메뉴 건너뛰기




Volumn 316, Issue 9, 2010, Pages 1513-1522

Identification of a lysine-rich region of Fas as a raft nanodomain targeting signal necessary for Fas-mediated cell death

Author keywords

Actin cytoskeleton; Cell death signalling; Fas receptor; Raft nanodomains

Indexed keywords

FAS ANTIGEN;

EID: 77952891292     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2010.03.002     Document Type: Article
Times cited : (18)

References (37)
  • 1
    • 85047692516 scopus 로고    scopus 로고
    • Signalling pathways of the TNF superfamily: a double-edged sword
    • Aggarwal B.B. Signalling pathways of the TNF superfamily: a double-edged sword. Nat. Rev. Immunol. 2003, 3:745-756.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 745-756
    • Aggarwal, B.B.1
  • 2
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: signaling and modulation
    • Ashkenazi A., Dixit V.M. Death receptors: signaling and modulation. Science 1998, 281:1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 3
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel F.C., Hellbardt S., Behrmann I., Germer M., Pawlita M., Krammer P.H., Peter M.E. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. Embo J. 1995, 14:5579-5588.
    • (1995) Embo J. , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3    Germer, M.4    Pawlita, M.5    Krammer, P.H.6    Peter, M.E.7
  • 5
    • 50249100375 scopus 로고    scopus 로고
    • Death receptor Fas (CD95) signaling in the central nervous system: tuning neuroplasticity?
    • Reich A., Spering C., Schulz J.B. Death receptor Fas (CD95) signaling in the central nervous system: tuning neuroplasticity?. Trends Neurosci. 2008, 31:478-486.
    • (2008) Trends Neurosci. , vol.31 , pp. 478-486
    • Reich, A.1    Spering, C.2    Schulz, J.B.3
  • 6
    • 4143108125 scopus 로고    scopus 로고
    • CD95 ligand induces motility and invasiveness of apoptosis-resistant tumor cells
    • Barnhart B.C., Legembre P., Pietras E., Bubici C., Franzoso G., Peter M.E. CD95 ligand induces motility and invasiveness of apoptosis-resistant tumor cells. Embo J. 2004, 23:3175-3185.
    • (2004) Embo J. , vol.23 , pp. 3175-3185
    • Barnhart, B.C.1    Legembre, P.2    Pietras, E.3    Bubici, C.4    Franzoso, G.5    Peter, M.E.6
  • 8
    • 0036195136 scopus 로고    scopus 로고
    • An essential role for membrane rafts in the initiation of Fas/CD95-triggered cell death in mouse thymocytes
    • Hueber A.O., Bernard A.M., Herincs Z., Couzinet A., He H.T. An essential role for membrane rafts in the initiation of Fas/CD95-triggered cell death in mouse thymocytes. EMBO Rep. 2002, 3:190-196.
    • (2002) EMBO Rep. , vol.3 , pp. 190-196
    • Hueber, A.O.1    Bernard, A.M.2    Herincs, Z.3    Couzinet, A.4    He, H.T.5
  • 9
  • 10
    • 16844381848 scopus 로고    scopus 로고
    • The extracellular domains of FasL and Fas are sufficient for the formation of supramolecular FasL-Fas clusters of high stability
    • Henkler F., Behrle E., Dennehy K.M., Wicovsky A., Peters N., Warnke C., Pfizenmaier K., Wajant H. The extracellular domains of FasL and Fas are sufficient for the formation of supramolecular FasL-Fas clusters of high stability. J. Cell Biol. 2005, 168:1087-1098.
    • (2005) J. Cell Biol. , vol.168 , pp. 1087-1098
    • Henkler, F.1    Behrle, E.2    Dennehy, K.M.3    Wicovsky, A.4    Peters, N.5    Warnke, C.6    Pfizenmaier, K.7    Wajant, H.8
  • 12
    • 56349087320 scopus 로고    scopus 로고
    • The extracellular glycosphingolipid-binding motif of Fas defines its internalization route, mode and outcome of signals upon activation by ligand
    • Chakrabandhu K., Huault S., Garmy N., Fantini J., Stebe E., Mailfert S., Marguet D., Hueber A.O. The extracellular glycosphingolipid-binding motif of Fas defines its internalization route, mode and outcome of signals upon activation by ligand. Cell Death Differ. 2008, 15:1824-1837.
    • (2008) Cell Death Differ. , vol.15 , pp. 1824-1837
    • Chakrabandhu, K.1    Huault, S.2    Garmy, N.3    Fantini, J.4    Stebe, E.5    Mailfert, S.6    Marguet, D.7    Hueber, A.O.8
  • 14
    • 0034597013 scopus 로고    scopus 로고
    • CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism of the CD95 apoptotic pathway
    • Parlato S., Giammarioli A.M., Logozzi M., Lozupone F., Matarrese P., Luciani F., Falchi M., Malorni W., Fais S. CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism of the CD95 apoptotic pathway. Embo J. 2000, 19:5123-5134.
    • (2000) Embo J. , vol.19 , pp. 5123-5134
    • Parlato, S.1    Giammarioli, A.M.2    Logozzi, M.3    Lozupone, F.4    Matarrese, P.5    Luciani, F.6    Falchi, M.7    Malorni, W.8    Fais, S.9
  • 16
    • 0347052860 scopus 로고    scopus 로고
    • CD4 receptor localized to non-raft membrane microdomains supports HIV-1 entry. Identification of a novel raft localization marker in CD4
    • Popik W., Alce T.M. CD4 receptor localized to non-raft membrane microdomains supports HIV-1 entry. Identification of a novel raft localization marker in CD4. J. Biol. Chem. 2004, 279:704-712.
    • (2004) J. Biol. Chem. , vol.279 , pp. 704-712
    • Popik, W.1    Alce, T.M.2
  • 17
    • 28444443820 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization
    • Wawrezinieck L., Rigneault H., Marguet D., Lenne P.F. Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization. Biophys. J. 2005, 89:4029-4042.
    • (2005) Biophys. J. , vol.89 , pp. 4029-4042
    • Wawrezinieck, L.1    Rigneault, H.2    Marguet, D.3    Lenne, P.F.4
  • 20
    • 0842266659 scopus 로고    scopus 로고
    • Labeling and quantifying sites of protein palmitoylation
    • Drisdel R.C., Green W.N. Labeling and quantifying sites of protein palmitoylation. Biotechniques 2004, 36:276-285.
    • (2004) Biotechniques , vol.36 , pp. 276-285
    • Drisdel, R.C.1    Green, W.N.2
  • 21
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias D.A., Violin J.D., Newton A.C., Tsien R.Y. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 2002, 296:913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 22
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signaling proteins: regulation and function
    • Smotrys J.E., Linder M.E. Palmitoylation of intracellular signaling proteins: regulation and function. Annu. Rev. Biochem. 2004, 73:559-587.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 559-587
    • Smotrys, J.E.1    Linder, M.E.2
  • 23
    • 0037067715 scopus 로고    scopus 로고
    • Second cysteine-rich region of epidermal growth factor receptor contains targeting information for caveolae/rafts
    • Yamabhai M., Anderson R.G. Second cysteine-rich region of epidermal growth factor receptor contains targeting information for caveolae/rafts. J. Biol. Chem. 2002, 277:24843-24846.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24843-24846
    • Yamabhai, M.1    Anderson, R.G.2
  • 24
    • 0037333399 scopus 로고    scopus 로고
    • Transmembrane domains 1 and 2 of the latent membrane protein 1 of Epstein-Barr virus contain a lipid raft targeting signal and play a critical role in cytostasis
    • Coffin W.F., Geiger T.R., Martin J.M. Transmembrane domains 1 and 2 of the latent membrane protein 1 of Epstein-Barr virus contain a lipid raft targeting signal and play a critical role in cytostasis. J. Virol. 2003, 77:3749-3758.
    • (2003) J. Virol. , vol.77 , pp. 3749-3758
    • Coffin, W.F.1    Geiger, T.R.2    Martin, J.M.3
  • 25
    • 14844337436 scopus 로고    scopus 로고
    • The cytosolic domains of Ca2+-sensitive adenylyl cyclases dictate their targeting to plasma membrane lipid rafts
    • Crossthwaite A.J., Seebacher T., Masada N., Ciruela A., Dufraux K., Schultz J.E., Cooper D.M. The cytosolic domains of Ca2+-sensitive adenylyl cyclases dictate their targeting to plasma membrane lipid rafts. J. Biol. Chem. 2005, 280:6380-6391.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6380-6391
    • Crossthwaite, A.J.1    Seebacher, T.2    Masada, N.3    Ciruela, A.4    Dufraux, K.5    Schultz, J.E.6    Cooper, D.M.7
  • 26
    • 62749084512 scopus 로고    scopus 로고
    • Palmitoylation of the TRAIL receptor DR4 confers an efficient TRAIL-induced cell death signalling
    • 2 p following 192
    • Rossin A., Derouet M., Abdel-Sater F., Hueber A.O. Palmitoylation of the TRAIL receptor DR4 confers an efficient TRAIL-induced cell death signalling. Biochem. J. 2009, 419:185-192. 2 p following 192.
    • (2009) Biochem. J. , vol.419 , pp. 185-192
    • Rossin, A.1    Derouet, M.2    Abdel-Sater, F.3    Hueber, A.O.4
  • 27
    • 2942614991 scopus 로고    scopus 로고
    • Differential regulation of TNF-R1 signaling: lipid raft dependency of p42mapk/erk2 activation, but not NF-kappaB activation
    • Doan J.E., Windmiller D.A., Riches D.W. Differential regulation of TNF-R1 signaling: lipid raft dependency of p42mapk/erk2 activation, but not NF-kappaB activation. J. Immunol. 2004, 172:7654-7660.
    • (2004) J. Immunol. , vol.172 , pp. 7654-7660
    • Doan, J.E.1    Windmiller, D.A.2    Riches, D.W.3
  • 28
    • 33845921822 scopus 로고    scopus 로고
    • Spatial compartmentalization of tumor necrosis factor (TNF) receptor 1-dependent signaling pathways in human airway smooth muscle cells. Lipid rafts are essential for TNF-alpha-mediated activation of RhoA but dispensable for the activation of the NF-kappaB and MAPK pathways.
    • Hunter I., Nixon G.F. Spatial compartmentalization of tumor necrosis factor (TNF) receptor 1-dependent signaling pathways in human airway smooth muscle cells. Lipid rafts are essential for TNF-alpha-mediated activation of RhoA but dispensable for the activation of the NF-kappaB and MAPK pathways. J. Biol. Chem. 2006, 281:34705-34715.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34705-34715
    • Hunter, I.1    Nixon, G.F.2
  • 29
    • 0038742813 scopus 로고    scopus 로고
    • Recruitment of TNF receptor 1 to lipid rafts is essential for TNFalpha-mediated NF-kappaB activation
    • Legler D.F., Micheau O., Doucey M.A., Tschopp J., Bron C. Recruitment of TNF receptor 1 to lipid rafts is essential for TNFalpha-mediated NF-kappaB activation. Immunity 2003, 18:655-664.
    • (2003) Immunity , vol.18 , pp. 655-664
    • Legler, D.F.1    Micheau, O.2    Doucey, M.A.3    Tschopp, J.4    Bron, C.5
  • 31
    • 29144512451 scopus 로고    scopus 로고
    • Raf-1 sets the threshold of Fas sensitivity by modulating Rok-alpha signaling
    • Piazzolla D., Meissl K., Kucerova L., Rubiolo C., Baccarini M. Raf-1 sets the threshold of Fas sensitivity by modulating Rok-alpha signaling. J. Cell Biol. 2005, 171:1013-1022.
    • (2005) J. Cell Biol. , vol.171 , pp. 1013-1022
    • Piazzolla, D.1    Meissl, K.2    Kucerova, L.3    Rubiolo, C.4    Baccarini, M.5
  • 32
    • 0034631843 scopus 로고    scopus 로고
    • Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane
    • Gautreau A., Louvard D., Arpin M. Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane. J. Cell Biol. 2000, 150:193-203.
    • (2000) J. Cell Biol. , vol.150 , pp. 193-203
    • Gautreau, A.1    Louvard, D.2    Arpin, M.3
  • 33
    • 58749115072 scopus 로고    scopus 로고
    • Rho-ROCK-dependent ezrin-radixin-moesin phosphorylation regulates Fas-mediated apoptosis in Jurkat cells
    • Hebert M., Potin S., Sebbagh M., Bertoglio J., Breard J., Hamelin J. Rho-ROCK-dependent ezrin-radixin-moesin phosphorylation regulates Fas-mediated apoptosis in Jurkat cells. J. Immunol. 2008, 181:5963-5973.
    • (2008) J. Immunol. , vol.181 , pp. 5963-5973
    • Hebert, M.1    Potin, S.2    Sebbagh, M.3    Bertoglio, J.4    Breard, J.5    Hamelin, J.6
  • 34
    • 50249118029 scopus 로고    scopus 로고
    • A novel juxtamembrane domain in tumor necrosis factor receptor superfamily molecules activates Rac1 and controls neurite growth
    • Ruan W., Lee C.T., Desbarats J. A novel juxtamembrane domain in tumor necrosis factor receptor superfamily molecules activates Rac1 and controls neurite growth. Mol. Biol. Cell 2008, 19:3192-3202.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3192-3202
    • Ruan, W.1    Lee, C.T.2    Desbarats, J.3
  • 35
    • 39449095203 scopus 로고    scopus 로고
    • Regulating Vav1 phosphorylation by the SHP-1 tyrosine phosphatase is a fine-tuning mechanism for the negative regulation of DISC formation and Fas-mediated cell death signaling
    • Koncz G., Kerekes K., Chakrabandhu K., Hueber A.O. Regulating Vav1 phosphorylation by the SHP-1 tyrosine phosphatase is a fine-tuning mechanism for the negative regulation of DISC formation and Fas-mediated cell death signaling. Cell Death Differ. 2008, 15:494-503.
    • (2008) Cell Death Differ. , vol.15 , pp. 494-503
    • Koncz, G.1    Kerekes, K.2    Chakrabandhu, K.3    Hueber, A.O.4
  • 36
    • 0036155137 scopus 로고    scopus 로고
    • Death receptors bind SHP-1 and block cytokine-induced anti-apoptotic signaling in neutrophils
    • Daigle I., Yousefi S., Colonna M., Green D.R., Simon H.U. Death receptors bind SHP-1 and block cytokine-induced anti-apoptotic signaling in neutrophils. Nat. Med. 2002, 8:61-67.
    • (2002) Nat. Med. , vol.8 , pp. 61-67
    • Daigle, I.1    Yousefi, S.2    Colonna, M.3    Green, D.R.4    Simon, H.U.5
  • 37
    • 14944344230 scopus 로고    scopus 로고
    • Integrin-dependent interaction of lipid rafts with the actin cytoskeleton in activated human platelets
    • Bodin S., Soulet C., Tronchere H., Sie P., Gachet C., Plantavid M., Payrastre B. Integrin-dependent interaction of lipid rafts with the actin cytoskeleton in activated human platelets. J. Cell Sci. 2005, 118:759-769.
    • (2005) J. Cell Sci. , vol.118 , pp. 759-769
    • Bodin, S.1    Soulet, C.2    Tronchere, H.3    Sie, P.4    Gachet, C.5    Plantavid, M.6    Payrastre, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.