Tgif1 and Tgif2 Repress Expression of the RabGAP Evi5l

REFERENCES

• Bertolino E, Reimund B, Wildt-Perinic D, Clerc R. 1995. A novel homeobox protein which recognizes a TGT core and functionally interferes with a retinoid-responsive motif. J Biol Chem 270:31178–31188. https://doi.org/10.1074/jbc.270.52.31178.
   PubMed Web of Science ®Google Scholar
• Hyman CA, Bartholin L, Newfeld SJ, Wotton D. 2003. Drosophila TGIF proteins are transcriptional activators. Mol Cell Biol 23:9262–9274. https://doi.org/10.1128/MCB.23.24.9262-9274.2003.
   PubMedGoogle Scholar
• Melhuish TA, Gallo CM, Wotton D. 2001. TGIF2 interacts with histone deacetylase 1 and represses transcription. J Biol Chem 276:32109–32114. https://doi.org/10.1074/jbc.M103377200.
   PubMed Web of Science ®Google Scholar
• Wotton D, Lo RS, Swaby LA, Massague J. 1999. Multiple modes of repression by the smad transcriptional corepressor TGIF. J Biol Chem 274:37105–37110. https://doi.org/10.1074/jbc.274.52.37105.
   PubMedGoogle Scholar
• Wotton D, Lo RS, Lee S, Massague J. 1999. A Smad transcriptional corepressor. Cell 97:29–39. https://doi.org/10.1016/S0092-8674(00)80712-6.
   PubMed Web of Science ®Google Scholar
• Zerlanko BJ, Bartholin L, Melhuish TA, Wotton D. 2012. Premature senescence and increased TGFbeta signaling in the absence of Tgif1. PLoS One 7:e35460. https://doi.org/10.1371/journal.pone.0035460.
   PubMed Web of Science ®Google Scholar
• Heldin C-H, Miyazono K, ten Dijke P. 1997. TGF-β signalling from cell membrane to nucleus through SMAD proteins. Nature 390:465–471. https://doi.org/10.1038/37284.
   PubMed Web of Science ®Google Scholar
• Massague J, Seoane J, Wotton D. 2005. Smad transcription factors. Genes Dev 19:2783–2810. https://doi.org/10.1101/gad.1350705.
   PubMed Web of Science ®Google Scholar
• Schmierer B, Hill CS. 2007. TGFbeta-SMAD signal transduction: molecular specificity and functional flexibility. Nat Rev Mol Cell Biol 8:970–982. https://doi.org/10.1038/nrm2297.
   PubMed Web of Science ®Google Scholar
• Melhuish TA, Wotton D. 2000. The interaction of C-terminal binding protein with the Smad corepressor TG-interacting factor is disrupted by a holoprosencephaly mutation in TGIF. J Biol Chem 275:39762–39766. https://doi.org/10.1074/jbc.C000416200.
   PubMed Web of Science ®Google Scholar
• Melhuish TA, Wotton D. 2006. The Tgif2 gene contains a retained intron within the coding sequence. BMC Mol Biol 7:2. https://doi.org/10.1186/1471-2199-7-2.
   PubMedGoogle Scholar
• Wotton D, Knoepfler PS, Laherty CD, Eisenman RN, Massague J. 2001. The Smad transcriptional corepressor TGIF recruits mSin3. Cell Growth Differ 12:457–463.
   PubMedGoogle Scholar
• Seo SR, Ferrand N, Faresse N, Prunier C, Abecassis L, Pessah M, Bourgeade MF, Atfi A. 2006. Nuclear retention of the tumor suppressor cPML by the homeodomain protein TGIF restricts TGF-beta signaling. Mol Cell 23:547–559. https://doi.org/10.1016/j.molcel.2006.06.018.
   PubMedGoogle Scholar
• Seo SR, Lallemand F, Ferrand N, Pessah M, L'Hoste S, Camonis J, Atfi A. 2004. The novel E3 ubiquitin ligase Tiul1 associates with TGIF to target Smad2 for degradation. EMBO J 23:3780–3792. https://doi.org/10.1038/sj.emboj.7600398.
   PubMed Web of Science ®Google Scholar
• Bartholin L, Powers SE, Melhuish TA, Lasse S, Weinstein M, Wotton D. 2006. TGIF inhibits retinoid signaling. Mol Cell Biol 26:990–1001. https://doi.org/10.1128/MCB.26.3.990-1001.2006.
   PubMed Web of Science ®Google Scholar
• Melhuish TA, Chung DD, Bjerke GA, Wotton D. 2010. Tgif1 represses apolipoprotein gene expression in liver. J Cell Biochem 111:380–390. https://doi.org/10.1002/jcb.22713.
   PubMedGoogle Scholar
• Pramfalk C, Melhuish TA, Wotton D, Jiang ZY, Eriksson M, Parini P. 2014. TG-interacting factor 1 acts as a transcriptional repressor of sterol O-acyltransferase 2. J Lipid Res 55:709–717. https://doi.org/10.1194/jlr.M045922.
   PubMedGoogle Scholar
• Yang Y, Hwang CK, D'Souza UM, Lee SH, Junn E, Mouradian MM. 2000. Tale homeodomain proteins Meis2 and TGIF differentially regulate transcription. J Biol Chem 275:20734–20741. https://doi.org/10.1074/jbc.M908382199.
   PubMed Web of Science ®Google Scholar
• Lee BK, Shen W, Lee J, Rhee C, Chung H, Kim KY, Park IH, Kim J. 2015. Tgif1 counterbalances the activity of core pluripotency factors in mouse embryonic stem cells. Cell Rep 13:52–60. https://doi.org/10.1016/j.celrep.2015.08.067.
   PubMedGoogle Scholar
• Geng X, Oliver G. 2009. Pathogenesis of holoprosencephaly. J Clin Invest 119:1403–1413. https://doi.org/10.1172/JCI38937.
   PubMedGoogle Scholar
• Gripp KW, Wotton D, Edwards MC, Roessler E, Ades L, Meinecke P, Richieri-Costa A, Zackai EH, Massague J, Muenke M, Elledge SJ. 2000. Mutations in TGIF cause holoprosencephaly and link NODAL signalling to human neural axis determination. Nat Genet 25:205–208. https://doi.org/10.1038/76074.
   PubMedGoogle Scholar
• Muenke M, Beachy PA. 2001. Holoprosencephaly, p 6203–6230. InScriver CR (ed), The metabolic and molecular bases of inherited disease. McGraw-Hill, New York, NY.
   Google Scholar
• Jin JZ, Gu S, McKinney P, Ding J. 2006. Expression and functional analysis of Tgif during mouse midline development. Dev Dyn 235:547–553. https://doi.org/10.1002/dvdy.20642.
   PubMedGoogle Scholar
• Mar L, Hoodless PA. 2006. Embryonic fibroblasts from mice lacking Tgif were defective in cell cycling. Mol Cell Biol 26:4302–4310. https://doi.org/10.1128/MCB.02156-05.
   PubMedGoogle Scholar
• Shen J, Walsh CA. 2005. Targeted disruption of Tgif, the mouse ortholog of a human holoprosencephaly gene, does not result in holoprosencephaly in mice. Mol Cell Biol 25:3639–3647. https://doi.org/10.1128/MCB.25.9.3639-3647.2005.
   PubMedGoogle Scholar
• Powers SE, Taniguchi K, Yen W, Melhuish TA, Shen J, Walsh CA, Sutherland AE, Wotton D. 2010. Tgif1 and Tgif2 regulate Nodal signaling and are required for gastrulation. Development 137:249–259. https://doi.org/10.1242/dev.040782.
   PubMedGoogle Scholar
• Taniguchi K, Anderson AE, Sutherland AE, Wotton D. 2012. Loss of Tgif function causes holoprosencephaly by disrupting the Shh signaling pathway. PLoS Genet 8:e1002524. https://doi.org/10.1371/journal.pgen.1002524.
   PubMedGoogle Scholar
• Kim S, Dynlacht BD. 2013. Assembling a primary cilium. Curr Opin Cell Biol 25:506–511. https://doi.org/10.1016/j.ceb.2013.04.011.
   PubMedGoogle Scholar
• Plotnikova OV, Pugacheva EN, Golemis EA. 2009. Primary cilia and the cell cycle. Methods Cell Biol 94:137–160. https://doi.org/10.1016/S0091-679X(08)94007-3.
   PubMed Web of Science ®Google Scholar
• Goetz SC, Anderson KV. 2010. The primary cilium: a signalling centre during vertebrate development. Nat Rev Genet 11:331–344. https://doi.org/10.1038/nrg2774.
   PubMed Web of Science ®Google Scholar
• Pedersen LB, Rosenbaum JL. 2008. Intraflagellar transport (IFT) role in ciliary assembly, resorption and signalling. Curr Top Dev Biol 85:23–61. https://doi.org/10.1016/S0070-2153(08)00802-8.
   PubMed Web of Science ®Google Scholar
• Huangfu D, Liu A, Rakeman AS, Murcia NS, Niswander L, Anderson KV. 2003. Hedgehog signalling in the mouse requires intraflagellar transport proteins. Nature 426:83–87. https://doi.org/10.1038/nature02061.
   PubMed Web of Science ®Google Scholar
• Corbit KC, Aanstad P, Singla V, Norman AR, Stainier DY, Reiter JF. 2005. Vertebrate Smoothened functions at the primary cilium. Nature 437:1018–1021. https://doi.org/10.1038/nature04117.
   PubMed Web of Science ®Google Scholar
• Haycraft CJ, Banizs B, Aydin-Son Y, Zhang Q, Michaud EJ, Yoder BK. 2005. Gli2 and Gli3 localize to cilia and require the intraflagellar transport protein polaris for processing and function. PLoS Genet 1:e53. https://doi.org/10.1371/journal.pgen.0010053.
   PubMed Web of Science ®Google Scholar
• Rohatgi R, Milenkovic L, Scott MP. 2007. Patched1 regulates hedgehog signaling at the primary cilium. Science 317:372–376. https://doi.org/10.1126/science.1139740.
   PubMed Web of Science ®Google Scholar
• Yoshimura S, Egerer J, Fuchs E, Haas AK, Barr FA. 2007. Functional dissection of Rab GTPases involved in primary cilium formation. J Cell Biol 178:363–369. https://doi.org/10.1083/jcb.200703047.
   PubMed Web of Science ®Google Scholar
• van Dam TJ, Wheway G, Slaats GG, SYSCILIA Study Group, Huynen MA, Giles RH. 2013. The SYSCILIA gold standard (SCGSv1) of known ciliary components and its applications within a systems biology consortium. Cilia 2:7. https://doi.org/10.1186/2046-2530-2-7.
   PubMedGoogle Scholar
• Garcia-Gonzalo FR, Reiter JF. 2012. Scoring a backstage pass: mechanisms of ciliogenesis and ciliary access. J Cell Biol 197:697–709. https://doi.org/10.1083/jcb.201111146.
   PubMed Web of Science ®Google Scholar
• Sung CH, Leroux MR. 2013. The roles of evolutionarily conserved functional modules in cilia-related trafficking. Nat Cell Biol 15:1387–1397. https://doi.org/10.1038/ncb2888.
   PubMed Web of Science ®Google Scholar
• Cho Y, Cavalli V. 2012. HDAC5 is a novel injury-regulated tubulin deacetylase controlling axon regeneration. EMBO J 31:3063–3078. https://doi.org/10.1038/emboj.2012.160.
   PubMed Web of Science ®Google Scholar
• North BJ, Marshall BL, Borra MT, Denu JM, Verdin E. 2003. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 11:437–444. https://doi.org/10.1016/S1097-2765(03)00038-8.
   PubMed Web of Science ®Google Scholar
• Niwa S, Nakajima K, Miki H, Minato Y, Wang D, Hirokawa N. 2012. KIF19A is a microtubule-depolymerizing kinesin for ciliary length control. Dev Cell 23:1167–1175. https://doi.org/10.1016/j.devcel.2012.10.016.
   PubMedGoogle Scholar
• Shiratori H, Hamada H. 2006. The left-right axis in the mouse: from origin to morphology. Development 133:2095–2104. https://doi.org/10.1242/dev.02384.
   PubMedGoogle Scholar
• Vandenberg LN, Levin M. 2013. A unified model for left-right asymmetry? Comparison and synthesis of molecular models of embryonic laterality. Dev Biol 379:1–15. https://doi.org/10.1016/j.ydbio.2013.03.021.
   PubMed Web of Science ®Google Scholar
• Boehlke C, Bashkurov M, Buescher A, Krick T, John AK, Nitschke R, Walz G, Kuehn EW. 2010. Differential role of Rab proteins in ciliary trafficking: Rab23 regulates smoothened levels. J Cell Sci 123:1460–1467. https://doi.org/10.1242/jcs.058883.
   PubMed Web of Science ®Google Scholar
• Eggenschwiler JT, Bulgakov OV, Qin J, Li T, Anderson KV. 2006. Mouse Rab23 regulates Hedgehog signaling from smoothened to Gli proteins. Dev Biol 290:1–12. https://doi.org/10.1016/j.ydbio.2005.09.022.
   PubMedGoogle Scholar
• Fuller K, O'Connell JT, Gordon J, Mauti O, Eggenschwiler J. 2014. Rab23 regulates Nodal signaling in vertebrate left-right patterning independently of the Hedgehog pathway. Dev Biol 391:182–195. https://doi.org/10.1016/j.ydbio.2014.04.012.
   PubMed Web of Science ®Google Scholar
• Hayashi S, Lewis P, Pevny L, McMahon AP. 2002. Efficient gene modulation in mouse epiblast using a Sox2Cre transgenic mouse strain. Mech Dev 119(Suppl 1):S97–S101. https://doi.org/10.1016/S0925-4773(03)00099-6.
   PubMedGoogle Scholar
• Truett GE, Heeger P, Mynatt RL, Truett AA, Walker JA, Warman ML. 2000. Preparation of PCR-quality mouse genomic DNA with hot sodium hydroxide and tris (HotSHOT). Biotechniques 29:52–54.
   PubMed Web of Science ®Google Scholar
• Dobin A, Davis CA, Schlesinger F, Drenkow J, Zaleski C, Jha S, Batut P, Chaisson M, Gingeras TR. 2013. STAR: ultrafast universal RNA-seq aligner. Bioinformatics 29:15–21. https://doi.org/10.1093/bioinformatics/bts635.
   PubMed Web of Science ®Google Scholar
• Liao Y, Smyth GK, Shi W. 2014. featureCounts: an efficient general purpose program for assigning sequence reads to genomic features. Bioinformatics 30:923–930. https://doi.org/10.1093/bioinformatics/btt656.
   PubMed Web of Science ®Google Scholar
• Love MI, Huber W, Anders S. 2014. Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2. Genome Biol 15:550. https://doi.org/10.1186/s13059-014-0550-8.
   PubMed Web of Science ®Google Scholar
• Huang da W, Sherman BT, Lempicki RA. 2009. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 4:44–57. https://doi.org/10.1038/nprot.2008.211.
   PubMed Web of Science ®Google Scholar
• Huang da W, Sherman BT, Lempicki RA. 2009. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res 37:1–13. https://doi.org/10.1093/nar/gkn923.
   PubMed Web of Science ®Google Scholar
• Newman AM, Cooper JB. 2010. AutoSOME: a clustering method for identifying gene expression modules without prior knowledge of cluster number. BMC Bioinformatics 11:117. https://doi.org/10.1186/1471-2105-11-117.
   PubMedGoogle Scholar
• Bjerke GA, Hyman-Walsh C, Wotton D. 2011. Cooperative transcriptional activation by Klf4, Meis2, and Pbx1. Mol Cell Biol 31:3723–3733. https://doi.org/10.1128/MCB.01456-10.
   PubMedGoogle Scholar