund R, Mélen K, Kinnunen L, Julkunen I. Arginine/lysine-rich nuclear localization signals mediate interactions between dimeric STATs and importin α 5. J Biol Chem 2002; 277:30072 - 8; http://dx.doi.org/10.1074/jbc.M202943200; PMID: 12048190
   PubMed Web of Science ®Google Scholar
• McBride KM, Banninger G, McDonald C, Reich NC. Regulated nuclear import of the STAT1 transcription factor by direct binding of importin-α. EMBO J 2002; 21:1754 - 63; http://dx.doi.org/10.1093/emboj/21.7.1754; PMID: 11927559
   PubMed Web of Science ®Google Scholar
• Melén K, Fagerlund R, Franke J, Köhler M, Kinnunen L, Julkunen I. Importin α nuclear localization signal binding sites for STAT1, STAT2, and influenza A virus nucleoprotein. J Biol Chem 2003; 278:28193 - 200; http://dx.doi.org/10.1074/jbc.M303571200; PMID: 12740372
   PubMed Web of Science ®Google Scholar
• Nardozzi J, Wenta N, Yasuhara N, Vinkemeier U, Cingolani G. Molecular basis for the recognition of phosphorylated STAT1 by importin α5. J Mol Biol 2010; 402:83 - 100; http://dx.doi.org/10.1016/j.jmb.2010.07.013; PMID: 20643137
   PubMed Web of Science ®Google Scholar
• Chen X, Vinkemeier U, Zhao Y, Jeruzalmi D, Darnell JE Jr., Kuriyan J. Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA. Cell 1998; 93:827 - 39; http://dx.doi.org/10.1016/S0092-8674(00)81443-9; PMID: 9630226
   PubMed Web of Science ®Google Scholar
• Mao X, Ren Z, Parker GN, Sondermann H, Pastorello MA, Wang W, et al. Structural bases of unphosphorylated STAT1 association and receptor binding. Mol Cell 2005; 17:761 - 71; http://dx.doi.org/10.1016/j.molcel.2005.02.021; PMID: 15780933
   PubMed Web of Science ®Google Scholar
• Zhong M, Henriksen MA, Takeuchi K, Schaefer O, Liu B, ten Hoeve J, et al. Implications of an antiparallel dimeric structure of nonphosphorylated STAT1 for the activation-inactivation cycle. Proc Natl Acad Sci U S A 2005; 102:3966 - 71; http://dx.doi.org/10.1073/pnas.0501063102; PMID: 15753310
   PubMed Web of Science ®Google Scholar
• Mertens C, Zhong M, Krishnaraj R, Zou W, Chen X, Darnell JE Jr.. Dephosphorylation of phosphotyrosine on STAT1 dimers requires extensive spatial reorientation of the monomers facilitated by the N-terminal domain. Genes Dev 2006; 20:3372 - 81; http://dx.doi.org/10.1101/gad.1485406; PMID: 17182865
   PubMed Web of Science ®Google Scholar
• Wenta N, Strauss H, Meyer S, Vinkemeier U. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Proc Natl Acad Sci U S A 2008; 105:9238 - 43; http://dx.doi.org/10.1073/pnas.0802130105; PMID: 18591661
   PubMed Web of Science ®Google Scholar
• ten Hoeve J, de Jesus Ibarra-Sanchez M, Fu Y, Zhu W, Tremblay M, David M, et al. Identification of a nuclear Stat1 protein tyrosine phosphatase. Mol Cell Biol 2002; 22:5662 - 8; http://dx.doi.org/10.1128/MCB.22.16.5662-5668.2002; PMID: 12138178
   PubMed Web of Science ®Google Scholar
• Yang E, Henriksen MA, Schaefer O, Zakharova N, Darnell JE Jr.. Dissociation time from DNA determines transcriptional function in a STAT1 linker mutant. J Biol Chem 2002; 277:13455 - 62; http://dx.doi.org/10.1074/jbc.M112038200; PMID: 11834743
   PubMed Web of Science ®Google Scholar
• Meyer T, Hendry L, Begitt A, John S, Vinkemeier U. A single residue modulates tyrosine dephosphorylation, oligomerization, and nuclear accumulation of stat transcription factors. J Biol Chem 2004; 279:18998 - 9007; http://dx.doi.org/10.1074/jbc.M400766200; PMID: 15010467
   PubMed Web of Science ®Google Scholar
• van de Stolpe A, Caldenhoven E, Stade BG, Koenderman L, Raaijmakers JA, Johnson JP, et al. 12-O-tetradecanoylphorbol-13-acetate- and tumor necrosis factor alpha-mediated induction of intercellular adhesion molecule-1 is inhibited by dexamethasone. Functional analysis of the human intercellular adhesion molecular-1 promoter. J Biol Chem 1994; 269:6185 - 92; PMID: 7907090
   PubMed Web of Science ®Google Scholar
• Müller M, Laxton C, Briscoe J, Schindler C, Improta T, Darnell JE Jr., et al. Complementation of a mutant cell line: central role of the 91 kDa polypeptide of ISGF3 in the interferon-α and -γ signal transduction pathways. EMBO J 1993; 12:4221 - 8; PMID: 7693454
   PubMed Web of Science ®Google Scholar
• Begitt A, Meyer T, van Rossum M, Vinkemeier U. Nucleocytoplasmic translocation of Stat1 is regulated by a leucine-rich export signal in the coiled-coil domain. Proc Natl Acad Sci U S A 2000; 97:10418 - 23; http://dx.doi.org/10.1073/pnas.190318397; PMID: 10973496
   PubMed Web of Science ®Google Scholar
• Lödige I, Marg A, Wiesner B, Malecová B, Oelgeschläger T, Vinkemeier U. Nuclear export determines the cytokine sensitivity of STAT transcription factors. J Biol Chem 2005; 280:43087 - 99; http://dx.doi.org/10.1074/jbc.M509180200; PMID: 16195225
   PubMed Web of Science ®Google Scholar
• Wen Z, Zhong Z, Darnell JE Jr.. Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation. Cell 1995; 82:241 - 50; http://dx.doi.org/10.1016/0092-8674(95)90311-9; PMID: 7543024
   PubMed Web of Science ®Google Scholar