TOB1
Protein Tob1 is a protein that in humans is encoded by the TOB1 gene.[1][2][3]
This gene encodes a member of the tob/btg1 family of anti-proliferative proteins that have the potential to regulate cell growth. When exogenously expressed, this protein supresses cell growth in tissue culture. The protein undergoes phophorylation by a serine/threonine kinase, 90 kDa ribosomal S6 kinase. Interactions of this protein with the v-erb-b2 erythroblastic leukemia viral oncogene homolog 2 gene product p185 interferes with growth suppression. This protein inhibits T cell proliferation and transcription of cytokines and cyclins. The protein interacts with both mothers against decapentaplegic Drosophila homolog 2 and 4 to enhance their DNA binding activity. This interaction inhibits interleukin 2 transcription in T cells.[3]
Interactions
TOB1 has been shown to interact with MARCKS,[4] RPS6KA1,[5] CNOT7,[6][7] MAPK1[8] and Mitogen-activated protein kinase 9.[8]
References
- ^ Matsuda S, Kawamura-Tsuzuku J, Ohsugi M, Yoshida M, Emi M, Nakamura Y, Onda M, Yoshida Y, Nishiyama A, Yamamoto T (Jul 1996). "Tob, a novel protein that interacts with p185erbB2, is associated with anti-proliferative activity". Oncogene 12 (4): 705–13. PMID 8632892.
- ^ Ezzeddine N, Chang TC, Zhu W, Yamashita A, Chen CY, Zhong Z, Yamashita Y, Zheng D, Shyu AB (Oct 2007). "Human TOB, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation". Mol Cell Biol 27 (22): 7791–801. doi:10.1128/MCB.01254-07. PMC 2169145. PMID 17785442. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2169145.
- ^ a b "Entrez Gene: TOB1 transducer of ERBB2, 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10140.
- ^ Jin Cho, S; La M, Ahn J K, Meadows G G, Joe C O (May. 2001). "Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation". Biochem. Biophys. Res. Commun. (United States) 283 (2): 273–7. doi:10.1006/bbrc.2001.4773. ISSN 0006-291X. PMID 11327693.
- ^ Suzuki, T; Matsuda S, Tsuzuku J K, Yoshida Y, Yamamoto T (Feb. 2001). "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob". Genes Cells (England) 6 (2): 131–8. doi:10.1046/j.1365-2443.2001.00406.x. ISSN 1356-9597. PMID 11260258.
- ^ Funakoshi, Yuji; Doi Yusuke, Hosoda Nao, Uchida Naoyuki, Osawa Masanori, Shimada Ichio, Tsujimoto Masafumi, Suzuki Tsutomu, Katada Toshiaki, Hoshino Shin-ichi (Dec. 2007). "Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases". Genes Dev. (United States) 21 (23): 3135–48. doi:10.1101/gad.1597707. ISSN 0890-9369. PMC 2081979. PMID 18056425. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2081979.
- ^ Ikematsu, N; Yoshida Y, Kawamura-Tsuzuku J, Ohsugi M, Onda M, Hirai M, Fujimoto J, Yamamoto T (Dec. 1999). "Tob2, a novel anti-proliferative Tob/BTG1 family member, associates with a component of the CCR4 transcriptional regulatory complex capable of binding cyclin-dependent kinases". Oncogene (ENGLAND) 18 (52): 7432–41. doi:10.1038/sj.onc.1203193. ISSN 0950-9232. PMID 10602502.
- ^ a b Maekawa, Momoko; Nishida Eisuke, Tanoue Takuji (Oct. 2002). "Identification of the Anti-proliferative protein Tob as a MAPK substrate". J. Biol. Chem. (United States) 277 (40): 37783–7. doi:10.1074/jbc.M204506200. ISSN 0021-9258. PMID 12151396.
Further reading
- Sasaki S, Imai K (2002). "[Monoclonal antibody induces apoptosis against cancer cells]". Nippon Rinsho 60 (3): 451–6. PMID 11904957.
- Yoshida Y, Matsuda S, Yamamoto T (1997). "Cloning and characterization of the mouse tob gene.". Gene 191 (1): 109–13. doi:10.1016/S0378-1119(97)00049-8. PMID 9210596.
- Ikematsu N, Yoshida Y, Kawamura-Tsuzuku J, et al. (2000). "Tob2, a novel anti-proliferative Tob/BTG1 family member, associates with a component of the CCR4 transcriptional regulatory complex capable of binding cyclin-dependent kinases.". Oncogene 18 (52): 7432–41. doi:10.1038/sj.onc.1203193. PMID 10602502.
- Yoshida Y, Tanaka S, Umemori H, et al. (2001). "Negative regulation of BMP/Smad signaling by Tob in osteoblasts.". Cell 103 (7): 1085–97. doi:10.1016/S0092-8674(00)00211-7. PMID 11163184.
- Suzuki T, Matsuda S, Tsuzuku JK, et al. (2001). "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob.". Genes Cells 6 (2): 131–8. doi:10.1046/j.1365-2443.2001.00406.x. PMID 11260258.
- Jin Cho S, La M, Ahn JK, et al. (2001). "Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation.". Biochem. Biophys. Res. Commun. 283 (2): 273–7. doi:10.1006/bbrc.2001.4773. PMID 11327693.
- Yoshida Y, Hosoda E, Nakamura T, Yamamoto T (2001). "Association of ANA, a member of the antiproliferative Tob family proteins, with a Caf1 component of the CCR4 transcriptional regulatory complex.". Jpn. J. Cancer Res. 92 (6): 592–6. doi:10.1111/j.1349-7006.2001.tb01135.x. PMID 11429045.
- Tzachanis D, Freeman GJ, Hirano N, et al. (2001). "Tob is a negative regulator of activation that is expressed in anergic and quiescent T cells.". Nat. Immunol. 2 (12): 1174–82. doi:10.1038/ni730. PMID 11694881.
- Suzuki T, K-Tsuzuku J, Ajima R, et al. (2002). "Phosphorylation of three regulatory serines of Tob by Erk1 and Erk2 is required for Ras-mediated cell proliferation and transformation.". Genes Dev. 16 (11): 1356–70. doi:10.1101/gad.962802. PMC 186319. PMID 12050114. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=186319.
- Sasajima H, Nakagawa K, Yokosawa H (2002). "Antiproliferative proteins of the BTG/Tob family are degraded by the ubiquitin-proteasome system.". Eur. J. Biochem. 269 (14): 3596–604. doi:10.1046/j.1432-1033.2002.03052.x. PMID 12135500.
- Maekawa M, Nishida E, Tanoue T (2002). "Identification of the Anti-proliferative protein Tob as a MAPK substrate.". J. Biol. Chem. 277 (40): 37783–7. doi:10.1074/jbc.M204506200. PMID 12151396.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Yoshida Y, von Bubnoff A, Ikematsu N, et al. (2004). "Tob proteins enhance inhibitory Smad-receptor interactions to repress BMP signaling.". Mech. Dev. 120 (5): 629–37. doi:10.1016/S0925-4773(03)00020-0. PMID 12782279.
- Iwanaga K, Sueoka N, Sato A, et al. (2004). "Alteration of expression or phosphorylation status of tob, a novel tumor suppressor gene product, is an early event in lung cancer.". Cancer Lett. 202 (1): 71–9. doi:10.1016/j.canlet.2003.08.019. PMID 14643028.
- Maekawa M, Yamamoto T, Nishida E (2004). "Regulation of subcellular localization of the antiproliferative protein Tob by its nuclear export signal and bipartite nuclear localization signal sequences.". Exp. Cell Res. 295 (1): 59–65. doi:10.1016/j.yexcr.2003.12.016. PMID 15051490.
- Kawamura-Tsuzuku J, Suzuki T, Yoshida Y, Yamamoto T (2004). "Nuclear localization of Tob is important for regulation of its antiproliferative activity.". Oncogene 23 (39): 6630–8. doi:10.1038/sj.onc.1207890. PMID 15235587.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Okochi K, Suzuki T, Inoue J, et al. (2005). "Interaction of anti-proliferative protein Tob with poly(A)-binding protein and inducible poly(A)-binding protein: implication of Tob in translational control.". Genes Cells 10 (2): 151–63. doi:10.1111/j.1365-2443.2005.00826.x. PMID 15676026.
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PDB gallery
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2d5r: Crystal Structure of a Tob-hCaf1 Complex
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