FYN

FYN

FYN oncogene related to SRC, FGR, YES, also known as FYN, is a human gene.cite journal | author = Semba K, Nishizawa M, Miyajima N, Yoshida MC, Sukegawa J, Yamanashi Y, Sasaki M, Yamamoto T, Toyoshima K| title = yes-related protooncogene, syn, belongs to the protein-tyrosine kinase family | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 83 | issue = 15 | pages = 5459–63 | year = 1986 | month = August | pmid = 3526330 | pmc = 386306 | doi = | url = http://www.pnas.org/content/83/15/5459 | issn = ]

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. [cite web | title = Entrez Gene: FYN FYN oncogene related to SRC, FGR, YES| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2534| accessdate = ]

Function

Fyn is a protein, present in the signaling pathway of [integrin] s, which activates ras. Fyn is a tyrosine specific phospho-transferase that is a member of the Src family of tyrosine protein kinases.cite journal | author = Resh MD | title = Fyn, a Src family tyrosine kinase | journal = The international journal of biochemistry & cell biology | volume = 30 | issue = 11 | pages = 1159–62 | year = 1998 | month = November | pmid = 9839441 | doi = 10.1016/S1357-2725(98)0 | url = | issn = ] 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 (4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo [3,4-"d"] pyrimidine; 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,cite journal | author = Zamoyska R, Basson A, Filby A, Legname G, Lovatt M, Seddon B | title = The influence of the src-family kinases, Lck and Fyn, on T cell differentiation, survival and activation | journal = Immunological reviews | volume = 191 | issue = | pages = 107–18 | year = 2003 | month = February | pmid = 12614355 | doi = 10.1034/j.1600-065X.2003.00015.x | url = | issn = ] cite journal | author = Palacios EH, Weiss A | title = Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation | journal = Oncogene | volume = 23 | issue = 48 | pages = 7990–8000 | year = 2004 | month = October | pmid = 15489916 | doi = 10.1038/sj.onc.1208074 | url = | issn = ] 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.

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=O'Sullivan E, Kinnon C, Brickell P |title=Wiskott-Aldrich syndrome protein, WASP. |journal=Int. J. Biochem. Cell Biol. |volume=31 |issue= 3-4 |pages= 383–7 |year= 1999 |pmid= 10224664 |doi=
*cite journal | author=Sasaoka T, Kobayashi M |title=The functional significance of Shc in insulin signaling as a substrate of the insulin receptor. |journal=Endocr. J. |volume=47 |issue= 4 |pages= 373–81 |year= 2000 |pmid= 11075717 |doi=
*cite journal | author=Leavitt SA, SchOn A, Klein JC, "et al." |title=Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm. |journal=Curr. Protein Pept. Sci. |volume=5 |issue= 1 |pages= 1–8 |year= 2004 |pmid= 14965316 |doi=
*cite journal | author=Tolstrup M, Ostergaard L, Laursen AL, "et al." |title=HIV/SIV escape from immune surveillance: focus on Nef. |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 141–51 |year= 2004 |pmid= 15078178 |doi=
*cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87–94 |year= 2005 |pmid= 15638726 |doi=
*cite journal | author=Stove V, Verhasselt B |title=Modelling thymic HIV-1 Nef effects. |journal=Curr. HIV Res. |volume=4 |issue= 1 |pages= 57–64 |year= 2006 |pmid= 16454711 |doi=

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