FYN

From Wikipedia, the free encyclopedia
FYN oncogene related to SRC, FGR, YES

PDB rendering based on 1a0n.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsFYN; SLK; SYN; p59-FYN
External IDsOMIM: 137025 MGI: 95602 HomoloGene: 48068 ChEMBL: 1841 GeneCards: FYN Gene
EC number2.7.10.2
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez253414360
EnsemblENSG00000010810ENSMUSG00000019843
UniProtP06241P39688
RefSeq (mRNA)NM_001242779NM_001122892
RefSeq (protein)NP_002028NP_001116364
Location (UCSC)Chr 6:
111.98 – 112.19 Mb		Chr 10:
39.37 – 39.57 Mb
PubMed search
This box:

Proto-oncogene tyrosine-protein kinase Fyn is an enzyme that in humans is encoded by the FYN gene.[1]

This gene is a member of the protein-tyrosine kinase oncogene family. It encodes a membrane-associated tyrosine kinase that has been implicated in the control of cell growth. The protein associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. Alternatively spliced transcript variants encoding distinct isoforms exist.[2]

Function

Fyn is a protein, present in the signaling pathway of integrins, which activates ras. Fyn is a tyrosine-specific phospho-transferase that is a member of the Src family of tyrosine protein kinases.[3] Fyn is primarily localized to the cytoplasmic leaflet of the plasma membrane, where it phosphorylates tyrosine residues on key targets involved in a variety of different signaling pathways. Tyrosine phosphorylation of target proteins by Fyn serves to either regulate target protein activity, and/or to generate a binding site on the target protein that recruits other signaling molecules.

Role in signaling pathways

At least three tools have been useful in discerning a requirement for Fyn function in a particular signaling system:

  • cells derived from Fyn-/- mice (as well as cells derived from Fyn, Src, Yes, Fyn triple knockout mice (SYF));
  • a kinase-inactive, dominant negative mutant form of Fyn (K299M);
  • pharmacologic inhibitors of Src family kinases, such as PP2; note that PP2 also inhibits other tyrosine protein kinases such as Abl, PDGFR and c-Kit.

Using these tools, a requirement for Fyn has been shown for the following signaling pathways: T and B cell receptor signaling,[4][5] integrin-mediated signaling, growth factor and cytokine receptor signaling, platelet activation, ion channel function, cell adhesion, axon guidance, fertilization, entry into mitosis, and differentiation of natural killer cells, oligodendrocytes and keratinocytes.

Interactions

FYN has been shown to interact with:

References

  1. ↑ Semba K, Nishizawa M, Miyajima N, Yoshida MC, Sukegawa J, Yamanashi Y, Sasaki M, Yamamoto T, Toyoshima K (August 1986). "yes-related protooncogene, syn, belongs to the protein-tyrosine kinase family". Proceedings of the National Academy of Sciences of the United States of America 83 (15): 5459–63. doi:10.1073/pnas.83.15.5459. PMC 386306. PMID 3526330. 
  2. ↑ "Entrez Gene: FYN FYN oncogene related to SRC, FGR, YES". 
  3. ↑ Resh MD (November 1998). "Fyn, a Src family tyrosine kinase". The international journal of biochemistry & cell biology 30 (11): 1159–62. doi:10.1016/S1357-2725(98)00089-2. PMID 9839441. 
  4. ↑ Zamoyska R, Basson A, Filby A, Legname G, Lovatt M, Seddon B (February 2003). "The influence of the src-family kinases, Lck and Fyn, on T cell differentiation, survival and activation". Immunological reviews 191 (1): 107–18. doi:10.1034/j.1600-065X.2003.00015.x. PMID 12614355. 
  5. ↑ Palacios EH, Weiss A (October 2004). "Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation". Oncogene 23 (48): 7990–8000. doi:10.1038/sj.onc.1208074. PMID 15489916. 
  6. ↑ Shima, T; Okumura N, Takao T, Satomi Y, Yagi T, Okada M, Nagai K (November 2001). "Interaction of the SH2 domain of Fyn with a cytoskeletal protein, beta-adducin". J. Biol. Chem. (United States) 276 (45): 42233–40. doi:10.1074/jbc.M102699200. ISSN 0021-9258. PMID 11526103. 
  7. ↑ 7.0 7.1 Klein, Corinna; Kramer Eva-Maria, Cardine Anne-Marie, Schraven Burkhardt, Brandt Roland, Trotter Jacqueline (February 2002). "Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau". J. Neurosci. (United States) 22 (3): 698–707. PMID 11826099. 
  8. ↑ Donaldson, J C; Dempsey P J, Reddy S, Bouton A H, Coffey R J, Hanks S K (April 2000). "Crk-associated substrate p130(Cas) interacts with nephrocystin and both proteins localize to cell-cell contacts of polarized epithelial cells". Exp. Cell Res. (UNITED STATES) 256 (1): 168–78. doi:10.1006/excr.2000.4822. ISSN 0014-4827. PMID 10739664. 
  9. ↑ Manié, S N; Astier A, Haghayeghi N, Canty T, Druker B J, Hirai H, Freedman A S (June 1997). "Regulation of integrin-mediated p130(Cas) tyrosine phosphorylation in human B cells. A role for p59(Fyn) and SHP2". J. Biol. Chem. (UNITED STATES) 272 (25): 15636–41. doi:10.1074/jbc.272.25.15636. ISSN 0021-9258. PMID 9188452. 
  10. ↑ Taher, Taher E I; Tjin Esther P M, Beuling Esther A, Borst Jannie, Spaargaren Marcel, Pals Steven T (October 2002). "c-Cbl is involved in Met signaling in B cells and mediates hepatocyte growth factor-induced receptor ubiquitination". J. Immunol. (United States) 169 (7): 3793–800. ISSN 0022-1767. PMID 12244174. 
  11. ↑ 11.0 11.1 Deckert, M; Elly C, Altman A, Liu Y C (April 1998). "Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases". J. Biol. Chem. (UNITED STATES) 273 (15): 8867–74. doi:10.1074/jbc.273.15.8867. ISSN 0021-9258. PMID 9535867. 
  12. ↑ Kim, M; Tezuka T, Suziki Y, Sugano S, Hirai M, Yamamoto T (October 1999). "Molecular cloning and characterization of a novel cbl-family gene, cbl-c". Gene (NETHERLANDS) 239 (1): 145–54. doi:10.1016/S0378-1119(99)00356-X. ISSN 0378-1119. PMID 10571044. 
  13. ↑ Huang, M M; Bolen J B, Barnwell J W, Shattil S J, Brugge J S (September 1991). "Membrane glycoprotein IV (CD36) is physically associated with the Fyn, Lyn, and Yes protein-tyrosine kinases in human platelets". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 88 (17): 7844–8. doi:10.1073/pnas.88.17.7844. ISSN 0027-8424. PMC 52400. PMID 1715582. 
  14. ↑ Bull, H A; Brickell P M, Dowd P M (August 1994). "Src-related protein tyrosine kinases are physically associated with the surface antigen CD36 in human dermal microvascular endothelial cells". FEBS Lett. (NETHERLANDS) 351 (1): 41–4. doi:10.1016/0014-5793(94)00814-0. ISSN 0014-5793. PMID 7521304. 
  15. ↑ Ilangumaran, S; Briol A, Hoessli D C (May 1998). "CD44 selectively associates with active Src family protein tyrosine kinases Lck and Fyn in glycosphingolipid-rich plasma membrane domains of human peripheral blood lymphocytes". Blood (UNITED STATES) 91 (10): 3901–8. ISSN 0006-4971. PMID 9573028. 
  16. ↑ 16.0 16.1 Piedra, Jose; Miravet Susana, Castaño Julio, Pálmer Héctor G, Heisterkamp Nora, García de Herreros Antonio, Duñach Mireia (April 2003). "p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction". Mol. Cell. Biol. (United States) 23 (7): 2287–97. doi:10.1128/MCB.23.7.2287-2297.2003. ISSN 0270-7306. PMC 150740. PMID 12640114. 
  17. ↑ Kihara, T; Shimohama S, Sawada H, Honda K, Nakamizo T, Shibasaki H, Kume T, Akaike A (April 2001). "alpha 7 nicotinic receptor transduces signals to phosphatidylinositol 3-kinase to block A beta-amyloid-induced neurotoxicity". J. Biol. Chem. (United States) 276 (17): 13541–6. doi:10.1074/jbc.M008035200. ISSN 0021-9258. PMID 11278378. 
  18. ↑ Courtneidge, S A; Dhand R, Pilat D, Twamley G M, Waterfield M D, Roussel M F (March 1993). "Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor". EMBO J. (ENGLAND) 12 (3): 943–50. ISSN 0261-4189. PMC 413295. PMID 7681396. 
  19. ↑ Cleghon, V; Morrison D K (July 1994). "Raf-1 interacts with Fyn and Src in a non-phosphotyrosine-dependent manner". J. Biol. Chem. (UNITED STATES) 269 (26): 17749–55. ISSN 0021-9258. PMID 7517401. 
  20. ↑ Martinez, Maria Cruz; Ochiishi Tomoyo, Majewski Michael, Kosik Kenneth S (July 2003). "Dual regulation of neuronal morphogenesis by a delta-catenin-cortactin complex and Rho". J. Cell Biol. (United States) 162 (1): 99–111. doi:10.1083/jcb.200211025. ISSN 0021-9525. PMC 2172717. PMID 12835311. 
  21. ↑ 21.0 21.1 Tezuka, T; Umemori H, Akiyama T, Nakanishi S, Yamamoto T (January 1999). "PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-D-aspartate receptor subunit NR2A". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (2): 435–40. doi:10.1073/pnas.96.2.435. ISSN 0027-8424. PMC 15154. PMID 9892651. 
  22. ↑ 22.0 22.1 Hou, Xiao-Yu; Zhang Guang-Yi, Yan Jing-Zhi, Chen Min, Liu Yong (November 2002). "Activation of NMDA receptors and L-type voltage-gated calcium channels mediates enhanced formation of Fyn-PSD95-NR2A complex after transient brain ischemia". Brain Res. (Netherlands) 955 (1-2): 123–32. doi:10.1016/S0006-8993(02)03376-0. ISSN 0006-8993. PMID 12419528. 
  23. ↑ Sotgia, F; Lee H, Bedford M T, Petrucci T, Sudol M, Lisanti M P (December 2001). "Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins". Biochemistry (United States) 40 (48): 14585–92. doi:10.1021/bi011247r. ISSN 0006-2960. PMID 11724572. 
  24. ↑ Choi, S; Park S (September 1999). "Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates Fyn binding to the Tyr-615 site by enhancing tyrosine kinase activity". Oncogene (ENGLAND) 18 (39): 5413–22. doi:10.1038/sj.onc.1202917. ISSN 0950-9232. PMID 10498895. 
  25. ↑ Wenzel, J; Sanzenbacher R, Ghadimi M, Lewitzky M, Zhou Q, Kaplan D R, Kabelitz D, Feller S M, Janssen O (December 2001). "Multiple interactions of the cytosolic polyproline region of the CD95 ligand: hints for the reverse signal transduction capacity of a death factor". FEBS Lett. (Netherlands) 509 (2): 255–62. doi:10.1016/S0014-5793(01)03174-X. ISSN 0014-5793. PMID 11741599. 
  26. ↑ Hane, M; Lowin B, Peitsch M, Becker K, Tschopp J (October 1995). "Interaction of peptides derived from the Fas ligand with the Fyn-SH3 domain". FEBS Lett. (NETHERLANDS) 373 (3): 265–8. doi:10.1016/0014-5793(95)01051-F. ISSN 0014-5793. PMID 7589480. 
  27. ↑ da Silva, A J; Janssen O, Rudd C E (December 1993). "T cell receptor zeta/CD3-p59fyn(T)-associated p120/130 binds to the SH2 domain of p59fyn(T)". J. Exp. Med. (UNITED STATES) 178 (6): 2107–13. doi:10.1084/jem.178.6.2107. ISSN 0022-1007. PMC 2191307. PMID 7504057. 
  28. ↑ 28.0 28.1 Marie-Cardine, A; Hendricks-Taylor L R, Boerth N J, Zhao H, Schraven B, Koretzky G A (October 1998). "Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130". J. Biol. Chem. (UNITED STATES) 273 (40): 25789–95. doi:10.1074/jbc.273.40.25789. ISSN 0021-9258. PMID 9748251. 
  29. ↑ Yaka, Rami; He Dao-Yao, Phamluong Khanhky, Ron Dorit (March 2003). "Pituitary adenylate cyclase-activating polypeptide (PACAP(1-38)) enhances N-methyl-D-aspartate receptor function and brain-derived neurotrophic factor expression via RACK1". J. Biol. Chem. (United States) 278 (11): 9630–8. doi:10.1074/jbc.M209141200. ISSN 0021-9258. PMID 12524444. 
  30. ↑ Yaka, Rami; Thornton Claire, Vagts Alicia J, Phamluong Khanhky, Bonci Antonello, Ron Dorit (April 2002). "NMDA receptor function is regulated by the inhibitory scaffolding protein, RACK1". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (8): 5710–5. doi:10.1073/pnas.062046299. ISSN 0027-8424. PMC 122836. PMID 11943848. 
  31. ↑ Ma, Juan; Zhang Guang-Yi (September 2003). "Lithium reduced N-methyl-D-aspartate receptor subunit 2A tyrosine phosphorylation and its interactions with Src and Fyn mediated by PSD-95 in rat hippocampus following cerebral ischemia". Neurosci. Lett. (Ireland) 348 (3): 185–9. doi:10.1016/S0304-3940(03)00784-5. ISSN 0304-3940. PMID 12932824. 
  32. ↑ Takagi, N; Cheung H H, Bissoon N, Teves L, Wallace M C, Gurd J W (August 1999). "The effect of transient global ischemia on the interaction of Src and Fyn with the N-methyl-D-aspartate receptor and postsynaptic densities: possible involvement of Src homology 2 domains". J. Cereb. Blood Flow Metab. (UNITED STATES) 19 (8): 880–8. doi:10.1097/00004647-199908000-00007. ISSN 0271-678X. PMID 10458595. 
  33. ↑ Bunnell, S C; Diehn M, Yaffe M B, Findell P R, Cantley L C, Berg L J (January 2000). "Biochemical interactions integrating Itk with the T cell receptor-initiated signaling cascade". J. Biol. Chem. (UNITED STATES) 275 (3): 2219–30. doi:10.1074/jbc.275.3.2219. ISSN 0021-9258. PMID 10636929. 
  34. ↑ Bunnell, S C; Henry P A, Kolluri R, Kirchhausen T, Rickles R J, Berg L J (October 1996). "Identification of Itk/Tsk Src homology 3 domain ligands". J. Biol. Chem. (UNITED STATES) 271 (41): 25646–56. doi:10.1074/jbc.271.41.25646. ISSN 0021-9258. PMID 8810341. 
  35. ↑ Sayeski, P P; Ali M S, Safavi A, Lyles M, Kim S O, Frank S J, Bernstein K E (November 1999). "A catalytically active Jak2 is required for the angiotensin II-dependent activation of Fyn". J. Biol. Chem. (UNITED STATES) 274 (46): 33131–42. doi:10.1074/jbc.274.46.33131. ISSN 0021-9258. PMID 10551884. 
  36. ↑ Oneyama, Chitose; Nakano Hirofumi, Sharma Sreenath V (March 2002). "UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drug". Oncogene (England) 21 (13): 2037–50. doi:10.1038/sj.onc.1205271. ISSN 0950-9232. PMID 11960376. 
  37. ↑ Fusaki, N; Iwamatsu A, Iwashima M, Fujisawa J i (March 1997). "Interaction between Sam68 and Src family tyrosine kinases, Fyn and Lck, in T cell receptor signaling". J. Biol. Chem. (UNITED STATES) 272 (10): 6214–9. doi:10.1074/jbc.272.10.6214. ISSN 0021-9258. PMID 9045636. 
  38. ↑ Lahdenperä, Juhani; Kilpeläinen Pekka, Liu Xiao Li, Pikkarainen Timo, Reponen Paula, Ruotsalainen Vesa, Tryggvason Karl (August 2003). "Clustering-induced tyrosine phosphorylation of nephrin by Src family kinases". Kidney Int. (United States) 64 (2): 404–13. doi:10.1046/j.1523-1755.2003.00097.x. ISSN 0085-2538. PMID 12846735. 
  39. ↑ Verma, Rakesh; Wharram Bryan, Kovari Iulia, Kunkel Robin, Nihalani Deepak, Wary Kishore K, Wiggins Roger C, Killen Paul, Holzman Lawrence B (June 2003). "Fyn binds to and phosphorylates the kidney slit diaphragm component Nephrin". J. Biol. Chem. (United States) 278 (23): 20716–23. doi:10.1074/jbc.M301689200. ISSN 0021-9258. PMID 12668668. 
  40. ↑ Brdicka, T; Pavlistová D, Leo A, Bruyns E, Korínek V, Angelisová P, Scherer J, Shevchenko A, Hilgert I, Cerný J, Drbal K, Kuramitsu Y, Kornacker B, Horejsí V, Schraven B (May 2000). "Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation". J. Exp. Med. (UNITED STATES) 191 (9): 1591–604. doi:10.1084/jem.191.9.1591. ISSN 0022-1007. PMC 2213442. PMID 10790433. 
  41. ↑ Gout, I; Dhand R, Panayotou G, Fry M J, Hiles I, Otsu M, Waterfield M D (December 1992). "Expression and characterization of the p85 subunit of the phosphatidylinositol 3-kinase complex and a related p85 beta protein by using the baculovirus expression system". Biochem. J. 288 (ENGLAND). ( Pt 2): 395–405. ISSN 0264-6021. PMC 1132024. PMID 1334406. 
  42. ↑ Ron, D; Napolitano E W, Voronova A, Vasquez N J, Roberts D N, Calio B L, Caothien R H, Pettiford S M, Wellik S, Mandac J B, Kauvar L M (July 1999). "Direct interaction in T-cells between thetaPKC and the tyrosine kinase p59fyn". J. Biol. Chem. (UNITED STATES) 274 (27): 19003–10. doi:10.1074/jbc.274.27.19003. ISSN 0021-9258. PMID 10383400. 
  43. ↑ Gorska, Magdalena M; Stafford Susan J, Cen Osman, Sur Sanjiv, Alam Rafeul (February 2004). "Unc119, a novel activator of Lck/Fyn, is essential for T cell activation". J. Exp. Med. (United States) 199 (3): 369–79. doi:10.1084/jem.20030589. ISSN 0022-1007. PMC 2211793. PMID 14757743. 
  44. ↑ Messina, Samantha; Onofri Franco, Bongiorno-Borbone Lucilla, Giovedì Silvia, Valtorta Flavia, Girault Jean-Antoine, Benfenati Fabio (January 2003). "Specific interactions of neuronal focal adhesion kinase isoforms with Src kinases and amphiphysin". J. Neurochem. (England) 84 (2): 253–65. doi:10.1046/j.1471-4159.2003.01519.x. ISSN 0022-3042. PMID 12558988. 
  45. ↑ Arold, S T; Ulmer T S, Mulhern T D, Werner J M, Ladbury J E, Campbell I D, Noble M E (May 2001). "The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases". J. Biol. Chem. (United States) 276 (20): 17199–205. doi:10.1074/jbc.M011185200. ISSN 0021-9258. PMID 11278857. 
  46. ↑ Ganju, R K; Hatch W C, Avraham H, Ona M A, Druker B, Avraham S, Groopman J E (March 1997). "RAFTK, a novel member of the focal adhesion kinase family, is phosphorylated and associates with signaling molecules upon activation of mature T lymphocytes". J. Exp. Med. (UNITED STATES) 185 (6): 1055–63. doi:10.1084/jem.185.6.1055. ISSN 0022-1007. PMC 2196239. PMID 9091579. 
  47. ↑ Katagiri, T; Takahashi T, Sasaki T, Nakamura S, Hattori S (June 2000). "Protein-tyrosine kinase Pyk2 is involved in interleukin-2 production by Jurkat T cells via its tyrosine 402". J. Biol. Chem. (UNITED STATES) 275 (26): 19645–52. doi:10.1074/jbc.M909828199. ISSN 0021-9258. PMID 10867021. 
  48. ↑ Qian, D; Lev S, van Oers N S, Dikic I, Schlessinger J, Weiss A (April 1997). "Tyrosine phosphorylation of Pyk2 is selectively regulated by Fyn during TCR signaling". J. Exp. Med. (UNITED STATES) 185 (7): 1253–9. doi:10.1084/jem.185.7.1253. ISSN 0022-1007. PMC 2196260. PMID 9104812. 
  49. ↑ Lim SH, Kwon SK, Lee MK, Moon J, Jeong DG, Park E et al. (2009). "Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn.". EMBO J 28 (22): 3564–78. doi:10.1038/emboj.2009.289. PMC 2782100. PMID 19816407. 
  50. ↑ Taniguchi, Sachiko; Liu Hui, Nakazawa Takanobu, Yokoyama Kazumasa, Tezuka Tohru, Yamamoto Tadashi (June 2003). "p250GAP, a neural RhoGAP protein, is associated with and phosphorylated by Fyn". Biochem. Biophys. Res. Commun. (United States) 306 (1): 151–5. doi:10.1016/S0006-291X(03)00923-9. ISSN 0006-291X. PMID 12788081. 
  51. ↑ Li, Chengjun; Iosef Cristiana, Jia Christina Y H, Han Victor K M, Li Shawn Shun-Cheng (February 2003). "Dual functional roles for the X-linked lymphoproliferative syndrome gene product SAP/SH2D1A in signaling through the signaling lymphocyte activation molecule (SLAM) family of immune receptors". J. Biol. Chem. (United States) 278 (6): 3852–9. doi:10.1074/jbc.M206649200. ISSN 0021-9258. PMID 12458214. 
  52. ↑ Chan, Betty; Lanyi Arpad, Song Hyun Kyu, Griesbach Jan, Simarro-Grande Maria, Poy Florence, Howie Duncan, Sumegi Janos, Terhorst Cox, Eck Michael J (February 2003). "SAP couples Fyn to SLAM immune receptors". Nat. Cell Biol. (England) 5 (2): 155–60. doi:10.1038/ncb920. ISSN 1465-7392. PMID 12545174. 
  53. ↑ Marie-Cardine, A; Bruyns E, Eckerskorn C, Kirchgessner H, Meuer S C, Schraven B (June 1997). "Molecular cloning of SKAP55, a novel protein that associates with the protein tyrosine kinase p59fyn in human T-lymphocytes". J. Biol. Chem. (UNITED STATES) 272 (26): 16077–80. doi:10.1074/jbc.272.26.16077. ISSN 0021-9258. PMID 9195899. 
  54. ↑ Wu, Liangtang; Yu Zhenbao, Shen Shi-Hsiang (October 2002). "SKAP55 recruits to lipid rafts and positively mediates the MAPK pathway upon T cell receptor activation". J. Biol. Chem. (United States) 277 (43): 40420–7. doi:10.1074/jbc.M206023200. ISSN 0021-9258. PMID 12171928. 
  55. ↑ Linseman, D A; Heidenreich K A, Fisher S K (February 2001). "Stimulation of M3 muscarinic receptors induces phosphorylation of the Cdc42 effector activated Cdc42Hs-associated kinase-1 via a Fyn tyrosine kinase signaling pathway". J. Biol. Chem. (United States) 276 (8): 5622–8. doi:10.1074/jbc.M006812200. ISSN 0021-9258. PMID 11087735. 
  56. ↑ Iwasaki, Y; Gay B, Wada K, Koizumi S (July 1998). "Association of the Src family tyrosine kinase Fyn with TrkB". J. Neurochem. (UNITED STATES) 71 (1): 106–11. doi:10.1046/j.1471-4159.1998.71010106.x. ISSN 0022-3042. PMID 9648856. 
  57. ↑ Hisatsune, Chihiro; Kuroda Yukiko, Nakamura Kyoko, Inoue Takafumi, Nakamura Takeshi, Michikawa Takayuki, Mizutani Akihiro, Mikoshiba Katsuhiko (April 2004). "Regulation of TRPC6 channel activity by tyrosine phosphorylation". J. Biol. Chem. (United States) 279 (18): 18887–94. doi:10.1074/jbc.M311274200. ISSN 0021-9258. PMID 14761972. 
  58. ↑ Uddin, S; Sher D A, Alsayed Y, Pons S, Colamonici O R, Fish E N, White M F, Platanias L C (June 1997). "Interaction of p59fyn with interferon-activated Jak kinases". Biochem. Biophys. Res. Commun. (UNITED STATES) 235 (1): 83–8. doi:10.1006/bbrc.1997.6741. ISSN 0006-291X. PMID 9196040. 
  59. ↑ Banin, S; Truong O, Katz D R, Waterfield M D, Brickell P M, Gout I (August 1996). "Wiskott-Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases". Curr. Biol. (ENGLAND) 6 (8): 981–8. doi:10.1016/S0960-9822(02)00642-5. ISSN 0960-9822. PMID 8805332. 
  60. ↑ Banin, S; Gout I, Brickell P (August 1999). "Interaction between Wiskott-Aldrich Syndrome protein (WASP) and the Fyn protein-tyrosine kinase". Mol. Biol. Rep. (NETHERLANDS) 26 (3): 173–7. doi:10.1023/A:1006954206151. ISSN 0301-4851. PMID 10532312. 
  61. ↑ Rivero-Lezcano, O M; Marcilla A, Sameshima J H, Robbins K C (October 1995). "Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains". Mol. Cell. Biol. (UNITED STATES) 15 (10): 5725–31. ISSN 0270-7306. PMC 230823. PMID 7565724. 
  62. ↑ Neumeister, E N; Zhu Y, Richard S, Terhorst C, Chan A C, Shaw A S (June 1995). "Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins". Mol. Cell. Biol. (UNITED STATES) 15 (6): 3171–8. ISSN 0270-7306. PMC 230549. PMID 7760813. 

Further reading

  • O'Sullivan E, Kinnon C, Brickell P (1999). "Wiskott-Aldrich syndrome protein, WASP.". Int. J. Biochem. Cell Biol. 31 (3-4): 383–7. doi:10.1016/S1357-2725(98)00118-6. PMID 10224664. 
  • Sasaoka T, Kobayashi M (2000). "The functional significance of Shc in insulin signaling as a substrate of the insulin receptor.". Endocr. J. 47 (4): 373–81. doi:10.1507/endocrj.47.373. PMID 11075717. 
  • Leavitt SA, SchOn A, Klein JC, et al. (2004). "Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm.". Curr. Protein Pept. Sci. 5 (1): 1–8. doi:10.2174/1389203043486955. PMID 14965316. 
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  • 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. PMID 15638726. 
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