How to cite this WIREs title:
WIREs RNA

Impact Factor: 9.957

The role of AUF1 in regulated mRNA decay

Advanced Review

Gary Brewer, Frances M. Gratacós

Published Online: Jun 14 2010

DOI: 10.1002/wrna.26

Full article on Wiley Online Library: HTML PDF

Can't access this content? Tell your librarian.

Abstract Messenger ribonucleic acid (mRNA) turnover is a major control point in gene expression. In mammals, many mRNAs encoding inflammatory cytokines, oncoproteins, and G‐protein‐coupled receptors are destabilized by the presence of AU‐rich elements (AREs) in their 3′‐untranslated regions. Association of ARE‐binding proteins (AUBPs) with these mRNAs promotes rapid mRNA degradation. ARE/poly(U)‐binding/degradation factor 1 (AUF1), one of the best‐characterized AUBPs, binds to many ARE‐mRNAs and assembles other factors necessary to recruit the mRNA degradation machinery. These factors include translation initiation factor eIF4G, chaperones hsp27 and hsp70, heat‐shock cognate protein hsc70, lactate dehydrogenase, poly(A)‐binding protein, and other unidentified proteins. Numerous signaling pathways alter the composition of this AUF1 complex of proteins to effect changes in ARE‐mRNA degradation rates. This review briefly describes the roles of mRNA decay in gene expression in general and ARE‐mediated decay (AMD) in particular, with a focus on AUF1 and the different modes of regulation that govern AUF1 involvement in AMD. Copyright © 2010 John Wiley & Sons, Ltd. This article is categorized under: RNA Interactions with Proteins and Other Molecules > Protein–RNA Interactions: Functional Implications RNA Turnover and Surveillance > Turnover/Surveillance Mechanisms RNA Turnover and Surveillance > Regulation of RNA Stability

Schematic of deadenylation‐dependent, AU‐rich element (ARE)‐mediated messenger ribonucleic acid (mRNA) degradation. The mRNA is depicted with a 5′‐cap structure and 3′‐poly(A) tail. The ARE is shown as the boxed AUUUA. The start and stop codons are highlighted. The sequential pathway involves exoribonucleolytic removal of the poly(A) tail, followed by decapping and subsequent 5′ → 3′ and/or 3′ → 5′ degradation.

[ Normal View | Magnified View ]

Dynamics of the ARE/poly(U)‐binding/degradation factor 1 (AUF1) complex of proteins and AU‐rich element (ARE)‐mediated mRNA decay. AUF1 interacts with eIF4G and the ARE. During ongoing translation, AUF1 is displaced from the ARE in a complex with poly(A)‐binding protein (PABP), perhaps exposing the poly(A) tail to ribonucleases. This may require destruction of AUF1 by proteasomes. During heat shock, association of hsp70 with AUF1 may disrupt or block the AUF1–PABP interaction, leaving PABP free to remain bound to the poly(A) tail, thus masking it from ribonucleases.

[ Normal View | Magnified View ]

Three‐step model of ARE/poly(U)‐binding/degradation factor 1 (AUF1)‐dependent, AU‐rich element (ARE)‐mediated decay. The first step, dynamic AUF1 dimer binding and oligomerization, may be sufficient for this phase of assembly. Other association of ARE‐binding proteins, including the Hu family of messenger ribonucleic acid (mRNA)‐stabilizing proteins, may compete for AUF1 binding to the ARE at this stage, thus preventing AUF1 oligomerization and subsequent factor recruitment. The second step, trans‐acting complex assembly, involves association of AUF1 with eIF4G, PABP, hsp/hsc70, hsp27, and additional unidentified proteins. The third step, mRNA catabolism, involves two linked catabolic steps—ubiquitin‐dependent degradation of AUF1 by proteasomes and mRNA destruction by mRNA decay enzymes. (Reprinted with kind permission from Ref. 101 Copyright 2002 Springer Science and Business Media).

[ Normal View | Magnified View ]

p40^AUF1 phosphorylation changes upon PKC: protein kinase c activation. In nonactivated monocytes, Ser 83 and Ser 87 are phosphorylated, concomitant with labile cytokine messenger ribonucleic acids (mRNAs). PKC activation promotes loss of phosphates from Ser 83 and Ser 87, concomitant with cytokine mRNA stabilization.

[ Normal View | Magnified View ]

ARE/poly(U)‐binding/degradation factor 1 proteins are generated by alternative pre‐messenger ribonucleic acid (mRNA) splicing. The AUF1/HNRPD gene has 10 exons (not shown to scale). The start codon in exon 1 and the stop codon in exon 8 are highlighted. The domain structures are shown in increasing order of apparent molecular weights. The dimerization domain, RRM1, RRM2, and Q‐rich domain common to all isoforms are highlighted. Alternatively spliced exons 2 and 7 are represented by the stripped box and the red box, respectively. (Reprinted with permission from Ref. 44 Copyright 1998 Elsevier).

[ Normal View | Magnified View ]

References

Nestler, EJ, Hyman, SE. Regulation of gene expression. In: Keneth, DC, Davis, L, Coyle, Joseph T, Nemeroff, Charles, eds. Neurophsycopharmacology: The Fifth Generation of Progress. Nashville, TN: American College of Neuropharmacology; 2002; 217–228.
Barreau, C, Paillard, L, Osborne, HB. AU‐rich elements and associated factors: are there unifying principles?. Nucleic Acids Res 2005; 33: 7138–7150. doi:33/22/7138 [pii].
Ross, J. mRNA stability in mammalian cells. Microbiol Rev 1995; 59: 423–450.
Wilusz, CJ, Wormington, M, Peltz, SW. The cap‐to‐tail guide to mRNA turnover. Nat Rev Mol Cell Biol 2001; 2: 237–246. doi:10.1038/35067025.
Tarun, SZ, Jr, Sachs, AB. Binding of eukaryotic translation initiation factor 4E (eIF4E) to eIF4G represses translation of uncapped mRNA. Mol Cell Biol 1997; 17: 6876–6886.
Mitchell, P, Tollervey, D. mRNA stability in eukaryotes. Curr Opin Genet Dev 2000; 10: 193–198. doi: S0959‐437X(00)00063‐0 [pii].
Guhaniyogi, J, Brewer, G. Regulation of mRNA stability in mammalian cells. Gene 2001; 265: 11–23. doi:S037811190100350X [pii].
Fritz, DT, Bergman, N, Kilpatrick, WJ, Wilusz, CJ, Wilusz, J. Messenger RNA decay in mammalian cells: the exonuclease perspective. Cell Biochem Biophys 2004; 41: 265–278. doi:CBB:41:2:265 [pii].
Chen, CY, Shyu, AB. AU‐rich elements: characterization and importance in mRNA degradation. Trends Biochem Sci 1995; 20: 465–470. doi:S0968000400891021 [pii].
Brewer, G. Evidence for a 3′ → 5′ decay pathway for c‐myc mRNA in mammalian cells. J Biol Chem 1999; 274: 16174–16179.
DeMaria, CT, Brewer, G. AUF1 binding affinity to A + U‐rich elements correlates with rapid mRNA degradation. J Biol Chem 1996; 271: 12179–12184.
Zubiaga, AM, Belasco, JG, Greenberg, ME. The nonamer UUAUUUAUU is the key AU‐rich sequence motif that mediates mRNA degradation. Mol Cell Biol 1995; 15: 2219–2230.
Savant‐Bhonsale, S, Cleveland, DW. Evidence for instability of mRNAs containing AUUUA motifs mediated through translation‐dependent assembly of a %3E 20S degradation complex. Genes Dev 1992; 6: 1927–1939.
Aharon, T, Schneider, RJ. Selective destabilization of short‐lived mRNAs with the granulocyte‐macrophage colony‐stimulating factor AU‐rich 3′ noncoding region is mediated by a cotranslational mechanism. Mol Cell Biol 1993; 13: 1971–1980.
Ma, WJ, Chung, S, Furneaux, H. The Elav‐like proteins bind to AU‐rich elements and to the poly(A) tail of mRNA. Nucleic Acids Res 1997; 25: 3564–3569. doi:gka577 [pii].
Myer, VE, Fan, XC, Steitz, JA. Identification of HuR as a protein implicated in AUUUA‐mediated mRNA decay. EMBO J 1997; 16: 2130–2139. doi:10.1093/emboj/16.8.2130.
Hanakahi, LA, Dempsey, LA, Li, MJ, Maizels, N. Nucleolin is one component of the B cell‐specific transcription factor and switch region binding protein, LR1. Proc Natl Acad Sci USA 1997; 94: 3605–3610.
Lal, A, Mazan‐Mamczarz, K, Kawai, T, Yang, X, Martindale, JL, Gorospe, M. Concurrent versus individual binding of HuR and AUF1 to common labile target mRNAs. EMBO J 2004; 23: 3092–3102. doi:10.1038/sj.emboj.7600305.
David, PS, Tanveer, R, Port, JD. FRET‐detectable interactions between the ARE binding proteins, HuR and p37AUF1. RNA 2007; 13: 1453–1468. doi:rna.501707 [pii].
Abdelmohsen, K, Srikantan, S, Yang, X, Lal, A, Kim, HH, Kuwano, Y, Galban, S, Becker, KG, Kamara, D, Cabo, R, et al. Ubiquitin‐mediated proteolysis of HuR by heat shock. EMBO J 2009; 28: 1271–1282. emboj200967 [pii].
Lafon, I, Carballes, F, Brewer, G, Poiret, M, Morello, D. Developmental expression of AUF1 and HuR, two c‐myc mRNA binding proteins. Oncogene 1998; 16: 3413–3421. doi:10.1038/sj.onc.1201895.
Brewer, G. An A + U‐rich element RNA‐binding factor regulates c‐myc mRNA stability in vitro. Mol Cell Biol 1991; 11: 2460–2466.
Pinol‐Roma, S, Choi, YD, Matunis, MJ, Dreyfuss, G. Immunopurification of heterogeneous nuclear ribonucleoprotein particles reveals an assortment of RNA‐binding proteins. Genes Dev 1988; 2: 215–227.
Zhang, W, Wagner, BJ, Ehrenman, K, Schaefer, AW, DeMaria, CT, Crater, D, DeHaven, K, Long, L, Brewer, G. Purification, characterization, and cDNA cloning of an AU‐rich element RNA‐binding protein. AUF1 Mol Cell Biol 1993; 13: 7652–7665.
DeMaria, CT, Sun, Y, Long, L, Wagner, BJ, Brewer, G. Structural determinants in AUF1 required for high affinity binding to A + U‐rich elements. J Biol Chem 1997; 272: 27635–27643.
Wilson, GM, Sun, Y, Lu, H, Brewer, G. Assembly of AUF1 oligomers on U‐rich RNA targets by sequential dimer association. J Biol Chem 1999; 274: 33374–33381.
Sagliocco, F, Laloo, B, Cosson, B, Laborde, L, Castroviejo, M, Rosenbaum, J, Ripoche, J, Grosset, C. The ARE‐associated factor AUF1 binds poly(A) in vitro in competition with PABP. Biochem J 2006; 400: 337–347. doi:BJ20060328 [pii].
Kiledjian, M, DeMaria, CT, Brewer, G, Novick, K. Identification of AUF1 (heterogeneous nuclear ribonucleoprotein D) as a component of the alpha‐globin mRNA stability complex. Mol Cell Biol 1997; 17: 4870–4876.
Loflin, P, Chen, CY, Shyu, AB. Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU‐rich element. Genes Dev 1999; 13: 1884–1897.
Xu, N, Chen, CY, Shyu, AB. Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover. Mol Cell Biol 2001; 21: 6960–6971. doi:10.1128/MCB.21.20.6960–6971.2001.
Ing, NH, Massuto, DA, Jaeger, LA. Estradiol up‐regulates AUF1p45 binding to stabilizing regions within the 3′‐untranslated region of estrogen receptor alpha mRNA. J Biol Chem 2008; 283: 1764–1772. doi:M704745200 [pii].
Raineri, I, Wegmueller, D, Gross, B, Certa, U, Moroni, C. Roles of AUF1 isoforms, HuR and BRF1 in ARE‐dependent mRNA turnover studied by RNA interference. Nucleic Acids Res 2004; 32: 1279–1288. doi:10.1093/nar/gkh282.
Pioli, PA, Hamilton, BJ, Connolly, JE, Brewer, G, Rigby, WF. Lactate dehydrogenase is an AU‐rich element‐binding protein that directly interacts with AUF1. J Biol Chem 2002; 277: 35738–35745. doi:10.1074/jbc.M204002200.
Eversole, A, Maizels, N. In vitro properties of the conserved mammalian protein hnRNP D suggest a role in telomere maintenance. Mol Cell Biol 2000; 20: 5425–5432.
Enokizono, Y, Konishi, Y, Nagata, K, Ouhashi, K, Uesugi, S, Ishikawa, F, Katahira, M. Structure of hnRNP D complexed with single‐stranded telomere DNA and unfolding of the quadruplex by heterogeneous nuclear ribonucleoprotein D. J Biol Chem 2005; 280: 18862–18870. doi:M411822200 [pii].
Tolnay, M, Baranyi, L, Tsokos, GC. Heterogeneous nuclear ribonucleoprotein D0 contains transactivator and DNA‐binding domains. Biochem J 2000; 348: 151–158.
Hanakahi, LA, Maizels, N. Transcriptional activation by LR1 at the Emu enhancer and switch region sites. Nucleic Acids Res 2000; 28: 2651–2657.
Dempsey, LA, Hanakahi, LA, Maizels, N. A specific isoform of hnRNP D interacts with DNA in the LR1 heterodimer: canonical RNA binding motifs in a sequence‐specific duplex DNA binding protein. J Biol Chem 1998; 273: 29224–29229.
Liao, B, Hu, Y, Brewer, G. Competitive binding of AUF1 and TIAR to MYC mRNA controls its translation. Nat Struct Mol Biol 2007; 14: 511–518. doi:nsmb1249 [pii].
Grosset, C, Chen, CY, Xu, N, Sonenberg, N, Jacquemin‐Sablon, H, Shyu, AB. A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c‐fos RNA coding determinant via a protein complex. Cell 2000; 103: 29–40. doi:S0092‐8674(00)00102‐1 [pii].
Wagner, BJ, Long, L, Rao, PN, Pettenati, MJ, Brewer, G. Localization and physical mapping of genes encoding the A + U‐rich element RNA‐binding protein AUF1 to human chromosomes 4 and X. Genomics 1996; 34: 219–222. doi:S0888‐7543(96)90269‐4 [pii].
Kamei, D, Tsuchiya, N, Yamazaki, M, Meguro, H, Yamada, M. Two forms of expression and genomic structure of the human heterogeneous nuclear ribonucleoprotein D‐like JKTBP gene (HNRPDL). Gene 1999; 228: 13–22.
Ehrenman, K, Long, L, Wagner, BJ, Brewer, G. Characterization of cDNAs encoding the murine A + U‐rich RNA‐binding protein AUF1. Gene 1994; 149: 315–319.
Wagner, BJ, DeMaria, CT, Sun, Y, Wilson, GM, Brewer, G. Structure and genomic organization of the human AUF1 gene: alternative pre‐mRNA splicing generates four protein isoforms. Genomics 1998; 48: 195–202. doi:S0888‐7543(97)95142‐9 [pii].
Buzby, JS, Brewer, G, Nugent, DJ. Developmental regulation of RNA transcript destabilization by A + U‐rich elements is AUF1‐dependent. J Biol Chem 1999; 274: 33973–33978.
Buzby, JS, Lee, SM, Van Winkle, P, DeMaria, CT, Brewer, G, Cairo, MS. Increased granulocyte‐macrophage colony‐stimulating factor mRNA instability in cord versus adult mononuclear cells is translation‐dependent and associated with increased levels of A + U‐rich element binding factor. Blood 1996; 88: 2889–2897.
Sheflin, LG, Spaulding, SW. Testosterone and dihydrotestosterone regulate AUF1 isoforms in a tissue‐specific fashion in the mouse. Am J Physiol Endocrinol Metab 2000; 278:E50–E57.
Nagata, T, Kurihara, Y, Matsuda, G, Saeki, J, Kohno, T, Yanagida, Y, Ishikawa, F, Uesugi, S, Katahira, M. Structure and interactions with RNA of the N‐terminal UUAG‐specific RNA‐binding domain of hnRNP D0. J Mol Biol 1999; 287: 221–237. doi:S0022283699926165 [pii].
Kajita, Y, Nakayama, J, Aizawa, M, Ishikawa, F. The UUAG‐specific RNA binding protein, heterogeneous nuclear ribonucleoprotein D0. Common modular structure and binding properties of the 2xRBD‐Gly family. J Biol Chem 1995; 270: 22167–22175.
Moraes, KC, Lee, WH, Kobarg, J. Analysis of the structural determinants for RNA binding of the human protein AUF1/hnRNP D. Biol Chem 2002; 383: 831–837. doi:10.1515/BC.2002.087.
Wilson, GM, Sun, Y, Sellers, J, Lu, H, Penkar, N, Dillard, G, Brewer, G. Regulation of AUF1 expression via conserved alternatively spliced elements in the 3′ untranslated region. Mol Cell Biol 1999; 19: 4056–4064.
Pullmann, R, Jr. Kim, HH, Abdelmohsen, K, Lal, A, Martindale, JL, Yang, X, Gorospe, M. Analysis of turnover and translation regulatory RNA‐binding protein expression through binding to cognate mRNAs. Mol Cell Biol 2007; 27: 6265–6278. doi:MCB.00500‐07 [pii].
Banihashemi, L, Wilson, GM, Das, N, Brewer, G. Upf1/Upf2 regulation of 3′ untranslated region splice variants of AUF1 links nonsense‐mediated and A + U‐rich element‐mediated mRNA decay. Mol Cell Biol 2006; 26: 8743–8754. doi:MCB.02251‐05 [pii].
Ni, JZ, Grate, L, Donohue, JP, Preston, C, Nobida, N, O`Brien, G, Shiue, L, Clark, TA, Blume, JE, Ares, M, Jr. Ultraconserved elements are associated with homeostatic control of splicing regulators by alternative splicing and nonsense‐mediated decay. Genes Dev 2007; 21: 708–718. doi:21/6/708 [pii].
Sarkar, B, Lu, JY, Schneider, RJ. Nuclear import and export functions in the different isoforms of the AUF1/heterogeneous nuclear ribonucleoprotein protein family. J Biol Chem 2003; 278: 20700–20707. doi: 10.1074/jbc.M301176200.
Weighardt, F, Cobianchi, F, Cartegni, L, Chiodi, I, Villa, A, Riva, S, Biamonti, G. A novel hnRNP protein (HAP/SAF‐B) enters a subset of hnRNP complexes and relocates in nuclear granules in response to heat shock. J Cell Sci 1999; 112: 1465–1476.
Chen, CY, Xu, N, Zhu, W, Shyu, AB. Functional dissection of hnRNP D suggests that nuclear import is required before hnRNP D can modulate mRNA turnover in the cytoplasm. RNA 2004; 10: 669–680.
Suzuki, M, Iijima, M, Nishimura, A, Tomozoe, Y, Kamei, D, Yamada, M. Two separate regions essential for nuclear import of the hnRNP D nucleocytoplasmic shuttling sequence. FEBS J 2005; 272: 3975–3987. doi:EJB4820 [pii].
He, C, Schneider, R. 14‐3‐3sigma is a p37 AUF1‐binding protein that facilitates AUF1 transport and AU‐rich mRNA decay. EMBO J 2006; 25: 3823–3831. doi:7601264 [pii].
Wilson, GM, Lu, J, Sutphen, K, Sun, Y, Huynh, Y, Brewer, G. Regulation of A + U‐rich element‐directed mRNA turnover involving reversible phosphorylation of AUF1. J Biol Chem 2003; 278: 33029–33038. doi:10.1074/jbc.M305772200.
Pomorski, P, Watson, JM, Haskill, S, Jacobson, KA. How adhesion, migration, and cytoplasmic calcium transients influence interleukin‐1beta mRNA stabilization in human monocytes. Cell Motil Cytoskeleton 2004; 57: 143–157. doi:10.1002/ cm.10159.
Sirenko, OI, Lofquist, AK, DeMaria, CT, Morris, JS, Brewer, G, Haskill, JS. Adhesion‐dependent regulation of an A + U‐rich element‐binding activity associated with AUF1. Mol Cell Biol 1997; 17: 3898–3906.
Wilson, GM, Lu, J, Sutphen, K, Suarez, Y, Sinha, S, Brewer, B, Villanueva‐Feliciano, EC, Ysla, RM, Charles, S, Brewer, G. Phosphorylation of p40AUF1 regulates binding to A + U‐rich mRNA‐destabilizing elements and protein‐induced changes in ribonucleoprotein structure. J Biol Chem 2003; 278: 33039–33048. doi:10.1074/jbc.M305775200.
Fawal, M, Armstrong, F, Ollier, S, Dupont, H, Touriol, C, Monsarrat, B, Delsol, G, Payrastre, B, Morello, D. A “liaison dangereuse” between AUF1/hnRNPD and the oncogenic tyrosine kinase NPM‐ALK. Blood 2006; 108: 2780–2788.
Lecker, SH, Goldberg, AL, Mitch, WE. Protein degradation by the ubiquitin‐proteasome pathway in normal and disease states. J Am Soc Nephrol 2006; 17: 1807–1819. doi:ASN.2006010083 [pii].
Laroia, G, Cuesta, R, Brewer, G, Schneider, RJ. Control of mRNA decay by heat shock‐ubiquitin‐proteasome pathway. Science 1999; 284: 499–502.
Wilson, GM, Sutphen, K, Bolikal, S, Chuang, KY, Brewer, G. Thermodynamics and kinetics of Hsp70 association with A + U‐rich mRNA‐destabilizing sequences. J Biol Chem 2001; 276: 44450–44456. doi:10.1074/jbc.M108521200.
Laroia, G, Schneider, RJ. Alternate exon insertion controls selective ubiquitination and degradation of different AUF1 protein isoforms. Nucleic Acids Res 2002; 30: 3052–3058.
Sinsimer, KS, Gratacos, FM, Knapinska, AM, Lu, J, Krause, CD, Wierzbowski, AV, Maher, LR, Scrudato, S, Rivera, YM, Gupta, S, et al. Chaperone Hsp27, a novel subunit of AUF1 protein complexes, functions in AU‐rich element‐mediated mRNA decay. Mol Cell Biol 2008; 28: 5223–5237.
Chen, CY, Gherzi, R, Ong, SE, Chan, EL, Raijmakers, R, Pruijn, GJ, Stoecklin, G, Moroni, C, Mann, M, Karin, M. AU binding proteins recruit the exosome to degrade ARE‐containing mRNAs. Cell 2001; 107: 451–464. doi:S0092‐8674(01)00578‐5 [pii].
Moraes, KC, Quaresma, AJ, Maehnss, K, Kobarg, J. Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D). Biol Chem 2003; 384: 25–37. doi:10.1515/BC.2003.004.
Lu, JY, Bergman, N, Sadri, N, Schneider, RJ. Assembly of AUF1 with eIF4G‐poly(A) binding protein complex suggests a translation function in AU‐rich mRNA decay.RNA 2006 12: 883–893. doi:rna.2308106 [pii].
Bhattacharya, S, Giordano, T, Brewer, G, Malter, JS. Identification of AUF‐1 ligands reveals vast diversity of early response gene mRNAs. Nucleic Acids Res 1999; 27: 1464–1472. doi: gkc281 [pii].
Lu, JY, Sadri, N, Schneider, RJ. Endotoxic shock in AUF1 knockout mice mediated by failure to degrade proinflammatory cytokine mRNAs. Genes Dev 2006; 20: 3174–3184. doi: gad.1467606 [pii].
Sadri, N, Schneider, RJ. Auf1/Hnrnpd‐deficient mice develop pruritic inflammatory skin disease. J Invest Dermatol 2009; 129: 657–670. doi:jid2008298 [pii].
Shen, ZJ, Esnault, S, Malter, JS. The peptidyl‐prolyl isomerase Pin1 regulates the stability of granulocyte‐macrophage colony‐stimulating factor mRNA in activated eosinophils. Nat Immunol 2005; 6: 1280–1287. doi: ni1266 [pii].
Esnault, S, Shen, ZJ, Whitesel, E, Malter, JS. The peptidyl‐prolyl isomerase Pin1 regulates granulocyte‐macrophage colony‐stimulating factor mRNA stability in T lymphocytes. J Immunol 2006; 177: 6999–7006. doi:177/10/6999 [pii].
Gouble, A, Grazide, S, Meggetto, F, Mercier, P, Delsol, G, Morello, D. A new player in oncogenesis: AUF1/hnRNPD overexpression leads to tumorigenesis in transgenic mice. Cancer Res 2002; 62: 1489–1495.
Brewer, G, Saccani, S, Sarkar, S, Lewis, A, Pestka, S, Brewer, G, et al. Increased interleukin‐10 mRNA stability in melanoma cells is associated with decreased levels of A + U‐rich element binding factor AUF1. J Interferon Cytokine Res 2003; 23: 553–564. doi:10.1089/107999003322485053.
Sarkar, S, Sinsimer, KS, Foster, RL, Brewer, G, Pestka, S. AUF1 isoform‐specific regulation of anti‐inflammatory IL10 expression in monocytes. J Interferon Cytokine Res 2008; 28: 679–691. doi: 10.1089/jir.2008.0028.
Woo, KC, Ha, DC, Lee, KH, Kim, DY, Kim, TD, Kim, KT. Circadian amplitude of cryptochrome 1 is modulated by mRNA stability regulation via cytoplasmic hnRNP D oscillation. Mol Cell Biol 2010; 30: 197–205. doi:MCB.01154‐09 [pii].
Pende, A, Tremmel, KD, DeMaria, CT, Blaxall, BC, Minobe, WA, Sherman, JA, Bisognano, JD, Bristow, MR, Brewer, G, Port, J. Regulation of the mRNA‐binding protein AUF1 by activation of the beta‐adrenergic receptor signal transduction pathway. J Biol Chem 1996; 271: 8493–8501.
Pende, A, Giacche, M, Castigliola, L, Contini, L, Passerone, G, Patrone, M, Port, JD, Lotti, G. Characterization of the binding of the RNA‐binding protein AUF1 to the human AT(1) receptor mRNA. Biochem Biophys Res Commun 1999; 266: 609–614. doi:10.1006/bbrc.1999.1862.
Zhou, C, Vignere, CZ, Levitan, ES. AUF1 is upregulated by angiotensin II to destabilize cardiac Kv4.3 channel mRNA. J Mol Cell Cardiol 2008; 45: 832–838. doi:S0022‐2828(08)00573‐7 [pii].
Torrisani, J, Unterberger, A, Tendulkar, SR, Shikimi, K, Szyf, M. AUF1 cell cycle variations define genomic DNA methylation by regulation of DNMT1 mRNA stability. Mol Cell Biol 2007; 27: 395–410. doi:MCB.01236‐06 [pii].
Hajarnis, S, Schroeder, JM, Curthoys, NP. 3′‐Untranslated region of phosphoenolpyruvate carboxykinase mRNA contains multiple instability elements that bind AUF1. J Biol Chem 2005; 280: 28272–28280. doi:M501204200 [pii].
Lapucci, A, Donnini, M, Papucci, L, Witort, E, Tempestini, A, Bevilacqua, A, Nicolin, A, Brewer, G, Schiavone, N, Capaccioli, S. AUF1 Is a bcl‐2 A + U‐rich element‐binding protein involved in bcl‐2 mRNA destabilization during apoptosis. J Biol Chem 2002; 277: 16139–16146. doi:10.1074/jbc.M201377200M201377200 [pii].
Lin, S, Wang, W, Wilson, GM, Yang, X, Brewer, G, Holbrook, NJ, Gorospe, M. Down‐regulation of cyclin D1 expression by prostaglandin A(2) is mediated by enhanced cyclin D1 mRNA turnover. Mol Cell Biol 2000; 20: 7903–7913.
Fuentes‐Panana, EM, Peng, R, Brewer, G, Tan, J, Ling, PD. Regulation of the Epstein‐Barr virus C promoter by AUF1 and the cyclic AMP/protein kinase A signaling pathway. J Virol 2000; 74: 8166–8175.
Sela‐Brown, A, Silver, J, Brewer, G, Naveh‐Many, T. Identification of AUF1 as a parathyroid hormone mRNA 3′‐untranslated region‐binding protein that determines parathyroid hormone mRNA stability. J Biol Chem 2000; 275: 7424–7429.
Tolnay, M, Vereshchagina, LA, Tsokos, GC. Heterogeneous nuclear ribonucleoprotein. D0 is a sequence‐specific DNA‐binding protein. Biochem J 1999; 338: 417–425.
Seymour, RM, Henderson, B. Pro‐inflammatory–anti‐inflammatory cytokine dynamics mediated by cytokine‐receptor dynamics in monocytes. IMA J Math Appl Med Biol 2001; 18: 159–192.
Shchors, K, Yehiely, F, Kular, RK, Kotlo, KU, Brewer, G, Deiss, LP. Cell death inhibiting RNA (CDIR) derived from a 3′‐untranslated region binds AUF1 and heat shock protein 27. J Biol Chem 2002; 277: 47061–47072. doi:10.1074/jbc.M202272200.
Hadcock, JR, Wang, HY, Malbon, CC. Agonist‐induced destabilization of beta‐adrenergic receptor mRNA. Attenuation of glucocorticoid‐induced up‐regulation of beta‐adrenergic receptors. J Biol Chem 1989; 264: 19928–19933.
Cleland, JG. The renin‐angiotensin system in heart failure. Herz 1991; 16: 68–81.
Glaser, ND, Lukyanenko, YO, Wang, Y, Wilson, GM, Rogers, TB. NK activation decreases PP2A regulatory subunit B56alpha expression and mRNA stability and increases AUF1 expression in cardiomyocytes. Am J Physiol Heart Circ Physiol 2006; 291:H1183–H1192. doi:01162.2005 [pii].
Guo, X, Gourronc, F, Audic, Y, Lyons‐Levy, G, Mitchell, T, Hartley, RS. ElrA and AUF1 differentially bind cyclin B2 mRNA. Biochem Biophys Res Commun 2008; 377: 653–657. ISSN:1090–2104 (Electronic). doi:S0006‐291X(08)02002‐0 [pii].
Cameron, EE, Bachman, KE, Myohanen, S, Herman, JG, Baylin, SB. Synergy of demethylation and histone deacetylase inhibition in the re‐expression of genes silenced in cancer. Nat Genet 1999; 21: 103–107. doi:10.1038/5047.
Palmisano, WA, Divine, KK, Saccomanno, G, Gilliland, FD, Baylin, SB, Herman, JG, Belinsky, SA. Predicting lung cancer by detecting aberrant promoter methylation in sputum. Cancer Res 2000; 60: 5954–5958.
Sommer, S, Cui, Y, Brewer, G, Fuqua, SA. The c‐Yes 3′‐UTR contains adenine/uridine‐rich elements that bind AUF1 and HuR involved in mRNA decay in breast cancer cells. J Steroid Biochem Mol Biol 2005; 97: 219–229. doi:S0960‐0760(05)00389‐4 [pii].
Wilson, GM, Brewer, G. Regulation of mRNA stability by AUF1. In: Sandberg, K, Mulroney, SE, eds. RNA Binding Proteins: New Concepts in Gene Regulation, Endocrine Updates, vol. 16. Norwell, MA: Kluwer Academic Publishers; 2002, 101–117.

Further Reading

Wilson, GM, Brewer, G. The search for trans‐acting factors controlling messenger RNA decay. Prog Nucleic Acid Res Mol Biol 1999, 62:257–291.
Naveh‐Many, T, Bell, O, Silver, J, Kilav, R. Cis and trans‐acting factors in the regulation of parathyroid hormone (PTH) mRNA stability by calcium and phosphate. FEBS Lett 2002, 529:60–64. doi:S0014579302032593 [pii].
Misquitta, CM, Chen, T, Grover, AK. Control of protein expression throughmRNA stability in calcium signalling. Cell Calcium 2006, 40:329–346. doi:S0143‐4160(06)00070‐4 [pii].

Resources

FURTHER READING

Wilson GM, Brewer G. The search for trans-acting factors controlling messenger RNA decay. Prog Nucleic Acid Res Mol Biol 1999, 62:257–291.
Naveh-Many T, Bell O, Silver J, Kilav R. Cis and trans-acting factors in the regulation of parathyroid hormone (PTH) mRNA stability by calcium and phosphate. FEBS Lett 2002, 529:60–64. doi:S0014579302032593 [pii].
Misquitta CM, Chen T, Grover AK. Control of protein expression throughmRNA stability in calcium signalling. Cell Calcium 2006, 40:329–346. doi:S0143-4160(06)00070-4 [pii].

Access to this WIREs title is by subscription only.

Recommend to Your
Librarian Now!

The latest WIREs articles in your inbox

Sign Up for Article Alerts