Biology:Janus kinase 1
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JAK1 is a human tyrosine kinase protein essential for signaling for certain type I and type II cytokines. It interacts with the common gamma chain (γc) of type I cytokine receptors, to elicit signals from the IL-2 receptor family (e.g. IL-2R, IL-7R, IL-9R and IL-15R), the IL-4 receptor family (e.g. IL-4R and IL-13R), the gp130 receptor family (e.g. IL-6R, IL-11R, LIF-R, OSM-R, cardiotrophin-1 receptor (CT-1R), ciliary neurotrophic factor receptor (CNTF-R), neurotrophin-1 receptor (NNT-1R) and Leptin-R). It is also important for transducing a signal by type I (IFN-α/β) and type II (IFN-γ) interferons, and members of the IL-10 family via type II cytokine receptors.[1] Jak1 plays a critical role in initiating responses to multiple major cytokine receptor families. Loss of Jak1 is lethal in neonatal mice, possibly due to difficulties suckling.[2] Expression of JAK1 in cancer cells enables individual cells to contract, potentially allowing them to escape their tumor and metastasize to other parts of the body.[3]
Interactions
Janus kinase 1 has been shown to interact with:
- ELP2,[4]
- GNB2L1[5]
- IL6ST,[6][7][8]
- Grb2,[9][10]
- IL2RB,[11][12][13][14][15]
- IRS1,[16][17]
- IL10RA,[11][18]
- PTPN11,[19][20]
- STAM2,[21][22]
- STAT3,[23][24]
- STAT5A,[25]
- STAT5B,[25] and
- TNFRSF1A.[26][27]
See also
- Janus kinase inhibitor
References
- ↑ "Signaling by type I and II cytokine receptors: ten years after". Curr. Opin. Immunol. 13 (3): 363–73. 2001. doi:10.1016/S0952-7915(00)00228-4. PMID 11406370. https://zenodo.org/record/1260155.
- ↑ "Disruption of the Jak1 gene demonstrates obligatory and nonredundant roles of the Jaks in cytokine-induced biologic responses". Cell 93 (3): 373–83. 1998. doi:10.1016/S0092-8674(00)81166-6. PMID 9590172.
- ↑ Christian Nordqvist. "Protein JAK Makes Cancer Cells Contract, So They Can Squeeze Out Of A Tumor". Medical News Today. http://www.medicalnewstoday.com/articles/232761.php.
- ↑ "A Stat3-interacting protein (StIP1) regulates cytokine signal transduction". Proc. Natl. Acad. Sci. U.S.A. 97 (18): 10120–5. August 2000. doi:10.1073/pnas.170192197. PMID 10954736. Bibcode: 2000PNAS...9710120C.
- ↑ "The WD motif-containing protein RACK-1 functions as a scaffold protein within the type I IFN receptor-signaling complex". J. Immunol. 171 (6): 2989–94. September 2003. doi:10.4049/jimmunol.171.6.2989. PMID 12960323.
- ↑ "Mapping of a region within the N terminus of Jak1 involved in cytokine receptor interaction". J. Biol. Chem. 276 (40): 37451–8. October 2001. doi:10.1074/jbc.M106135200. PMID 11468294.
- ↑ "Transmembrane domain of gp130 contributes to intracellular signal transduction in hepatic cells". J. Biol. Chem. 272 (49): 30741–7. December 1997. doi:10.1074/jbc.272.49.30741. PMID 9388212.
- ↑ "Structural requirements of the interleukin-6 signal transducer gp130 for its interaction with Janus kinase 1: the receptor is crucial for kinase activation". Biochem. J. 361 (Pt 1): 105–11. January 2002. doi:10.1042/0264-6021:3610105. PMID 11742534.
- ↑ "Through induction of juxtaposition and tyrosine kinase activity of Jak1, X-gene product of hepatitis B virus stimulates Ras and the transcriptional activation through AP-1, NF-kappaB, and SRE enhancers". Biochem. Biophys. Res. Commun. 286 (5): 886–94. September 2001. doi:10.1006/bbrc.2001.5496. PMID 11527382.
- ↑ "Involvement of Janus kinases in the insulin signaling pathway". Eur. J. Biochem. 234 (2): 656–60. December 1995. doi:10.1111/j.1432-1033.1995.656_b.x. PMID 8536716.
- ↑ 11.0 11.1 "Two distinct domains within the N-terminal region of Janus kinase 1 interact with cytokine receptors". J. Immunol. 169 (3): 1302–8. August 2002. doi:10.4049/jimmunol.169.3.1302. PMID 12133952.
- ↑ "Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits". Science 266 (5187): 1045–7. November 1994. doi:10.1126/science.7973659. PMID 7973659. Bibcode: 1994Sci...266.1045M.
- ↑ "Interaction of IL-2R beta and gamma c chains with Jak1 and Jak3: implications for XSCID and XCID". Science 266 (5187): 1042–5. November 1994. doi:10.1126/science.7973658. PMID 7973658. Bibcode: 1994Sci...266.1042R. https://zenodo.org/record/1231239.
- ↑ "Delineation of the regions of interleukin-2 (IL-2) receptor beta chain important for association of Jak1 and Jak3. Jak1-independent functional recruitment of Jak3 to Il-2Rbeta". J. Biol. Chem. 273 (17): 10719–25. April 1998. doi:10.1074/jbc.273.17.10719. PMID 9553136.
- ↑ "Functional cooperation of the interleukin-2 receptor beta chain and Jak1 in phosphatidylinositol 3-kinase recruitment and phosphorylation". Mol. Cell. Biol. 18 (11): 6416–22. November 1998. doi:10.1128/mcb.18.11.6416. PMID 9774657.
- ↑ "Interaction of Janus kinases JAK-1 and JAK-2 with the insulin receptor and the insulin-like growth factor-1 receptor". Endocrinology 139 (3): 884–93. March 1998. doi:10.1210/endo.139.3.5829. PMID 9492017.
- ↑ "Interleukins 2, 4, 7, and 15 stimulate tyrosine phosphorylation of insulin receptor substrates 1 and 2 in T cells. Potential role of JAK kinases". J. Biol. Chem. 270 (48): 28527–30. December 1995. doi:10.1074/jbc.270.48.28527. PMID 7499365.
- ↑ "Contribution of the Box 1 and Box 2 motifs of cytokine receptors to Jak1 association and activation". J. Biol. Chem. 277 (50): 48220–6. December 2002. doi:10.1074/jbc.M205757200. PMID 12374810.
- ↑ "Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases". J. Biol. Chem. 272 (2): 1032–7. January 1997. doi:10.1074/jbc.272.2.1032. PMID 8995399.
- ↑ "SHP2 and SOCS3 contribute to Tyr-759-dependent attenuation of interleukin-6 signaling through gp130". J. Biol. Chem. 278 (1): 661–71. January 2003. doi:10.1074/jbc.M210552200. PMID 12403768.
- ↑ "Identification of a novel immunoreceptor tyrosine-based activation motif-containing molecule, STAM2, by mass spectrometry and its involvement in growth factor and cytokine receptor signaling pathways". J. Biol. Chem. 275 (49): 38633–9. December 2000. doi:10.1074/jbc.M007849200. PMID 10993906.
- ↑ "STAM2, a new member of the STAM family, binding to the Janus kinases". FEBS Lett. 477 (1–2): 55–61. July 2000. doi:10.1016/s0014-5793(00)01760-9. PMID 10899310.
- ↑ "Activation of the androgen receptor N-terminal domain by interleukin-6 via MAPK and STAT3 signal transduction pathways". J. Biol. Chem. 277 (9): 7076–85. March 2002. doi:10.1074/jbc.M108255200. PMID 11751884.
- ↑ "Constitutive activation of STAT transcription factors in acute myelogenous leukemia". Eur. J. Haematol. 67 (2): 63–71. August 2001. doi:10.1034/j.1600-0609.2001.t01-1-00385.x. PMID 11722592.
- ↑ 25.0 25.1 "An alternative pathway for STAT activation that is mediated by the direct interaction between JAK and STAT". Oncogene 14 (7): 751–61. February 1997. doi:10.1038/sj.onc.1200907. PMID 9047382.
- ↑ "Induction of Jak/STAT signaling by activation of the type 1 TNF receptor". J. Immunol. 160 (6): 2742–50. March 1998. doi:10.4049/jimmunol.160.6.2742. PMID 9510175.
- ↑ "Tumor necrosis factor alpha (TNF-alpha) activates Jak1/Stat3-Stat5B signaling through TNFR-1 in human B cells". Cell Growth Differ. 13 (1): 13–8. January 2002. PMID 11801527.
Further reading
- "The interleukin-10 signal transduction pathway and regulation of gene expression in mononuclear phagocytes". J. Interferon Cytokine Res. 19 (6): 563–73. 1999. doi:10.1089/107999099313695. PMID 10433356. https://zenodo.org/record/1235223.
- "SH2-B and SIRP: JAK2 binding proteins that modulate the actions of growth hormone". Recent Prog. Horm. Res. 55: 293–311. 2000. PMID 11036942.
- Kostrodymova GM (1976). "[An experimental study of the possible sensitizing properties of triethanolamine contained in chemical compounds used at home]". Gigiena i Sanitariia (6): 10–2. PMID 1213395.
- Howard OM; Dean M; Young H; Ramsburg, M; Turpin, JA; Michiel, DF; Kelvin, DJ; Lee, L et al. (1992). "Characterization of a class 3 tyrosine kinase". Oncogene 7 (5): 895–900. PMID 1373877.
- Pritchard MA; Baker E; Callen DF; Sutherland, Grant R.; Wilks, Andrew F. (1992). "Two members of the JAK family of protein tyrosine kinases map to chromosomes 1p31.3 and 9p24". Mamm. Genome 3 (1): 36–8. doi:10.1007/BF00355839. PMID 1581631.
- Wilks AF; Harpur AG; Kurban RR; Ralph, SJ; Zürcher, G; Ziemiecki, A (1991). "Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase". Mol. Cell. Biol. 11 (4): 2057–65. doi:10.1128/MCB.11.4.2057. PMID 1848670.
- Johnston JA; Wang LM; Hanson EP; Sun, XJ; White, MF; Oakes, SA; Pierce, JH; O'Shea, JJ (1996). "Interleukins 2, 4, 7, and 15 stimulate tyrosine phosphorylation of insulin receptor substrates 1 and 2 in T cells. Potential role of JAK kinases". J. Biol. Chem. 270 (48): 28527–30. doi:10.1074/jbc.270.48.28527. PMID 7499365.
- Nicholson SE; Oates AC; Harpur AG; Ziemiecki, A; Wilks, AF; Layton, JE (1994). "Tyrosine kinase JAK1 is associated with the granulocyte-colony-stimulating factor receptor and both become tyrosine-phosphorylated after receptor activation". Proc. Natl. Acad. Sci. U.S.A. 91 (8): 2985–8. doi:10.1073/pnas.91.8.2985. PMID 7512720. Bibcode: 1994PNAS...91.2985N.
- Domanski P; Yan H; Witte MM; Krolewski, J; Colamonici, OR (1995). "Homodimerization and intermolecular tyrosine phosphorylation of the Tyk-2 tyrosine kinase". FEBS Lett. 374 (3): 317–22. doi:10.1016/0014-5793(95)01094-U. PMID 7589562.
- "Confirmed assignment of a novel human tyrosine kinase gene (JAK1A) to 1p32.3→p31.3 by nonisotopic in situ hybridization". Cytogenet. Cell Genet. 69 (3–4): 232–4. 1995. doi:10.1159/000133971. PMID 7698020. https://zenodo.org/record/1235414.
- Miyazaki T; Kawahara A; Fujii H; Nakagawa, Y; Minami, Y; Liu, Z.; Oishi, I; Silvennoinen, O et al. (1994). "Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits". Science 266 (5187): 1045–7. doi:10.1126/science.7973659. PMID 7973659. Bibcode: 1994Sci...266.1045M.
- Müller M; Briscoe J; Laxton C; Guschin, Dmitry; Ziemiecki, Andrew; Silvennoinen, Olli; Harpur, Ailsa G.; Barbieri, Giovanna et al. (1993). "The protein tyrosine kinase JAK1 complements defects in interferon-alpha/beta and -gamma signal transduction". Nature 366 (6451): 129–35. doi:10.1038/366129a0. PMID 8232552. Bibcode: 1993Natur.366..129M.
- "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes". Oncogene 8 (12): 3403–10. 1993. PMID 8247543.
- Lütticken C; Wegenka UM; Yuan J; Buschmann, J; Schindler, C; Ziemiecki, A; Harpur, A.; Wilks, A. et al. (1994). "Association of transcription factor APRF and protein kinase Jak1 with the interleukin-6 signal transducer gp130". Science 263 (5143): 89–92. doi:10.1126/science.8272872. PMID 8272872. Bibcode: 1994Sci...263...89L.
- "Involvement of Janus kinases in the insulin signaling pathway". Eur. J. Biochem. 234 (2): 656–60. 1996. doi:10.1111/j.1432-1033.1995.656_b.x. PMID 8536716.
- "Different interleukin 2 receptor beta-chain tyrosines couple to at least two signaling pathways and synergistically mediate interleukin 2-induced proliferation". Proc. Natl. Acad. Sci. U.S.A. 93 (5): 2077–82. 1996. doi:10.1073/pnas.93.5.2077. PMID 8700888. Bibcode: 1996PNAS...93.2077F.
- Gauzzi MC; Velazquez L; McKendry R; Mogensen, KE; Fellous, M; Pellegrini, S (1996). "Interferon-alpha-dependent activation of Tyk2 requires phosphorylation of positive regulatory tyrosines by another kinase". J. Biol. Chem. 271 (34): 20494–500. doi:10.1074/jbc.271.34.20494. PMID 8702790.
- Demoulin JB; Uyttenhove C; Van Roost E; Delestré, B; Donckers, D; Van Snick, J; Renauld, JC (1996). "A single tyrosine of the interleukin-9 (IL-9) receptor is required for STAT activation, antiapoptotic activity, and growth regulation by IL-9". Mol. Cell. Biol. 16 (9): 4710–6. doi:10.1128/MCB.16.9.4710. PMID 8756628.
- "Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases". J. Biol. Chem. 272 (2): 1032–7. 1997. doi:10.1074/jbc.272.2.1032. PMID 8995399.
- "Stat2 is a transcriptional activator that requires sequence-specific contacts provided by stat1 and p48 for stable interaction with DNA". J. Biol. Chem. 272 (7): 4600–5. 1997. doi:10.1074/jbc.272.7.4600. PMID 9020188.
External links
- Janus+Kinase+1 at the US National Library of Medicine Medical Subject Headings (MeSH)
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