Tirozinska proteinska kinaza Lyn je protein koji je kod ljudi kodiran LYNgenom.[1]
Lin je član Src familije proteinskih tirozinskih kinaza, koja je uglavnom izražena u hematopoietskim ćelijama,[2] u nervnom tkivu[3] jetri, i adipoznom tkivu.[4] U raznim hematopoietskim ćelijama, Lyn je ključni enzim koji učestvuje u regulaciji ćelijske aktivacije. U tim ćelijama, male količina LYN'a su asocirane sa receptorskim proteinima na ćelijskoj površini, uključujući B ćelijski antigenski receptor (BCR),[5][6]CD40,[7] ili CD19.[8]
↑Umemori H, Wanaka A, Kato H, Takeuchi M, Tohyama M, Yamamoto T (December 1992). „Specific expressions of Fyn and Lyn, lymphocyte antigen receptor-associated tyrosine kinases, in the central nervous system”. Brain Res. Mol. Brain Res.16 (3–4): 303–10. DOI:10.1016/0169-328X(92)90239-8. PMID1337939.
↑ 9,09,1Manié SN, Beck AR, Astier A, Law SF, Canty T, Hirai H, Druker BJ, Avraham H, Haghayeghi N, Sattler M, Salgia R, Griffin JD, Golemis EA, Freedman AS (February 1997). „Involvement of p130(Cas) and p105(HEF1), a novel Cas-like docking protein, in a cytoskeleton-dependent signaling pathway initiated by ligation of integrin or antigen receptor on human B cells”. J. Biol. Chem.272 (7): 4230–6. DOI:10.1074/jbc.272.7.4230. PMID9020138.
↑Qiu W, Cobb RR, Scholz W (May 1998). „Inhibition of p130cas tyrosine phosphorylation by calyculin A”. J. Leukoc. Biol.63 (5): 631–5. PMID9581808.
↑ 11,011,1Liang X, Wisniewski D, Strife A, Clarkson B, Resh MD (April 2002). „Phosphatidylinositol 3-kinase and Src family kinases are required for phosphorylation and membrane recruitment of Dok-1 in c-Kit signaling”. J. Biol. Chem.277 (16): 13732–8. DOI:10.1074/jbc.M200277200. PMID11825908.
↑Linnekin D, DeBerry CS, Mou S (October 1997). „Lyn associates with the juxtamembrane region of c-Kit and is activated by stem cell factor in hematopoietic cell lines and normal progenitor cells”. J. Biol. Chem.272 (43): 27450–5. DOI:10.1074/jbc.272.43.27450. PMID9341198.
↑Poe JC, Fujimoto M, Jansen PJ, Miller AS, Tedder TF (June 2000). „CD22 forms a quaternary complex with SHIP, Grb2, and Shc. A pathway for regulation of B lymphocyte antigen receptor-induced calcium flux”. J. Biol. Chem.275 (23): 17420–7. DOI:10.1074/jbc.M001892200. PMID10748054.
↑Greer SF, Justement LB (May 1999). „CD45 regulates tyrosine phosphorylation of CD22 and its association with the protein tyrosine phosphatase SHP-1”. J. Immunol.162 (9): 5278–86. PMID10228003.
↑Kharbanda S, Yuan ZM, Rubin E, Weichselbaum R, Kufe D (August 1994). „Activation of Src-like p56/p53lyn tyrosine kinase by ionizing radiation”. J. Biol. Chem.269 (32): 20739–43. PMID8051175.
↑Pathan NI, Geahlen RL, Harrison ML (November 1996). „The protein-tyrosine kinase Lck associates with and is phosphorylated by Cdc2”. J. Biol. Chem.271 (44): 27517–23. DOI:10.1074/jbc.271.44.27517. PMID8910336.
↑van Dijk TB, van Den Akker E, Amelsvoort MP, Mano H, Löwenberg B, von Lindern M (November 2000). „Stem cell factor induces phosphatidylinositol 3'-kinase-dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells”. Blood96 (10): 3406–13. PMID11071635.
↑Chin H, Arai A, Wakao H, Kamiyama R, Miyasaka N, Miura O (May 1998). „Lyn physically associates with the erythropoietin receptor and may play a role in activation of the Stat5 pathway”. Blood91 (10): 3734–45. PMID9573010.
↑Suzuki-Inoue K, Tulasne D, Shen Y, Bori-Sanz T, Inoue O, Jung SM, Moroi M, Andrews RK, Berndt MC, Watson SP (June 2002). „Association of Fyn and Lyn with the proline-rich domain of glycoprotein VI regulates intracellular signaling”. J. Biol. Chem.277 (24): 21561–6. DOI:10.1074/jbc.M201012200. PMID11943772.
↑Baran CP, Tridandapani S, Helgason CD, Humphries RK, Krystal G, Marsh CB (October 2003). „The inositol 5'-phosphatase SHIP-1 and the Src kinase Lyn negatively regulate macrophage colony-stimulating factor-induced Akt activity”. J. Biol. Chem.278 (40): 38628–36. DOI:10.1074/jbc.M305021200. PMID12882960.
↑Gross BS, Lee JR, Clements JL, Turner M, Tybulewicz VL, Findell PR, Koretzky GA, Watson SP (February 1999). „Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets”. J. Biol. Chem.274 (9): 5963–71. DOI:10.1074/jbc.274.9.5963. PMID10026222.
↑Xu H, Zhao H, Tian W, Yoshida K, Roullet JB, Cohen DM (March 2003). „Regulation of a transient receptor potential (TRP) channel by tyrosine phosphorylation. SRC family kinase-dependent tyrosine phosphorylation of TRPV4 on TYR-253 mediates its response to hypotonic stress”. J. Biol. Chem.278 (13): 11520–7. DOI:10.1074/jbc.M211061200. PMID12538589.
↑Cen O, Gorska MM, Stafford SJ, Sur S, Alam R (March 2003). „Identification of UNC119 as a novel activator of SRC-type tyrosine kinases”. J. Biol. Chem.278 (10): 8837–45. DOI:10.1074/jbc.M208261200. PMID12496276.
Jouvin MH, Numerof RP, Kinet JP (1995). „Signal transduction through the conserved motifs of the high affinity IgE receptor Fc epsilon RI”. Semin. Immunol.7 (1): 29–35. DOI:10.1016/1044-5323(95)90005-5. PMID7612892.
Blasioli J, Goodnow CC (2002). „Signal Transduction Pathways in Autoimmunity. Lyn/CD22/SHP-1 and Their Importance in Autoimmunity”. Curr. Dir. Autoimmun.. Current Directions in Autoimmunity 5: 151–60. DOI:10.1159/000060551. ISBN3-8055-7308-1. PMID11826756.
Greenway AL, Holloway G, McPhee DA, et al. (2004). „HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication”. J. Biosci.28 (3): 323–35. DOI:10.1007/BF02970151. PMID12734410.
Tolstrup M, Ostergaard L, Laursen AL, et al. (2004). „HIV/SIV escape from immune surveillance: focus on Nef”. Curr. HIV Res.2 (2): 141–51. DOI:10.2174/1570162043484924. PMID15078178.
Joseph AM, Kumar M, Mitra D (2005). „Nef: "necessary and enforcing factor" in HIV infection”. Curr. HIV Res.3 (1): 87–94. DOI:10.2174/1570162052773013. PMID15638726.