products references :
Fas ligand mediates activation-induced cell death in human T lymphocytes.Alderson M.J. Exp. Med. 181:71-77(1995)
Human Fas ligand
gene structure, chromosomal location and species specificity.Takahashi T., Tanaka M., Inazawa J., Abe T., Suda T., Nagata S.Int. Immunol. 6:1567-1574(1994)
Schaetzlein C.E., Poehlmann R., Philippsen P., Eibel H.Role of Fas ligand in apoptosis induced by hepatitis C virus infection.Mita E., Hayashi N., Iio S., Takehara T., Hijioka T., Kasahara A., Fusamoto H., Kamada T.Biochem. Biophys. Res. Commun. 204:468-474(1994)
Isolation and characterization of a new naturally occurring variant of human Fas ligand that is expressed only in membrane bound form.Zeytun A., Nagarkatti M., Nagarkatti P.S. The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006)
Matsumura M., Nakanishi Y., Ohba Y. Fas ligand mutation in a patient with systemic lupus erythematosus and lymphoproliferative disease.Wu J., Wilson J., He J., Xiang L., Schur P.H., Mountz J.D.J. Clin. Invest. 98:1107-1113(1996)
Characterization of Fas (Apo-1, CD95)
-Fas ligand interaction.Schneider P., Bodmer J.-L., Holler N., Mattmann C., Scuderi P., Terskikh A., Peitsch M.C., Tschopp J.J. Biol. Chem. 272:18827-18833(1997)
Downregulation of Fas ligand by shedding.Tanaka M., Itai T., Adachi M., Nagata S.Nat. Med. 4:31-36(1998)
The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells.Kirkin V., Cahuzac N., Guardiola-Serrano F., Huault S., Luckerath K., Friedmann E., Novac N., Wels W.S., Martoglio B., Hueber A.O., Zornig M.Cell Death Differ. 14:1678-1687(2007)
Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation.Zuccato E., Blott E.J., Holt O., Sigismund S., Shaw M., Bossi G., Griffiths G.M.J. Cell Sci. 120:191-199(2007)
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uniprot summary :
FasL: Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells. May be involved in cytotoxic T-cell mediated apoptosis and in T-cell development. TNFRSF6/FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. Binding to the decoy receptor TNFRSF6B/DcR3 modulates its effects. Homotrimer (Probable). Interacts with ARHGAP9, BAIAP2L1, BTK, CACNB3, CACNB4, CRK, DLG2, DNMBP, DOCK4, EPS8L3, FGR, FYB, FYN, HCK, ITK, ITSN2, KALRN, LYN, MACC1, MIA, MPP4, MYO15A, NCF1, NCK1, NCK2, NCKIPSD, OSTF1, PIK3R1, PSTPIP1, RIMBP3C, SAMSN1, SH3GL3, SH3PXD2B, SH3PXD2A, SH3RF2, SKAP2, SNX33, SNX9, SORBS3, SPTA1, SRC, SRGAP1, SRGAP2, SRGAP3, TEC, TJP3 and YES1. Belongs to the tumor necrosis factor family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: Cytokine; Apoptosis; Membrane protein, integral. Chromosomal Location of Human Ortholog: 1q23. Cellular Component: caveola; external side of plasma membrane; extracellular region; extracellular space; integral to plasma membrane; lysosomal lumen; nucleus; perinuclear region of cytoplasm; plasma membrane. Molecular Function: cytokine activity; protein binding; receptor binding; tumor necrosis factor receptor binding. Biological Process: apoptosis; caspase activation; cell surface receptor linked signal transduction; cell-cell signaling; cellular chloride ion homeostasis; endosomal lumen acidification; immune response; induction of apoptosis via death domain receptors; inflammatory cell apoptosis; negative regulation of angiogenesis; negative regulation of caspase activity; negative regulation of transcription from RNA polymerase II promoter; positive regulation of apoptosis; positive regulation of cell proliferation; positive regulation of epidermal growth factor receptor signaling pathway; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of neuron apoptosis; programmed cell death; response to lipopolysaccharide; retinal cell programmed cell death; signal transduction; transcription, DNA-dependent. Disease: Autoimmune Lymphoproliferative Syndrome; Lung Cancer