The Growth Factor Granulin Interacts with Cyclin T1 and Modulates P-TEFb-Dependent Transcription

REFERENCES

• Anakwe, O. O., and G. L. Gerton. 1990. Acrosome biogenesis begins during meiosis: evidence from the synthesis and distribution of an acrosomal glycoprotein, acrogranin, during guinea pig spermatogenesis. Biol. Reprod. 42: 317–328.
   PubMed Web of Science ®Google Scholar
• Baba, T., H. B. Hoff 3rd, H. Nemoto, H. Lee, J. Orth, Y. Arai, and G. L. Gerton. 1993. Acrogranin, an acrosomal cysteine-rich glycoprotein, is the precursor of the growth-modulating peptides, granulins, and epithelins, and is expressed in somatic as well as male germ cells. Mol. Reprod. Dev. 34: 233–243.
   PubMed Web of Science ®Google Scholar
• Barboric, M., R. M. Nissen, S. Kanazawa, N. Jabrane-Ferrat, and B. M. Peterlin. 2001. NF-κB binds P-TEFb to stimulate transcriptional elongation by RNA polymerase II. Mol. Cell 8: 327–337.
   PubMed Web of Science ®Google Scholar
• Bateman, A., and H. P. Bennett. 1998. Granulins: the structure and function of an emerging family of growth factors. J. Endocrinol. 158: 145–151.
   PubMed Web of Science ®Google Scholar
• Daniel, R., Z. He, K. P. Carmichael, J. Halper, and A. Bateman. 2000. Cellular localization of gene expression for progranulin. J. Histochem. Cytochem. 48: 999–1009.
   PubMed Web of Science ®Google Scholar
• Diaz-Cueto, L., P. Stein, A. Jacobs, R. M. Schultz, and G. L. Gerton. 2000. Modulation of mouse preimplantation embryo development by acrogranin (epithelin/granulin precursor). Dev. Biol. 217: 406–418.
   PubMed Web of Science ®Google Scholar
• Donald, C. D., A. Laddu, P. Chandham, S. D. Lim, C. Cohen, M. Amin, G. L. Gerton, F. F. Marshall, and J. A. Petros. 2001. Expression of progranulin and the epithelin/granulin precursor acrogranin correlates with neoplastic state in renal epithelium. Anticancer Res. 21: 3739–3742.
   PubMed Web of Science ®Google Scholar
• Endicott, J. A., M. E. Noble, and J. A. Tucker. 1999. Cyclin-dependent kinases: inhibition and substrate recognition. Curr. Opin. Struct. Biol. 9: 738–744.
   PubMed Web of Science ®Google Scholar
• Flores, O., G. Lee, J. Kessler, M. Miller, W. Schlief, J. Tomassini, and D. Hazuda. 1999. Host-cell positive transcription elongation factor b kinase activity is essential and limiting for HIV type 1 replication. Proc. Natl. Acad. Sci. USA 96: 7208–7213.
   PubMed Web of Science ®Google Scholar
• Fong, Y. W., and Q. Zhou. 2000. Relief of two built-In autoinhibitory mechanisms in P-TEFb is required for assembly of a multicomponent transcription elongation complex at the human immunodeficiency virus type 1 promoter. Mol. Cell. Biol. 20: 5897–5907.
   PubMed Web of Science ®Google Scholar
• Fujinaga, K., T. P. Cujec, J. Peng, J. Garriga, D. H. Price, X. Grana, and B. M. Peterlin. 1998. The ability of positive transcription elongation factor b To transactivate human immunodeficiency virus transcription depends on a functional kinase domain, cyclin T1, and Tat. J. Virol. 72: 7154–7159.
   PubMed Web of Science ®Google Scholar
• Fujinaga, K., R. Taube, J. Wimmer, T. P. Cujec, and B. M. Peterlin. 1999. Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T. Proc. Natl. Acad. Sci. USA 96: 1285–1290.
   PubMed Web of Science ®Google Scholar
• Garber, M. E., T. P. Mayall, E. M. Suess, J. Meisenhelder, N. E. Thompson, and K. A. Jones. 2000. CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA. Mol. Cell. Biol. 20: 6958–6969.
   PubMed Web of Science ®Google Scholar
• Garber, M. E., P. Wei, V. N. KewalRamani, T. P. Mayall, C. H. Herrmann, A. P. Rice, D. R. Littman, and K. A. Jones. 1998. The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein. Genes Dev. 12: 3512–3527.
   PubMed Web of Science ®Google Scholar
• Graña, X., A. DeLuca, N. Sang, Y. Fu, P. P. Claudio, J. Rosenblatt, D. O. Morgan, and A. Giordano. 1994. PITALRE, a nuclear CDC2-related protein kinase that phosphorylates the retinoblastoma protein in vitro. Proc. Natl. Acad. Sci. USA 91: 3834–3838.
   PubMed Web of Science ®Google Scholar
• Hartzog, G. A., T. Wada, H. Handa, and F. Winston. 1998. Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae. Genes Dev. 12: 357–369.
   PubMed Web of Science ®Google Scholar
• Herrmann, C. H., and M. A. Mancini. 2001. The Cdk9 and cyclin T subunits of TAK/P-TEFb localize to splicing factor-rich nuclear speckle regions. J. Cell Sci 114: 1491–1503.
   PubMed Web of Science ®Google Scholar
• Herrmann, C. H., and A. P. Rice. 1995. Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactor. J. Virol. 69: 1612–1620.
   PubMed Web of Science ®Google Scholar
• Hirose, Y., and J. L. Manley. 1998. RNA polymerase II is an essential mRNA polyadenylation factor. Nature (London) 395: 93–96.
   PubMed Web of Science ®Google Scholar
• Hrabal, R., Z. Chen, S. James, H. P. Bennett, and F. Ni. 1996. The hairpin stack fold, a novel protein architecture for a new family of protein growth factors. Nat. Struct. Biol. 3: 747–752.
   PubMedGoogle Scholar
• Huang, H. W., and K. T. Wang. 1996. Structural characterization of the metal binding site in the cysteine-rich region of HIV-1 Tat protein. Biochem. Biophys. Res. Commun. 227: 615–621.
   PubMedGoogle Scholar
• Isel, C., and J. Karn. 1999. Direct evidence that HIV-1 Tat stimulates RNA polymerase II carboxyl-terminal domain hyperphosphorylation during transcriptional elongation. J. Mol. Biol. 290: 929–941.
   PubMed Web of Science ®Google Scholar
• Iuchi, S. 2001. Three classes of C2H2 zinc finger proteins. Cell. Mol. Life Sci. 58: 625–635.
   PubMedGoogle Scholar
• Kanazawa, S., T. Okamoto, and B. M. Peterlin. 2000. Tat competes with CIITA for the binding to P-TEFb and blocks the expression of MHC class II genes in HIV infection. Immunity 12: 61–70.
   PubMedGoogle Scholar
• Kaplan, C. D., J. R. Morris, C. Wu, and F. Winston. 2000. Spt5 and spt6 are associated with active transcription and have characteristics of general elongation factors in D. melanogaster. Genes Dev. 14: 2623–2634.
   PubMed Web of Science ®Google Scholar
• Karn, J. 1999. Tackling Tat. J. Mol. Biol. 293: 235–254.
   PubMed Web of Science ®Google Scholar
• Kiernan, R. E., S. Emiliani, K. Nakayama, A. Castro, J. C. Labbe, T. Lorca, K. Nakayama Ki, and M. Benkirane. 2001. Interaction between cyclin T1 and SCF.(SKP2) targets CDK9 for ubiquitination and degradation by the proteasome. Mol. Cell. Biol. 21: 7956–7970.
   PubMedGoogle Scholar
• Kim, J. B., and P. A. Sharp. 2001. Positive transcription elongation factor B phosphorylates human SPT5 and RNA polymerase II carboxyl-terminal domain independently of cyclin-dependent kinase-activating kinase. J. Biol. Chem. 276: 12317–12323.
   PubMed Web of Science ®Google Scholar
• Kim, J. B., Y. Yamaguchi, T. Wada, H. Handa, and P. A. Sharp. 1999. Tat-SF1 protein associates with RAP30 and human SPT5 proteins. Mol. Cell. Biol. 19: 5960–5968.
   PubMedGoogle Scholar
• Kino, T., O. Slobodskaya, G. N. Pavlakis, and G. P. Chrousos. 2002. Nuclear receptor coactivator p160 proteins enhance the HIV-1 long terminal repeat promoter by bridging promoter-bound factors and the Tat-P-TEFb complex. J. Biol. Chem. 277: 2396–2405.
   PubMedGoogle Scholar
• Laity, J. H., B. M. Lee, and P. E. Wright. 2001. Zinc finger proteins: new insights into structural and functional diversity. Curr. Opin. Struct. Biol. 11: 39–46.
   PubMed Web of Science ®Google Scholar
• Liau, L. M., R. L. Lallone, R. S. Seitz, A. Buznikov, J. P. Gregg, H. I. Kornblum, S. F. Nelson, and J. M. Bronstein. 2000. Identification of a human glioma-associated growth factor gene, granulin, with differential immuno-absorption. Cancer Res. 60: 1353–1360.
   PubMed Web of Science ®Google Scholar
• Line, A., A. Stengrevics, Z. Slucka, G. Li, E. Jankevics, and R. C. Rees. 2002. Serological identification and expression analysis of gastric cancer-associated genes. Br. J. Cancer 86: 1824–1830.
   PubMed Web of Science ®Google Scholar
• Lu, R., and G. Serrero. 2000. Inhibition of PC cell-derived growth factor (PCDGF, epithelin/granulin precursor) expression by antisense PCDGF cDNA transfection inhibits tumorigenicity of the human breast carcinoma cell line MDA-MB-468. Proc. Natl. Acad. Sci. USA 97: 3993–3998.
   PubMed Web of Science ®Google Scholar
• Lu, R., and G. Serrero. 2001. Mediation of estrogen mitogenic effect in human breast cancer MCF-7 cells by PC-cell-derived growth factor (PCDGF/granulin precursor). Proc. Natl. Acad. Sci. USA 98: 142–147.
   PubMed Web of Science ®Google Scholar
• Lu, R., and G. Serrero. 1999. Stimulation of PC cell-derived growth factor (epithelin/granulin precursor) expression by estradiol in human breast cancer cells. Biochem. Biophys. Res. Commun. 256: 204–207.
   PubMedGoogle Scholar
• Majello, B., G. Napolitano, A. Giordano, and L. Lania. 1999. Transcriptional regulation by targeted recruitment of cyclin-dependent CDK9 kinase in vivo. Oncogene 18: 4598–4605.
   PubMed Web of Science ®Google Scholar
• Marcello, A., R. A. Cinelli, A. Ferrari, A. Signorelli, M. Tyagi, V. Pellegrini, F. Beltram, and M. Giacca. 2001. Visualization of in vivo direct interaction between HIV-1 TAT and human cyclin T1 in specific subcellular compartments by fluorescence resonance energy transfer. J. Biol. Chem. 276: 39220–39225.
   PubMedGoogle Scholar
• Marshall, N. F., J. Peng, Z. Xie, and D. H. Price. 1996. Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J. Biol. Chem. 271: 27176–27183.
   PubMed Web of Science ®Google Scholar
• Miller, M. E., and F. R. Cross. 2001. Cyclin specificity: how many wheels do you need on a unicycle? J. Cell Sci. 114: 1811–1820.
   PubMedGoogle Scholar
• Morris, G. F., and M. B. Mathews. 1990. Analysis of the proliferating cell nuclear antigen promoter and its response to adenovirus early region 1. J. Biol. Chem. 265: 16116–16125.
   PubMedGoogle Scholar
• Napolitano, G., P. Licciardo, R. Carbone, B. Majello, and L. Lania. 2002. CDK9 has the intrinsic property to shuttle between nucleus and cytoplasm, and enhanced expression of cyclin T1 promotes its nuclear localization. J. Cell. Physiol. 192: 209–215.
   PubMedGoogle Scholar
• Napolitano, G., B. Majello, P. Licciardo, A. Giordano, and L. Lania. 2000. Transcriptional activity of positive transcription elongation factor b kinase in vivo requires the C-terminal domain of RNA polymerase II. Gene 254: 139–145.
   PubMed Web of Science ®Google Scholar
• Parada, C. A., and R. G. Roeder. 1999. A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription. EMBO J. 18: 3688–3701.
   PubMedGoogle Scholar
• Pendergrast, P. S., C. Wang, N. Hernandez, and S. Huang. 2002. FBI-1 can stimulate HIV-1 Tat activity and is targeted to a novel subnuclear domain that includes the Tat-P-TEFb-containing nuclear speckles. Mol. Biol. Cell 13: 915–929.
   PubMed Web of Science ®Google Scholar
• Peng, J., N. F. Marshall, and D. H. Price. 1998. Identification of a cyclin subunit required for the function of Drosophila P-TEFb. J. Biol. Chem. 273: 13855–13860.
   PubMed Web of Science ®Google Scholar
• Peng, J., Y. Zhu, J. T. Milton, and D. H. Price. 1998. Identification of multiple cyclin subunits of human P-TEFb. Genes Dev. 12: 755–762.
   PubMed Web of Science ®Google Scholar
• Price, D. H. 2000. P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II. Mol. Cell. Biol. 20: 2629–2634.
   PubMed Web of Science ®Google Scholar
• Ramanathan, Y., S. M. Rajpara, S. M. Reza, E. Lees, S. Shuman, M. B. Mathews, and T. Pe'ery. 2001. Three RNA polymerase II carboxyl-terminal domain kinases display distinct substrate preferences. J. Biol. Chem. 276: 10913–10920.
   PubMed Web of Science ®Google Scholar
• Ramanathan, Y., S. M. Reza, T. M. Young, M. B. Mathews, and T. Pe'ery. 1999. Human and rodent transcription elongation factor P-TEFb: interactions with human immunodeficiency virus type 1 tat and carboxy-terminal domain substrate. J. Virol. 73: 5448–5458.
   PubMed Web of Science ®Google Scholar
• Reza, S. M., M. Rosetti, M. B. Mathews, and T. Pe'ery. Differential activation of Tat variants in mitogen-stimulated cells: implications for HIV-1 postintegration latency. Virology, in press.
   Google Scholar
• Romisch, K. 1999. Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane. J. Cell Sci. 112: 4185–4191.
   PubMedGoogle Scholar
• Saurin, A. J., K. L. Borden, M. N. Boddy, and P. S. Freemont. 1996. Does this have a familiar RING? Trends Biochem. Sci. 21: 208–214.
   PubMed Web of Science ®Google Scholar
• Schulman, B. A., D. L. Lindstrom, and E. Harlow. 1998. Substrate recruitment to cyclin-dependent kinase 2 by a multipurpose docking site on cyclin A. Proc. Natl. Acad. Sci. USA 95: 10453–10458.
   PubMed Web of Science ®Google Scholar
• Sui, D., and J. E. Wilson. 2000. Interaction of insulin-like growth factor binding protein-4, Miz-1, leptin, lipocalin-type prostaglandin D synthase, and granulin precursor with the N-terminal half of type III hexokinase. Arch. Biochem. Biophys. 382: 262–274.
   PubMedGoogle Scholar
• Sune, C., A. C. Goldstrohm, J. Peng, D. H. Price, and M. A. Garcia-Blanco. 2000. An in vitro transcription system that recapitulates equine infectious anemia virus tat-mediated inhibition of human immunodeficiency virus type 1 Tat activity demonstrates a role for positive transcription elongation factor b and associated proteins in the mechanism of Tat activation. Virology 274: 356–366.
   PubMedGoogle Scholar
• Taube, R., X. Lin, D. Irwin, K. Fujinaga, and B. M. Peterlin. 2002. Interaction between P-TEFb and the C-terminal domain of RNA polymerase II activates transcriptional elongation from sites upstream or downstream of target genes. Mol. Cell. Biol. 22: 321–331.
   PubMed Web of Science ®Google Scholar
• Trinh, D. P., K. M. Brown, and K. T. Jeang. 1999. Epithelin/granulin growth factors: extracellular cofactors for HIV-1 and HIV-2 Tat proteins. Biochem. Biophys. Res. Commun. 256: 299–306.
   PubMedGoogle Scholar
• Wada, T., T. Takagi, Y. Yamaguchi, A. Ferdous, T. Imai, S. Hirose, S. Sugimoto, K. Yano, G. A. Hartzog, F. Winston, S. Buratowski, and H. Handa. 1998. DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs. Genes Dev. 12: 343–356.
   PubMed Web of Science ®Google Scholar
• Wada, T., T. Takagi, Y. Yamaguchi, D. Watanabe, and H. Handa. 1998. Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro. EMBO J. 17: 7395–7403.
   PubMed Web of Science ®Google Scholar
• Wakasugi, K., and P. Schimmel. 1999. Two distinct cytokines released from a human aminoacyl-tRNA synthetase. Science 284: 147–151.
   PubMed Web of Science ®Google Scholar
• Wei, P., M. E. Garber, S. M. Fang, W. H. Fischer, and K. A. Jones. 1998. A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell 92: 451–462.
   PubMed Web of Science ®Google Scholar
• Wimmer, J., K. Fujinaga, R. Taube, T. P. Cujec, Y. Zhu, J. Peng, D. H. Price, and B. M. Peterlin. 1999. Interactions between Tat and TAR and human immunodeficiency virus replication are facilitated by human cyclin T1 but not cyclins T2a or T2b. Virology 255: 182–189.
   PubMed Web of Science ®Google Scholar
• Wu-Baer, F., W. S. Lane, and R. B. Gaynor. 1998. Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation. J. Mol. Biol. 277: 179–197.
   PubMed Web of Science ®Google Scholar
• Xu, S. Q., D. Tang, S. Chamberlain, G. Pronk, F. R. Masiarz, S. Kaur, M. Prisco, T. ZanoccoMarani, and R. Baserga. 1998. The granulin/epithelin precursor abrogates the requirement for the insulin-like growth factor 1 receptor for growth in vitro. J. Biol. Chem. 273: 20078–20083.
   PubMed Web of Science ®Google Scholar
• Yamaguchi, Y., T. Takagi, T. Wada, K. Yano, A. Furuya, S. Sugimoto, J. Hasegawa, and H. Handa. 1999. NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation. Cell 97: 41–51.
   PubMed Web of Science ®Google Scholar
• Zanocco-Marani, T., A. Bateman, G. Romano, B. Valentinis, Z. H. He, and R. Baserga. 1999. Biological activities and signaling pathways of the granulin/epithelin precursor. Cancer Res.. 59: 5331–5340.
   PubMed Web of Science ®Google Scholar
• Zhang, H., and G. Serrero. 1998. Inhibition of tumorigenicity of the teratoma PC cell line by transfection with antisense cDNA for PC cell-derived growth factor (PCDGF, epithelin/granulin precursor). Proc. Natl. Acad. Sci. USA 95: 14202–14207.
   PubMed Web of Science ®Google Scholar
• Zhang, J., N. Tamilarasu, S. Hwang, M. E. Garber, I. Huq, K. A. Jones, and T. M. Rana. 2000. HIV-1 TAR RNA enhances the interaction between Tat and cyclin T1. J. Biol. Chem. 275: 34314–34319.
   PubMedGoogle Scholar
• Zhou, J., G. Gao, J. W. Crabb, and G. Serrero. 1993. Purification of an autocrine growth factor homologous with mouse epithelin precursor from a highly tumorigenic cell line. J. Biol. Chem. 268: 10863–10869.
   PubMed Web of Science ®Google Scholar
• Zhu, Y., T. Pe'ery, J. Peng, Y. Ramanathan, N. Marshall, T. Marshall, B. Amendt, M. B. Mathews, and D. H. Price. 1997. Transcription elongation factor P-TEFb is required for HIV-1 tat transactivation in vitro. Genes Dev. 11: 2622–2632.
   PubMed Web of Science ®Google Scholar