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{{ | '''Protein Tob1''' is a [[protein]] that in humans is encoded by the ''TOB1'' [[gene]].<ref name="pmid8632892">{{cite journal | vauthors = Matsuda S, Kawamura-Tsuzuku J, Ohsugi M, Yoshida M, Emi M, Nakamura Y, Onda M, Yoshida Y, Nishiyama A, Yamamoto T | title = Tob, a novel protein that interacts with p185erbB2, is associated with anti-proliferative activity | journal = Oncogene | volume = 12 | issue = 4 | pages = 705–13 | date = Feb 1996 | pmid = 8632892 | pmc = | doi = }}</ref><ref name="pmid17785442">{{cite journal | vauthors = Ezzeddine N, Chang TC, Zhu W, Yamashita A, Chen CY, Zhong Z, Yamashita Y, Zheng D, Shyu AB | title = Human TOB, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation | journal = Molecular and Cellular Biology | volume = 27 | issue = 22 | pages = 7791–801 | date = Nov 2007 | pmid = 17785442 | pmc = 2169145 | doi = 10.1128/MCB.01254-07 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TOB1 transducer of ERBB2, 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10140| accessdate = }}</ref> | ||
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== 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.<ref name="entrez"/> | |||
== | == Interactions == | ||
{{protein- | TOB1 has been shown to [[Protein-protein interaction|interact]] with: | ||
{{ | * [[CNOT7]],<ref name = pmid18056425>{{cite journal | vauthors = Funakoshi Y, Doi Y, Hosoda N, Uchida N, Osawa M, Shimada I, Tsujimoto M, Suzuki T, Katada T, Hoshino S | title = Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases | journal = Genes & Development | volume = 21 | issue = 23 | pages = 3135–48 | date = Dec 2007 | pmid = 18056425 | pmc = 2081979 | doi = 10.1101/gad.1597707 }}</ref><ref name = pmid10602502>{{cite journal | vauthors = Ikematsu N, Yoshida Y, Kawamura-Tsuzuku J, Ohsugi M, Onda M, Hirai M, Fujimoto J, Yamamoto T | title = 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 | journal = Oncogene | volume = 18 | issue = 52 | pages = 7432–41 | date = Dec 1999 | pmid = 10602502 | doi = 10.1038/sj.onc.1203193 }}</ref> | ||
* [[MAPK1]]<ref name = pmid12151396>{{cite journal | vauthors = Maekawa M, Nishida E, Tanoue T | title = Identification of the Anti-proliferative protein Tob as a MAPK substrate | journal = The Journal of Biological Chemistry | volume = 277 | issue = 40 | pages = 37783–7 | date = Oct 2002 | pmid = 12151396 | doi = 10.1074/jbc.M204506200 }}</ref> | |||
* [[MARCKS]],<ref name = pmid11327693>{{cite journal | vauthors = Jin Cho S, La M, Ahn JK, Meadows GG, Joe CO | title = Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation | journal = Biochemical and Biophysical Research Communications | volume = 283 | issue = 2 | pages = 273–7 | date = May 2001 | pmid = 11327693 | doi = 10.1006/bbrc.2001.4773 }}</ref> | |||
* [[Mitogen-activated protein kinase 9]],<ref name = pmid12151396/> and | |||
* [[RPS6KA1]].<ref name = pmid11260258>{{cite journal | vauthors = Suzuki T, Matsuda S, Tsuzuku JK, Yoshida Y, Yamamoto T | title = A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob | journal = Genes to Cells | volume = 6 | issue = 2 | pages = 131–8 | date = Feb 2001 | pmid = 11260258 | doi = 10.1046/j.1365-2443.2001.00406.x}}</ref> | |||
== References == | |||
{{Reflist}} | |||
== Further reading == | |||
{{Refbegin | 2}} | |||
* {{cite journal | vauthors = Sasaki S, Imai K | title = [Monoclonal antibody induces apoptosis against cancer cells] | journal = Nihon Rinsho. Japanese Journal of Clinical Medicine | volume = 60 | issue = 3 | pages = 451–6 | date = Mar 2002 | pmid = 11904957 | doi = }} | |||
* {{cite journal | vauthors = Yoshida Y, Matsuda S, Yamamoto T | title = Cloning and characterization of the mouse tob gene | journal = Gene | volume = 191 | issue = 1 | pages = 109–13 | date = May 1997 | pmid = 9210596 | doi = 10.1016/S0378-1119(97)00049-8 }} | |||
* {{cite journal | vauthors = Ikematsu N, Yoshida Y, Kawamura-Tsuzuku J, Ohsugi M, Onda M, Hirai M, Fujimoto J, Yamamoto T | title = 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 | journal = Oncogene | volume = 18 | issue = 52 | pages = 7432–41 | date = Dec 1999 | pmid = 10602502 | doi = 10.1038/sj.onc.1203193 }} | |||
* {{cite journal | vauthors = 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 | title = Negative regulation of BMP/Smad signaling by Tob in osteoblasts | journal = Cell | volume = 103 | issue = 7 | pages = 1085–97 | date = Dec 2000 | pmid = 11163184 | doi = 10.1016/S0092-8674(00)00211-7 }} | |||
* {{cite journal | vauthors = Suzuki T, Matsuda S, Tsuzuku JK, Yoshida Y, Yamamoto T | title = A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob | journal = Genes to Cells | volume = 6 | issue = 2 | pages = 131–8 | date = Feb 2001 | pmid = 11260258 | doi = 10.1046/j.1365-2443.2001.00406.x }} | |||
* {{cite journal | vauthors = Jin Cho S, La M, Ahn JK, Meadows GG, Joe CO | title = Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation | journal = Biochemical and Biophysical Research Communications | volume = 283 | issue = 2 | pages = 273–7 | date = May 2001 | pmid = 11327693 | doi = 10.1006/bbrc.2001.4773 }} | |||
* {{cite journal | vauthors = Yoshida Y, Hosoda E, Nakamura T, Yamamoto T | title = Association of ANA, a member of the antiproliferative Tob family proteins, with a Caf1 component of the CCR4 transcriptional regulatory complex | journal = Japanese Journal of Cancer Research | volume = 92 | issue = 6 | pages = 592–6 | date = Jun 2001 | pmid = 11429045 | doi = 10.1111/j.1349-7006.2001.tb01135.x }} | |||
* {{cite journal | vauthors = Tzachanis D, Freeman GJ, Hirano N, van Puijenbroek AA, Delfs MW, Berezovskaya A, Nadler LM, Boussiotis VA | title = Tob is a negative regulator of activation that is expressed in anergic and quiescent T cells | journal = Nature Immunology | volume = 2 | issue = 12 | pages = 1174–82 | date = Dec 2001 | pmid = 11694881 | doi = 10.1038/ni730 }} | |||
* {{cite journal | vauthors = Suzuki T, K-Tsuzuku J, Ajima R, Nakamura T, Yoshida Y, Yamamoto T | title = Phosphorylation of three regulatory serines of Tob by Erk1 and Erk2 is required for Ras-mediated cell proliferation and transformation | journal = Genes & Development | volume = 16 | issue = 11 | pages = 1356–70 | date = Jun 2002 | pmid = 12050114 | pmc = 186319 | doi = 10.1101/gad.962802 }} | |||
* {{cite journal | vauthors = Sasajima H, Nakagawa K, Yokosawa H | title = Antiproliferative proteins of the BTG/Tob family are degraded by the ubiquitin-proteasome system | journal = European Journal of Biochemistry / FEBS | volume = 269 | issue = 14 | pages = 3596–604 | date = Jul 2002 | pmid = 12135500 | doi = 10.1046/j.1432-1033.2002.03052.x }} | |||
* {{cite journal | vauthors = Maekawa M, Nishida E, Tanoue T | title = Identification of the Anti-proliferative protein Tob as a MAPK substrate | journal = The Journal of Biological Chemistry | volume = 277 | issue = 40 | pages = 37783–7 | date = Oct 2002 | pmid = 12151396 | doi = 10.1074/jbc.M204506200 }} | |||
* {{cite journal | vauthors = Yoshida Y, von Bubnoff A, Ikematsu N, Blitz IL, Tsuzuku JK, Yoshida EH, Umemori H, Miyazono K, Yamamoto T, Cho KW | title = Tob proteins enhance inhibitory Smad-receptor interactions to repress BMP signaling | journal = Mechanisms of Development | volume = 120 | issue = 5 | pages = 629–37 | date = May 2003 | pmid = 12782279 | doi = 10.1016/S0925-4773(03)00020-0 }} | |||
* {{cite journal | vauthors = 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 | title = Alteration of expression or phosphorylation status of tob, a novel tumor suppressor gene product, is an early event in lung cancer | journal = Cancer Letters | volume = 202 | issue = 1 | pages = 71–9 | date = Dec 2003 | pmid = 14643028 | doi = 10.1016/j.canlet.2003.08.019 }} | |||
* {{cite journal | vauthors = Maekawa M, Yamamoto T, Nishida E | title = Regulation of subcellular localization of the antiproliferative protein Tob by its nuclear export signal and bipartite nuclear localization signal sequences | journal = Experimental Cell Research | volume = 295 | issue = 1 | pages = 59–65 | date = Apr 2004 | pmid = 15051490 | doi = 10.1016/j.yexcr.2003.12.016 }} | |||
* {{cite journal | vauthors = Kawamura-Tsuzuku J, Suzuki T, Yoshida Y, Yamamoto T | title = Nuclear localization of Tob is important for regulation of its antiproliferative activity | journal = Oncogene | volume = 23 | issue = 39 | pages = 6630–8 | date = Aug 2004 | pmid = 15235587 | doi = 10.1038/sj.onc.1207890 }} | |||
* {{cite journal | vauthors = Okochi K, Suzuki T, Inoue J, Matsuda S, Yamamoto T | title = Interaction of anti-proliferative protein Tob with poly(A)-binding protein and inducible poly(A)-binding protein: implication of Tob in translational control | journal = Genes to Cells | volume = 10 | issue = 2 | pages = 151–63 | date = Feb 2005 | pmid = 15676026 | doi = 10.1111/j.1365-2443.2005.00826.x }} | |||
{{Refend}} | |||
== External links == | |||
* {{UCSC genome browser|TOB1}} | |||
* {{UCSC gene details|TOB1}} | |||
{{PDB Gallery|geneid=10140}} | |||
{{Gene-17-stub}} |
Latest revision as of 02:03, 27 October 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
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UniProt |
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RefSeq (mRNA) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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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
- ↑ 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.
- ↑ 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.
- ↑ 3.0 3.1 "Entrez Gene: TOB1 transducer of ERBB2, 1".
- ↑ 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.
- ↑ 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.
- ↑ 6.0 6.1 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.
- ↑ 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.
- ↑ 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.
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
- TOB1 human gene location in the UCSC Genome Browser.
- TOB1 human gene details in the UCSC Genome Browser.
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