메뉴 건너뛰기
Journal of Virology
Volumn 88, Issue 17, 2014, Pages 10039-10055
Influenza a virus hemagglutinin and neuraminidase mutually accelerate their apical targeting through clustering of lipid rafts
Author keywords

[No Author keywords available]
Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ; NA PROTEIN, INFLUENZA A VIRUS; PROTEIN BINDING; SIALIDASE; VIRUS PROTEIN;
EID: 84918811386     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00586-14     Document Type: Article
Times cited : (47)
References (59)
  • 1
    • 68949192806 scopus 로고    scopus 로고
    • Influenza virus morphogenesis and budding
    • Nayak DP, Balogun RA, Yamada H, Zhou ZH, Barman S. 2009. Influenza virus morphogenesis and budding. Virus Res. 143:147-161. http://dx.doi.org/10.1016/j.virusres.2009.05.010.
    • (2009) Virus Res , vol.143 , pp. 147-161
    • Nayak, D.P.1    Balogun, R.A.2    Yamada, H.3    Zhou, Z.H.4    Barman, S.5
  • 2
    • 0032514155 scopus 로고    scopus 로고
    • Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells
    • Lin S, Naim HY, Rodriguez AC, Roth MG. 1998. Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells. J. Cell Biol. 142:51-57. http://dx.doi.org/10.1083/jcb.142.1.51.
    • (1998) J. Cell Biol , vol.142 , pp. 51-57
    • Lin, S.1    Naim, H.Y.2    Rodriguez, A.C.3    Roth, M.G.4
  • 3
    • 0033934725 scopus 로고    scopus 로고
    • Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association
    • Barman S, Nayak DP. 2000. Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association. J. Virol. 74:6538-6545. http://dx.doi.org/10.1128/JVI.74.14.6538-6545.2000.
    • (2000) J. Virol , vol.74 , pp. 6538-6545
    • Barman, S.1    Nayak, D.P.2
  • 4
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele P, Roth MG, Simons K. 1997. Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J. 16:5501-5508. http://dx.doi.org/10.1093/emboj/16.18.5501.
    • (1997) EMBO J , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 5
    • 0347482478 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fu-sion
    • Takeda M, Leser GP, Russell CJ, Lamb RA. 2003. Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fu-sion. Proc. Natl. Acad. Sci. U. S. A. 100:14610-14617. http://dx.doi.org/10.1073/pnas.2235620100.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 14610-14617
    • Takeda, M.1    Leser, G.P.2    Russell, C.J.3    Lamb, R.A.4
  • 6
    • 27644440465 scopus 로고    scopus 로고
    • Influenza virus assembly and budding in raft-derived microdomains: a quantitative analysis of the surface distribution of HA, NA and M2 proteins
    • Leser GP, Lamb RA. 2005. Influenza virus assembly and budding in raft-derived microdomains: a quantitative analysis of the surface distribution of HA, NA and M2 proteins. Virology 342:215-227. http://dx.doi.org/10.1016/j.virol.2005.09.049.
    • (2005) Virology , vol.342 , pp. 215-227
    • Leser, G.P.1    Lamb, R.A.2
  • 7
    • 0033995067 scopus 로고    scopus 로고
    • Influenza virus assembly and lipid raft microdomains: a role for the cytoplasmic tails of the spike glycoproteins
    • Zhang J, Pekosz A, Lamb RA. 2000. Influenza virus assembly and lipid raft microdomains: a role for the cytoplasmic tails of the spike glycoproteins. J. Virol. 74:4634-4644. http://dx.doi.org/10.1128/JVI.74.10.4634-4644.2000.
    • (2000) J. Virol , vol.74 , pp. 4634-4644
    • Zhang, J.1    Pekosz, A.2    Lamb, R.A.3
  • 8
    • 27144533145 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly
    • Chen BJ, Takeda M, Lamb RA. 2005. Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly. J. Virol. 79:13673-13684. http://dx.doi.org/10.1128/JVI.79.21.13673-13684.2005.
    • (2005) J. Virol , vol.79 , pp. 13673-13684
    • Chen, B.J.1    Takeda, M.2    Lamb, R.A.3
  • 9
    • 77956637693 scopus 로고    scopus 로고
    • Influenza virus M2 protein mediates ESCRT-independent membrane scission
    • Rossman JS, Jing X, Leser GP, Lamb RA. 2010. Influenza virus M2 protein mediates ESCRT-independent membrane scission. Cell 142:902-913. http://dx.doi.org/10.1016/j.cell.2010.08.029.
    • (2010) Cell , vol.142 , pp. 902-913
    • Rossman, J.S.1    Jing, X.2    Leser, G.P.3    Lamb, R.A.4
  • 11
  • 12
    • 33749180269 scopus 로고    scopus 로고
    • Clustering of raft-associated proteins in the external membrane leaflet modulates internal leaflet H-ras diffusion and signaling
    • Eisenberg S, Shvartsman DE, Ehrlich M, Henis YI. 2006. Clustering of raft-associated proteins in the external membrane leaflet modulates internal leaflet H-ras diffusion and signaling. Mol. Cell. Biol. 26:7190-7200. http://dx.doi.org/10.1128/MCB.01059-06.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 7190-7200
    • Eisenberg, S.1    Shvartsman, D.E.2    Ehrlich, M.3    Henis, Y.I.4
  • 13
    • 57649233034 scopus 로고    scopus 로고
    • Compartmentalization of phosphatidylinositol 4, 5-bisphosphate signaling evidenced using targeted phosphatases
    • Johnson CM, Chichili GR, Rodgers W. 2008. Compartmentalization of phosphatidylinositol 4, 5-bisphosphate signaling evidenced using targeted phosphatases. J. Biol. Chem. 283:29920-29928. http://dx.doi.org/10.1074/jbc.M805921200.
    • (2008) J. Biol. Chem , vol.283 , pp. 29920-29928
    • Johnson, C.M.1    Chichili, G.R.2    Rodgers, W.3
  • 14
    • 0029839393 scopus 로고    scopus 로고
    • Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells
    • Kundu A, Avalos RT, Sanderson CM, Nayak DP. 1996. Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells. J. Virol. 70:6508-6515.
    • (1996) J. Virol , vol.70 , pp. 6508-6515
    • Kundu, A.1    Avalos, R.T.2    Sanderson, C.M.3    Nayak, D.P.4
  • 15
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. 1997. Functional rafts in cell membranes. Nature 387:569-572. http://dx.doi.org/10.1038/42408.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 16
    • 0032559854 scopus 로고    scopus 로고
    • Cholesterol is required for surface transport of influenza virus hemagglutinin
    • Keller P, Simons K. 1998. Cholesterol is required for surface transport of influenza virus hemagglutinin. J. Cell Biol. 140:1357-1367. http://dx.doi.org/10.1083/jcb.140.6.1357.
    • (1998) J. Cell Biol , vol.140 , pp. 1357-1367
    • Keller, P.1    Simons, K.2
  • 17
    • 9444267662 scopus 로고    scopus 로고
    • Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins
    • Paladino S, Sarnataro D, Pillich R, Tivodar S, Nitsch L, Zurzolo C. 2004. Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins. J. Cell Biol. 167:699-709. http://dx.doi.org/10.1083/jcb.200407094.
    • (2004) J. Cell Biol , vol.167 , pp. 699-709
    • Paladino, S.1    Sarnataro, D.2    Pillich, R.3    Tivodar, S.4    Nitsch, L.5    Zurzolo, C.6
  • 18
    • 0033858756 scopus 로고    scopus 로고
    • Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 protein
    • Ali A, Avalos RT, Ponimaskin E, Nayak DP. 2000. Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 protein. J. Virol. 74:8709-8719. http://dx.doi.org/10.1128/JVI.74.18.8709-8719.2000.
    • (2000) J. Virol , vol.74 , pp. 8709-8719
    • Ali, A.1    Avalos, R.T.2    Ponimaskin, E.3    Nayak, D.P.4
  • 19
    • 34547584458 scopus 로고    scopus 로고
    • Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions
    • Noton SL, Medcalf E, Fisher D, Mullin AE, Elton D, Digard P. 2007. Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions. J. Gen. Virol. 88:2280-2290. http://dx.doi.org/10.1099/vir.0.82809-0.
    • (2007) J. Gen. Virol , vol.88 , pp. 2280-2290
    • Noton, S.L.1    Medcalf, E.2    Fisher, D.3    Mullin, A.E.4    Elton, D.5    Digard, P.6
  • 20
    • 53749092893 scopus 로고    scopus 로고
    • The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding
    • Chen BJ, Leser GP, Jackson D, Lamb RA. 2008. The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding. J. Virol. 82:10059-10070. http://dx.doi.org/10.1128/JVI.01184-08.
    • (2008) J. Virol , vol.82 , pp. 10059-10070
    • Chen, B.J.1    Leser, G.P.2    Jackson, D.3    Lamb, R.A.4
  • 22
    • 0028102718 scopus 로고
    • The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity
    • Jin H, Leser GP, Lamb RA. 1994. The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity. EMBO J. 13:5504-5515.
    • (1994) EMBO J , vol.13 , pp. 5504-5515
    • Jin, H.1    Leser, G.P.2    Lamb, R.A.3
  • 23
    • 0029014741 scopus 로고
    • The cytoplasmic tail of the neuraminidase protein of influenza A virus does not play an important role in the packaging of this protein into viral envelopes
    • Garcia-Sastre A, Palese P. 1995. The cytoplasmic tail of the neuraminidase protein of influenza A virus does not play an important role in the packaging of this protein into viral envelopes. Virus Res. 37:37-47. http://dx.doi.org/10.1016/0168-1702(95)00017-K.
    • (1995) Virus Res , vol.37 , pp. 37-47
    • Garcia-Sastre, A.1    Palese, P.2
  • 24
    • 84856461452 scopus 로고    scopus 로고
    • Epitope mapping of neutralizing monoclonal antibody in avian influenza A H5N1 virus hemagglutinin
    • Ohkura T, Kikuchi Y, Kono N, Itamura S, Komase K, Momose F, Morikawa Y. 2012. Epitope mapping of neutralizing monoclonal antibody in avian influenza A H5N1 virus hemagglutinin. Biochem. Biophys. Res. Commun. 418:38-43. http://dx.doi.org/10.1016/j.bbrc.2011.12.108.
    • (2012) Biochem. Biophys. Res. Commun , vol.418 , pp. 38-43
    • Ohkura, T.1    Kikuchi, Y.2    Kono, N.3    Itamura, S.4    Komase, K.5    Momose, F.6    Morikawa, Y.7
  • 25
    • 78650878020 scopus 로고    scopus 로고
    • Hsc70 regulates the nuclear export but not the import of influenza viral RNP: a possible target for the development of anti-influenza virus drugs
    • Watanabe K, Takizawa N, Noda S, Tsukahara F, Maru Y, Kobayashi N. 2008. Hsc70 regulates the nuclear export but not the import of influenza viral RNP: a possible target for the development of anti-influenza virus drugs. Drug Discov. Ther. 4:77-84.
    • (2008) Drug Discov. Ther , vol.4 , pp. 77-84
    • Watanabe, K.1    Takizawa, N.2    Noda, S.3    Tsukahara, F.4    Maru, Y.5    Kobayashi, N.6
  • 26
    • 35548976680 scopus 로고    scopus 로고
    • Visualization of microtubule-mediated transport of influenza viral progeny ribonucleoprotein
    • Momose F, Kikuchi Y, Komase K, Morikawa Y. 2007. Visualization of microtubule-mediated transport of influenza viral progeny ribonucleoprotein. Microbes Infect. 9:1422-1433. http://dx.doi.org/10.1016/j.micinf.2007.07.007.
    • (2007) Microbes Infect , vol.9 , pp. 1422-1433
    • Momose, F.1    Kikuchi, Y.2    Komase, K.3    Morikawa, Y.4
  • 28
    • 60049093598 scopus 로고    scopus 로고
    • BlobFinder, a tool for fluorescence microscopy image cytometry
    • Allalou A, Wahlby C. 2009. BlobFinder, a tool for fluorescence microscopy image cytometry. Comput. Methods Programs Biomed. 94:58-65. http://dx.doi.org/10.1016/j.cmpb.2008.08.006.
    • (2009) Comput. Methods Programs Biomed , vol.94 , pp. 58-65
    • Allalou, A.1    Wahlby, C.2
  • 29
    • 0034875316 scopus 로고    scopus 로고
    • Trans-Golgi network sorting
    • Gu F, Crump CM, Thomas G. 2001. Trans-Golgi network sorting. Cell. Mol. Life Sci. 58:1067-1084. http://dx.doi.org/10.1007/PL00000922.
    • (2001) Cell. Mol. Life Sci , vol.58 , pp. 1067-1084
    • Gu, F.1    Crump, C.M.2    Thomas, G.3
  • 30
    • 0030755820 scopus 로고    scopus 로고
    • Apical sorting of influenza hemagglutinin by transcytosis in retinal pigment epithelium
    • Bonilha VL, Marmorstein AD, Cohen-Gould L, Rodriguez-Boulan E. 1997. Apical sorting of influenza hemagglutinin by transcytosis in retinal pigment epithelium. J. Cell Sci. 110:1717-1727.
    • (1997) J. Cell Sci , vol.110 , pp. 1717-1727
    • Bonilha, V.L.1    Marmorstein, A.D.2    Cohen-Gould, L.3    Rodriguez-Boulan, E.4
  • 31
    • 0025612221 scopus 로고
    • Transport of influenza HA from the trans-Golgi network to the apical surface of MDCK cells permeabilized in their basolateral plasma membranes: energy dependence and involvement of GTP-binding proteins
    • Gravotta D, Adesnik M, Sabatini DD. 1990. Transport of influenza HA from the trans-Golgi network to the apical surface of MDCK cells permeabilized in their basolateral plasma membranes: energy dependence and involvement of GTP-binding proteins. J. Cell Biol. 111:2893-2908. http://dx.doi.org/10.1083/jcb.111.6.2893.
    • (1990) J. Cell Biol , vol.111 , pp. 2893-2908
    • Gravotta, D.1    Adesnik, M.2    Sabatini, D.D.3
  • 32
    • 84858980804 scopus 로고    scopus 로고
    • Transport of influenza virus neuraminidase (NA) to host cell surface is regulated by ARHGAP21 and Cdc42 proteins
    • Wang S, Li H, Chen Y, Wei H, Gao GF, Liu H, Huang S, Chen JL. 2012. Transport of influenza virus neuraminidase (NA) to host cell surface is regulated by ARHGAP21 and Cdc42 proteins. J. Biol. Chem. 287:9804-9816. http://dx.doi.org/10.1074/jbc.M111.312959.
    • (2012) J. Biol. Chem , vol.287 , pp. 9804-9816
    • Wang, S.1    Li, H.2    Chen, Y.3    Wei, H.4    Gao, G.F.5    Liu, H.6    Huang, S.7    Chen, J.L.8
  • 33
    • 0032513021 scopus 로고    scopus 로고
    • Influenza virus M2 protein slows traffic along the secretory pathway. pH perturbation of acidified compartments affects early Golgi transport steps
    • Henkel JR, Weisz OA. 1998. Influenza virus M2 protein slows traffic along the secretory pathway. pH perturbation of acidified compartments affects early Golgi transport steps. J. Biol. Chem. 273:6518-6524. http://dx.doi.org/10.1074/jbc.273.11.6518.
    • (1998) J. Biol. Chem , vol.273 , pp. 6518-6524
    • Henkel, J.R.1    Weisz, O.A.2
  • 34
    • 0029861558 scopus 로고    scopus 로고
    • Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins
    • Bui M, Whittaker G, Helenius A. 1996. Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins. J. Virol. 70: 8391-8401.
    • (1996) J. Virol , vol.70 , pp. 8391-8401
    • Bui, M.1    Whittaker, G.2    Helenius, A.3
  • 35
    • 0034614944 scopus 로고    scopus 로고
    • InfluenzaM2proton channel activity selectively inhibits trans-Golgi network release of apical membrane and secreted proteins in polarized Madin-Darby canine kidney cells
    • Henkel JR, Gibson GA, Poland PA, Ellis MA, Hughey RP, Weisz OA. 2000. InfluenzaM2proton channel activity selectively inhibits trans-Golgi network release of apical membrane and secreted proteins in polarized Madin-Darby canine kidney cells. J. Cell Biol. 148:495-504. http://dx.doi.org/10.1083/jcb.148.3.495.
    • (2000) J. Cell Biol , vol.148 , pp. 495-504
    • Henkel, J.R.1    Gibson, G.A.2    Poland, P.A.3    Ellis, M.A.4    Hughey, R.P.5    Weisz, O.A.6
  • 36
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipidenriched membrane subdomains during transport to the apical cell surface
    • Brown DA, Rose JK. 1992. Sorting of GPI-anchored proteins to glycolipidenriched membrane subdomains during transport to the apical cell surface. Cell 68:533-544. http://dx.doi.org/10.1016/0092-8674(92)90189-J.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 37
    • 0022975133 scopus 로고
    • The trans Golgi network: sorting at the exit site of the Golgi complex
    • Griffiths G, Simons K. 1986. The trans Golgi network: sorting at the exit site of the Golgi complex. Science 234:438-443. http://dx.doi.org/10.1126/science.2945253.
    • (1986) Science , vol.234 , pp. 438-443
    • Griffiths, G.1    Simons, K.2
  • 38
    • 8444221583 scopus 로고    scopus 로고
    • Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane ofMDCK cells
    • Ang AL, Taguchi T, Francis S, Folsch H, Murrells LJ, Pypaert M, Warren G, Mellman I. 2004. Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane ofMDCK cells. J. Cell Biol. 167:531-543. http://dx.doi.org/10.1083/jcb.200408165.
    • (2004) J. Cell Biol , vol.167 , pp. 531-543
    • Ang, A.L.1    Taguchi, T.2    Francis, S.3    Folsch, H.4    Murrells, L.J.5    Pypaert, M.6    Warren, G.7    Mellman, I.8
  • 39
    • 12344260000 scopus 로고    scopus 로고
    • Polarized sorting in epithelial cells: raft clustering and the biogenesis of the apical membrane
    • Schuck S, Simons K. 2004. Polarized sorting in epithelial cells: raft clustering and the biogenesis of the apical membrane. J. Cell Sci. 117:5955-5964. http://dx.doi.org/10.1242/jcs.01596.
    • (2004) J. Cell Sci , vol.117 , pp. 5955-5964
    • Schuck, S.1    Simons, K.2
  • 40
    • 33645277808 scopus 로고    scopus 로고
    • GPI-anchored proteins are directly targeted to the apical surface in fully polarized MDCK cells
    • Paladino S, Pocard T, Catino MA, Zurzolo C. 2006. GPI-anchored proteins are directly targeted to the apical surface in fully polarized MDCK cells. J. Cell Biol. 172:1023-1034. http://dx.doi.org/10.1083/jcb.200507116.
    • (2006) J. Cell Biol , vol.172 , pp. 1023-1034
    • Paladino, S.1    Pocard, T.2    Catino, M.A.3    Zurzolo, C.4
  • 41
    • 2342585501 scopus 로고    scopus 로고
    • Role of transmembrane domain and cytoplasmic tail amino acid sequences of influenza a virus neuraminidase in raft association and virus budding
    • Barman S, Adhikary L, Chakrabarti AK, Bernas C, Kawaoka Y, Nayak DP. 2004. Role of transmembrane domain and cytoplasmic tail amino acid sequences of influenza a virus neuraminidase in raft association and virus budding. J. Virol. 78:5258-5269. http://dx.doi.org/10.1128/JVI.78.10.5258-5269.2004.
    • (2004) J. Virol , vol.78 , pp. 5258-5269
    • Barman, S.1    Adhikary, L.2    Chakrabarti, A.K.3    Bernas, C.4    Kawaoka, Y.5    Nayak, D.P.6
  • 42
    • 0030991137 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape
    • Jin H, Leser GP, Zhang J, Lamb RA. 1997. Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape. EMBO J. 16: 1236-1247. http://dx.doi.org/10.1093/emboj/16.6.1236.
    • (1997) EMBO J , vol.16 , pp. 1236-1247
    • Jin, H.1    Leser, G.P.2    Zhang, J.3    Lamb, R.A.4
  • 43
    • 0030726211 scopus 로고    scopus 로고
    • The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells
    • Yeaman C, Le Gall AH, Baldwin AN, Monlauzeur L, Le Bivic A, Rodriguez-Boulan E. 1997. The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells. J. Cell Biol. 139:929-940. http://dx.doi.org/10.1083/jcb.139.4.929.
    • (1997) J. Cell Biol , vol.139 , pp. 929-940
    • Yeaman, C.1    Le Gall, A.H.2    Baldwin, A.N.3    Monlauzeur, L.4    Le Bivic, A.5    Rodriguez-Boulan, E.6
  • 44
    • 0036733284 scopus 로고    scopus 로고
    • Caveolae: from cell biology to animal physiology
    • Razani B, Woodman SE, Lisanti MP. 2002. Caveolae: from cell biology to animal physiology. Pharmacol. Rev. 54:431-467. http://dx.doi.org/10.1124/pr.54.3.431.
    • (2002) Pharmacol. Rev , vol.54 , pp. 431-467
    • Razani, B.1    Woodman, S.E.2    Lisanti, M.P.3
  • 45
    • 77954761089 scopus 로고    scopus 로고
    • Hydrophobic mismatch-induced clustering as a primer for protein sorting in the secretory pathway
    • Schmidt U, Weiss M. 2010. Hydrophobic mismatch-induced clustering as a primer for protein sorting in the secretory pathway. Biophys. Chem. 151:34-38. http://dx.doi.org/10.1016/j.bpc.2010.04.009.
    • (2010) Biophys. Chem , vol.151 , pp. 34-38
    • Schmidt, U.1    Weiss, M.2
  • 46
    • 80053962808 scopus 로고    scopus 로고
    • Gag induces the coalescence of clustered lipid rafts and tetraspanin-enriched microdomains at HIV-1 assembly sites on the plasma membrane
    • Hogue IB, Grover JR, Soheilian F, Nagashima K, Ono A. 2011. Gag induces the coalescence of clustered lipid rafts and tetraspanin-enriched microdomains at HIV-1 assembly sites on the plasma membrane. J. Virol. 85:9749-9766. http://dx.doi.org/10.1128/JVI.00743-11.
    • (2011) J. Virol , vol.85 , pp. 9749-9766
    • Hogue, I.B.1    Grover, J.R.2    Soheilian, F.3    Nagashima, K.4    Ono, A.5
  • 47
    • 0035923728 scopus 로고    scopus 로고
    • Distinction between signaling mechanisms in lipid rafts vs. caveolae
    • Sowa G, Pypaert M, Sessa WC. 2001. Distinction between signaling mechanisms in lipid rafts vs. caveolae. Proc. Natl. Acad. Sci. U. S. A. 98: 14072-14077. http://dx.doi.org/10.1073/pnas.241409998.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 14072-14077
    • Sowa, G.1    Pypaert, M.2    Sessa, W.C.3
  • 48
    • 35648987939 scopus 로고    scopus 로고
    • Intracellular trafficking of raft/caveolae domains: insights from integrin signaling
    • Echarri A, Muriel O, Del Pozo MA. 2007. Intracellular trafficking of raft/caveolae domains: insights from integrin signaling. Semin. Cell Dev. Biol. 18:627-637. http://dx.doi.org/10.1016/j.semcdb.2007.08.004.
    • (2007) Semin. Cell Dev. Biol , vol.18 , pp. 627-637
    • Echarri, A.1    Muriel, O.2    Del Pozo, M.A.3
  • 49
    • 0345683542 scopus 로고    scopus 로고
    • The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells
    • Puertollano R, Martin-Belmonte F, Millan J, de Marco MC, Albar JP, Kremer L, Alonso MA. 1999. The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells. J. Cell Biol. 145:141-151. http://dx.doi.org/10.1083/jcb.145.1.141.
    • (1999) J. Cell Biol , vol.145 , pp. 141-151
    • Puertollano, R.1    Martin-Belmonte, F.2    Millan, J.3    de Marco, M.C.4    Albar, J.P.5    Kremer, L.6    Alonso, M.A.7
  • 50
    • 0346752326 scopus 로고    scopus 로고
    • Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL
    • Tall RD, Alonso MA, Roth MG. 2003. Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL. Traffic 4:838-849. http://dx.doi.org/10.1046/j.1398-9219.2003.0138.x.
    • (2003) Traffic , vol.4 , pp. 838-849
    • Tall, R.D.1    Alonso, M.A.2    Roth, M.G.3
  • 51
    • 34548070234 scopus 로고    scopus 로고
    • Differential involvement of endocytic compartments in the biosynthetic traffic of apical proteins
    • Cresawn KO, Potter BA, Oztan A, Guerriero CJ, Ihrke G, Goldenring JR, Apodaca G, Weisz OA. 2007. Differential involvement of endocytic compartments in the biosynthetic traffic of apical proteins. EMBO J. 26: 3737-3748. http://dx.doi.org/10.1038/sj.emboj.7601813.
    • (2007) EMBO J , vol.26 , pp. 3737-3748
    • Cresawn, K.O.1    Potter, B.A.2    Oztan, A.3    Guerriero, C.J.4    Ihrke, G.5    Goldenring, J.R.6    Apodaca, G.7    Weisz, O.A.8
  • 52
    • 0033593321 scopus 로고    scopus 로고
    • Influenza viruses select ordered lipid domains during budding from the plasma membrane
    • Scheiffele P, Rietveld A, Wilk T, Simons K. 1999. Influenza viruses select ordered lipid domains during budding from the plasma membrane. J. Biol. Chem. 274:2038-2044. http://dx.doi.org/10.1074/jbc.274.4.2038.
    • (1999) J. Biol. Chem , vol.274 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 53
    • 0030945486 scopus 로고    scopus 로고
    • Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast
    • Rayner JC, Pelham HR. 1997. Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast. EMBO J. 16: 1832-1841. http://dx.doi.org/10.1093/emboj/16.8.1832.
    • (1997) EMBO J , vol.16 , pp. 1832-1841
    • Rayner, J.C.1    Pelham, H.R.2
  • 54
    • 0033944545 scopus 로고    scopus 로고
    • Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae
    • Levine TP, Wiggins CA, Munro S. 2000. Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae. Mol. Biol. Cell 11:2267-2281. http://dx.doi.org/10.1091/mbc.11.7.2267.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2267-2281
    • Levine, T.P.1    Wiggins, C.A.2    Munro, S.3
  • 55
    • 23244449276 scopus 로고    scopus 로고
    • Transbilayer peptide sorting between raft and nonraft bilayers: comparisons of detergent extraction and confocal microscopy
    • Vidal A, McIntosh TJ. 2005. Transbilayer peptide sorting between raft and nonraft bilayers: comparisons of detergent extraction and confocal microscopy. Biophys. J. 89:1102-1108. http://dx.doi.org/10.1529/biophysj.105.062380.
    • (2005) Biophys. J , vol.89 , pp. 1102-1108
    • Vidal, A.1    McIntosh, T.J.2
  • 57
    • 84883556425 scopus 로고    scopus 로고
    • How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains
    • Fantini J, Barrantes FJ. 2013. How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains. Front. Physiol. 4:31. http://dx.doi.org/10.3389/fphys.2013.00031.
    • (2013) Front. Physiol , vol.4 , pp. 31
    • Fantini, J.1    Barrantes, F.J.2
  • 59
    • 0026531034 scopus 로고
    • Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity
    • Simpson DA, Lamb RA. 1992. Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity. J. Virol. 66:790-803.
    • (1992) J. Virol , vol.66 , pp. 790-803
    • Simpson, D.A.1    Lamb, R.A.2

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.