TOB1

Transducer of ERBB2, 1

PDB rendering based on 2d5r.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols TOB1 ; APRO6; PIG49; TOB; TROB; TROB1
External IDs OMIM: 605523 MGI: 1349721 HomoloGene: 31334 GeneCards: TOB1 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 10140 22057
Ensembl ENSG00000141232 ENSMUSG00000037573
UniProt P50616 Q61471
RefSeq (mRNA) NM_001243877 NM_009427
RefSeq (protein) NP_001230806 NP_033453
Location (UCSC) Chr 17:
50.86 – 50.87 Mb		 Chr 11:
94.21 – 94.22 Mb
PubMed search

Protein Tob1 is a protein that in humans is encoded by the TOB1 gene.[1][2][3]

Function

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 suppresses cell growth in tissue culture. The protein undergoes phosphorylation 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:

References

  1. ↑ Matsuda S, Kawamura-Tsuzuku J, Ohsugi M, Yoshida M, Emi M, Nakamura Y, Onda M, Yoshida Y, Nishiyama A, Yamamoto T (Feb 1996). "Tob, a novel protein that interacts with p185erbB2, is associated with anti-proliferative activity". Oncogene 12 (4): 705–13. PMID 8632892.
  2. ↑ Ezzeddine N, Chang TC, Zhu W, Yamashita A, Chen CY, Zhong Z, Yamashita Y, Zheng D, Shyu AB (Nov 2007). "Human TOB, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation". Molecular and Cellular Biology 27 (22): 7791–801. doi:10.1128/MCB.01254-07. PMC 2169145. PMID 17785442.
  3. 1 2 "Entrez Gene: TOB1 transducer of ERBB2, 1".
  4. ↑ Funakoshi Y, Doi Y, Hosoda N, Uchida N, Osawa M, Shimada I, Tsujimoto M, Suzuki T, Katada T, Hoshino S (Dec 2007). "Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases". Genes & Development 21 (23): 3135–48. doi:10.1101/gad.1597707. PMC 2081979. PMID 18056425.
  5. ↑ 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 18 (52): 7432–41. doi:10.1038/sj.onc.1203193. PMID 10602502.
  6. 1 2 Maekawa M, Nishida E, Tanoue T (Oct 2002). "Identification of the Anti-proliferative protein Tob as a MAPK substrate". The Journal of Biological Chemistry 277 (40): 37783–7. doi:10.1074/jbc.M204506200. PMID 12151396.
  7. ↑ Jin Cho S, La M, Ahn JK, Meadows GG, Joe CO (May 2001). "Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation". Biochemical and Biophysical Research Communications 283 (2): 273–7. doi:10.1006/bbrc.2001.4773. PMID 11327693.
  8. ↑ Suzuki T, Matsuda S, Tsuzuku JK, Yoshida Y, Yamamoto T (Feb 2001). "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob". Genes to Cells 6 (2): 131–8. PMID 11260258.

Further reading

  • Sasaki S, Imai K (Mar 2002). "[Monoclonal antibody induces apoptosis against cancer cells]". Nihon Rinsho. Japanese Journal of Clinical Medicine 60 (3): 451–6. PMID 11904957. 
  • Yoshida Y, Matsuda S, Yamamoto T (May 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, 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 18 (52): 7432–41. doi:10.1038/sj.onc.1203193. PMID 10602502. 
  • Yoshida Y, Tanaka S, Umemori H, Minowa O, Usui M, Ikematsu N, Hosoda E, Imamura T, Kuno J, Yamashita T, Miyazono K, Noda M, Noda T, Yamamoto T (Dec 2000). "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, Yoshida Y, Yamamoto T (Feb 2001). "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob". Genes to Cells 6 (2): 131–8. doi:10.1046/j.1365-2443.2001.00406.x. PMID 11260258. 
  • Jin Cho S, La M, Ahn JK, Meadows GG, Joe CO (May 2001). "Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation". Biochemical and Biophysical Research Communications 283 (2): 273–7. doi:10.1006/bbrc.2001.4773. PMID 11327693. 
  • Yoshida Y, Hosoda E, Nakamura T, Yamamoto T (Jun 2001). "Association of ANA, a member of the antiproliferative Tob family proteins, with a Caf1 component of the CCR4 transcriptional regulatory complex". Japanese Journal of Cancer Research 92 (6): 592–6. doi:10.1111/j.1349-7006.2001.tb01135.x. PMID 11429045. 
  • Tzachanis D, Freeman GJ, Hirano N, van Puijenbroek AA, Delfs MW, Berezovskaya A, Nadler LM, Boussiotis VA (Dec 2001). "Tob is a negative regulator of activation that is expressed in anergic and quiescent T cells". Nature Immunology 2 (12): 1174–82. doi:10.1038/ni730. PMID 11694881. 
  • Suzuki T, K-Tsuzuku J, Ajima R, Nakamura T, Yoshida Y, Yamamoto T (Jun 2002). "Phosphorylation of three regulatory serines of Tob by Erk1 and Erk2 is required for Ras-mediated cell proliferation and transformation". Genes & Development 16 (11): 1356–70. doi:10.1101/gad.962802. PMC 186319. PMID 12050114. 
  • Sasajima H, Nakagawa K, Yokosawa H (Jul 2002). "Antiproliferative proteins of the BTG/Tob family are degraded by the ubiquitin-proteasome system". European Journal of Biochemistry / FEBS 269 (14): 3596–604. doi:10.1046/j.1432-1033.2002.03052.x. PMID 12135500. 
  • Maekawa M, Nishida E, Tanoue T (Oct 2002). "Identification of the Anti-proliferative protein Tob as a MAPK substrate". The Journal of Biological Chemistry 277 (40): 37783–7. doi:10.1074/jbc.M204506200. PMID 12151396. 
  • Yoshida Y, von Bubnoff A, Ikematsu N, Blitz IL, Tsuzuku JK, Yoshida EH, Umemori H, Miyazono K, Yamamoto T, Cho KW (May 2003). "Tob proteins enhance inhibitory Smad-receptor interactions to repress BMP signaling". Mechanisms of Development 120 (5): 629–37. doi:10.1016/S0925-4773(03)00020-0. PMID 12782279. 
  • Iwanaga K, Sueoka N, Sato A, Sakuragi T, Sakao Y, Tominaga M, Suzuki T, Yoshida Y, K-Tsuzuku J, Yamamoto T, Hayashi S, Nagasawa K, Sueoka E (Dec 2003). "Alteration of expression or phosphorylation status of tob, a novel tumor suppressor gene product, is an early event in lung cancer". Cancer Letters 202 (1): 71–9. doi:10.1016/j.canlet.2003.08.019. PMID 14643028. 
  • Maekawa M, Yamamoto T, Nishida E (Apr 2004). "Regulation of subcellular localization of the antiproliferative protein Tob by its nuclear export signal and bipartite nuclear localization signal sequences". Experimental Cell Research 295 (1): 59–65. doi:10.1016/j.yexcr.2003.12.016. PMID 15051490. 
  • Kawamura-Tsuzuku J, Suzuki T, Yoshida Y, Yamamoto T (Aug 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. 
  • Okochi K, Suzuki T, Inoue J, Matsuda S, Yamamoto T (Feb 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 to Cells 10 (2): 151–63. doi:10.1111/j.1365-2443.2005.00826.x. PMID 15676026. 

External links

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