RTKN
From Wikipedia, the free encyclopedia
| Rhotekin | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||||
| Symbol | RTKN | ||||||||||||
| External IDs | OMIM: 602288 MGI: 107371 HomoloGene: 7522 GeneCards: RTKN Gene | ||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 6242 | 20166 | |||||||||||
| Ensembl | ENSG00000114993 | ENSMUSG00000034930 | |||||||||||
| UniProt | Q9BST9 | Q8C6B2 | |||||||||||
| RefSeq (mRNA) | NM_001015055 | NM_001136227 | |||||||||||
| RefSeq (protein) | NP_001015055 | NP_001129699 | |||||||||||
| Location (UCSC) | Chr 2: 74.65 – 74.67 Mb | Chr 6: 83.14 – 83.15 Mb | |||||||||||
| PubMed search | |||||||||||||
Rhotekin is a protein that in humans is encoded by the RTKN gene.[1][2][3]
This gene encodes a scaffold protein that interacts with GTP-bound Rho proteins. Binding of this protein inhibits the GTPase activity of Rho proteins. This protein may interfere with the conversion of active, GTP-bound Rho to the inactive GDP-bound form by RhoGAP. Rho proteins regulate many important cellular processes, including cytokinesis, transcription, smooth muscle contraction, cell growth and transformation. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Alternative splicing results in multiple transcript variants encoding different isoforms.[3]
References
- ↑ Jang W, Weber JS, Harkins EB, Meisler MH (May 1997). "Localization of the rhotekin gene RTKN on the physical maps of mouse chromosome 6 and human chromosome 2p13 and exclusion as a candidate for mnd2 and LGMD2B". Genomics 40 (3): 506–7. doi:10.1006/geno.1996.4593. PMID 9073523.
- ↑ Reynaud C, Fabre S, Jalinot P (Nov 2000). "The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element". J Biol Chem 275 (43): 33962–8. doi:10.1074/jbc.M000465200. PMID 10940294.
- ↑ 3.0 3.1 "Entrez Gene: RTKN rhotekin".
Further reading
- Reid T, Furuyashiki T, Ishizaki T, et al. (1996). "Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain.". J. Biol. Chem. 271 (23): 13556–60. doi:10.1074/jbc.271.23.13556. PMID 8662891.
- "Toward a complete human genome sequence.". Genome Res. 8 (11): 1097–108. 1999. doi:10.1101/gr.8.11.1097. PMID 9847074.
- Fu Q, Yu L, Liu Q, et al. (2000). "Molecular cloning, expression characterization, and mapping of a novel putative inhibitor of rho GTPase activity, RTKN, to D2S145-D2S286.". Genomics 66 (3): 328–32. doi:10.1006/geno.2000.6212. PMID 10873388.
- 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.
- Sharfe N, Freywald A, Toro A, et al. (2003). "Ephrin stimulation modulates T cell chemotaxis.". Eur. J. Immunol. 32 (12): 3745–55. doi:10.1002/1521-4141(200212)32:12<3745::AID-IMMU3745>3.0.CO;2-M. PMID 12516569.
- Katoh H, Negishi M (2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo.". Nature 424 (6947): 461–4. doi:10.1038/nature01817. PMID 12879077.
- Liu CA, Wang MJ, Chi CW, et al. (2005). "Overexpression of rho effector rhotekin confers increased survival in gastric adenocarcinoma.". J. Biomed. Sci. 11 (5): 661–70. doi:10.1159/000079679. PMID 15316142.
- Jacinto E, Loewith R, Schmidt A, et al. (2004). "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive.". Nat. Cell Biol. 6 (11): 1122–8. doi:10.1038/ncb1183. PMID 15467718.
- Liu CA, Wang MJ, Chi CW, et al. (2005). "Rho/Rhotekin-mediated NF-kappaB activation confers resistance to apoptosis.". Oncogene 23 (54): 8731–42. doi:10.1038/sj.onc.1208106. PMID 15480428.
- 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.
- Fan J, Ma LJ, Xia SJ, et al. (2005). "Association between clinical characteristics and expression abundance of RTKN gene in human bladder carcinoma tissues from Chinese patients.". J. Cancer Res. Clin. Oncol. 131 (3): 157–62. doi:10.1007/s00432-004-0638-8. PMID 15599595.
- Fernandez-Zapico ME, Gonzalez-Paz NC, Weiss E, et al. (2005). "Ectopic expression of VAV1 reveals an unexpected role in pancreatic cancer tumorigenesis.". Cancer Cell 7 (1): 39–49. doi:10.1016/j.ccr.2004.11.024. PMID 15652748.
- Park JB, Yiu G, Kaneko S, et al. (2005). "A TNF receptor family member, TROY, is a coreceptor with Nogo receptor in mediating the inhibitory activity of myelin inhibitors.". Neuron 45 (3): 345–51. doi:10.1016/j.neuron.2004.12.040. PMID 15694321.
- Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells.". Science 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153.
- Satchi-Fainaro R, Mamluk R, Wang L, et al. (2005). "Inhibition of vessel permeability by TNP-470 and its polymer conjugate, caplostatin.". Cancer Cell 7 (3): 251–61. doi:10.1016/j.ccr.2005.02.007. PMID 15766663.
- Kukar T, Murphy MP, Eriksen JL, et al. (2005). "Diverse compounds mimic Alzheimer disease-causing mutations by augmenting Abeta42 production.". Nat. Med. 11 (5): 545–50. doi:10.1038/nm1235. PMID 15834426.
- Kiyan J, Kiyan R, Haller H, Dumler I (2005). "Urokinase-induced signaling in human vascular smooth muscle cells is mediated by PDGFR-beta.". EMBO J. 24 (10): 1787–97. doi:10.1038/sj.emboj.7600669. PMC 1142599. PMID 15889147.
- Ito H, Iwamoto I, Morishita R, et al. (2005). "Possible role of Rho/Rhotekin signaling in mammalian septin organization.". Oncogene 24 (47): 7064–72. doi:10.1038/sj.onc.1208862. PMID 16007136.
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