메뉴 건너뛰기




Volumn 81, Issue 5, 2007, Pages 2263-2273

The YLDL sequence within sendai virus M protein is critical for budding of virus-like particles and interacts with Alix/AIP1 independently of C protein

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CELL PROTEIN; GAG PROTEIN; MATRIX PROTEIN; PROTEIN ALIX AIP1; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS PROTEIN C;

EID: 33847190289     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02218-06     Document Type: Article
Times cited : (68)

References (52)
  • 1
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: An endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst, M., D. J. Katzmann, E. J. Estepa-Sabal, T. Meerloo, and S. D. Emr. 2002. Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev. Cell 3:271-282.
    • (2002) Dev. Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 2
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • Babst, M, D. J. Katzmann, W. B. Snyder, B. Wendland, and S. D. Emr. 2002. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev. Cell 3:283-289.
    • (2002) Dev. Cell , vol.3 , pp. 283-289
    • Babst, M.1    Katzmann, D.J.2    Snyder, W.B.3    Wendland, B.4    Emr, S.D.5
  • 3
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • Babst, M., T. K. Sato, L. M. Banta, and S. D. Emr. 1997. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 16:1820-1831.
    • (1997) EMBO J , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 4
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst, M., B. Wendland, E. J. Estepa, and S. D. Emr. 1998. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17:2982-2993.
    • (1998) EMBO J , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 5
    • 29144474443 scopus 로고    scopus 로고
    • Late budding domains and host proteins in enveloped virus release
    • Bieniasz, P. D. 2006. Late budding domains and host proteins in enveloped virus release. Virology 344:55-63.
    • (2006) Virology , vol.344 , pp. 55-63
    • Bieniasz, P.D.1
  • 6
    • 0033959713 scopus 로고    scopus 로고
    • ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking
    • Bishop, N., and P. Woodman. 2000. ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking. Mol. Biol. Cell 11:227-239.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 227-239
    • Bishop, N.1    Woodman, P.2
  • 7
    • 0035853688 scopus 로고    scopus 로고
    • TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes
    • Bishop, N., and P. Woodman. 2001. TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes. J. Biol. Chem. 276:11735-11742.
    • (2001) J. Biol. Chem , vol.276 , pp. 11735-11742
    • Bishop, N.1    Woodman, P.2
  • 8
    • 3042694692 scopus 로고    scopus 로고
    • Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding
    • Blot, V., F. Perugi, B. Gay, M. C. Prevost, L. Briant, F. Tangy, H. Abriel, O. Staub, M. C. Dokhelar, and C. Pique. 2004. Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding. J. Cell Sci. 117:2357-2367.
    • (2004) J. Cell Sci , vol.117 , pp. 2357-2367
    • Blot, V.1    Perugi, F.2    Gay, B.3    Prevost, M.C.4    Briant, L.5    Tangy, F.6    Abriel, H.7    Staub, O.8    Dokhelar, M.C.9    Pique, C.10
  • 9
    • 28844506638 scopus 로고    scopus 로고
    • Functions of early (AP-2) and late (AIP1/ALIX) endocytic proteins in equine infectious anemia virus budding
    • Chen, C., O. Vincent, J. Jin, O. A. Weisz, and R. C. Montelaro. 2005. Functions of early (AP-2) and late (AIP1/ALIX) endocytic proteins in equine infectious anemia virus budding. J. Biol. Chem. 280:40474-40480.
    • (2005) J. Biol. Chem , vol.280 , pp. 40474-40480
    • Chen, C.1    Vincent, O.2    Jin, J.3    Weisz, O.A.4    Montelaro, R.C.5
  • 10
  • 11
    • 9744221135 scopus 로고    scopus 로고
    • Retrovirus budding
    • Demirov, D. G., and E. O. Freed. 2004. Retrovirus budding. Virus Res. 106:87-102.
    • (2004) Virus Res , vol.106 , pp. 87-102
    • Demirov, D.G.1    Freed, E.O.2
  • 12
    • 0037154214 scopus 로고    scopus 로고
    • Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function
    • Demirov, D. G., A. Ono, J. M. Orenstein, and E. O. Freed. 2002. Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function. Proc. Natl. Acad. Sci. USA 99:955-960.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 955-960
    • Demirov, D.G.1    Ono, A.2    Orenstein, J.M.3    Freed, E.O.4
  • 13
    • 0036133283 scopus 로고    scopus 로고
    • The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner
    • Demirov, D. G., J. M. Orenstein, and E. O. Freed. 2002. The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner. J. Virol. 76:105-117.
    • (2002) J. Virol , vol.76 , pp. 105-117
    • Demirov, D.G.1    Orenstein, J.M.2    Freed, E.O.3
  • 15
    • 29144487064 scopus 로고    scopus 로고
    • Filovirus assembly and budding
    • Hartlieb, B., and W. Weissenhorn. 2006. Filovirus assembly and budding. Virology 344:64-70.
    • (2006) Virology , vol.344 , pp. 64-70
    • Hartlieb, B.1    Weissenhorn, W.2
  • 16
    • 0034610295 scopus 로고    scopus 로고
    • A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: Implications for filovirus budding
    • Harry, R. N., M. E. Brown, G. Wang, J. Huibregtse, and F. P. Hayes. 2000. A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: implications for filovirus budding. Proc. Natl. Acad. Sci. USA 97:13871-13876.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13871-13876
    • Harry, R.N.1    Brown, M.E.2    Wang, G.3    Huibregtse, J.4    Hayes, F.P.5
  • 17
    • 0033050750 scopus 로고    scopus 로고
    • A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: Implications for viral budding
    • Harty, R. N., J. Paragas, M. Sudol, and P. Palese. 1999. A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: implications for viral budding. J. Virol. 73:2921-2929.
    • (1999) J. Virol , vol.73 , pp. 2921-2929
    • Harty, R.N.1    Paragas, J.2    Sudol, M.3    Palese, P.4
  • 18
    • 0034926390 scopus 로고    scopus 로고
    • CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins
    • Howard, T. L., D. R. Stauffer, C. R. Degnin, and S. M. Hollenberg. 2001. CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins. J. Cell Sci. 114:2395-2404.
    • (2001) J. Cell Sci , vol.114 , pp. 2395-2404
    • Howard, T.L.1    Stauffer, D.R.2    Degnin, C.R.3    Hollenberg, S.M.4
  • 19
    • 18844392879 scopus 로고    scopus 로고
    • Functional characterization of Ebola virus L-domains using VSV recombinants
    • Irie, T., J. M. Licata, and R. N. Harty. 2005. Functional characterization of Ebola virus L-domains using VSV recombinants. Virology 336:291-298.
    • (2005) Virology , vol.336 , pp. 291-298
    • Irie, T.1    Licata, J.M.2    Harty, R.N.3
  • 20
    • 3142751325 scopus 로고    scopus 로고
    • Functional analysis of late-budding domain activity associated with the PSAP motif within the vesicular stomatitis virus M protein
    • Irie, T., J. M. Licata, H. R. Jayakar, M. A. Whitt, P. Bell, and R. N. Harty. 2004. Functional analysis of late-budding domain activity associated with the PSAP motif within the vesicular stomatitis virus M protein. J. Virol. 78:7823-7827.
    • (2004) J. Virol , vol.78 , pp. 7823-7827
    • Irie, T.1    Licata, J.M.2    Jayakar, H.R.3    Whitt, M.A.4    Bell, P.5    Harty, R.N.6
  • 21
    • 1542377646 scopus 로고    scopus 로고
    • Budding of PPxY-containing rhabdoviruses is not dependent on host proteins TGS101 and VPS4A
    • Irie, T., J. M. Licata, J. P. McGettigan, M. J. Schnell, and R. N. Harty. 2004. Budding of PPxY-containing rhabdoviruses is not dependent on host proteins TGS101 and VPS4A. J. Virol. 78:2657-2665.
    • (2004) J. Virol , vol.78 , pp. 2657-2665
    • Irie, T.1    Licata, J.M.2    McGettigan, J.P.3    Schnell, M.J.4    Harty, R.N.5
  • 22
    • 9644303143 scopus 로고    scopus 로고
    • Filovirus budding
    • Jasenosky, L. D., and Y. Kawaoka. 2004. Filovirus budding. Virus Res. 106:181-188.
    • (2004) Virus Res , vol.106 , pp. 181-188
    • Jasenosky, L.D.1    Kawaoka, Y.2
  • 23
    • 0035031534 scopus 로고    scopus 로고
    • Ebola virus VP40-induced particle formation and association with the lipid bilayer
    • Jasenosky, L. D., G. Neumann, I. Lukasherich, and Y. Kawaoka. 2001. Ebola virus VP40-induced particle formation and association with the lipid bilayer. J. Virol. 75:5205-5214.
    • (2001) J. Virol , vol.75 , pp. 5205-5214
    • Jasenosky, L.D.1    Neumann, G.2    Lukasherich, I.3    Kawaoka, Y.4
  • 24
    • 9744271721 scopus 로고    scopus 로고
    • Rhabdovirus assembly and budding
    • Jayakar, H. R., E. Jeetendra, and M. A. Whitt. 2004. Rhabdovirus assembly and budding. Virus Res. 106:117-132.
    • (2004) Virus Res , vol.106 , pp. 117-132
    • Jayakar, H.R.1    Jeetendra, E.2    Whitt, M.A.3
  • 25
    • 0028987484 scopus 로고
    • Membrane vesiculation function and exocytosis of wild-type and mutant matrix proteins of vesicular stomatitis virus
    • Justice, P. A., W. Sun, Y. Li, Z. Ye, P. R. Grigera, and R. R. Wagner. 1995. Membrane vesiculation function and exocytosis of wild-type and mutant matrix proteins of vesicular stomatitis virus. J. Virol. 69:3156-3160.
    • (1995) J. Virol , vol.69 , pp. 3156-3160
    • Justice, P.A.1    Sun, W.2    Li, Y.3    Ye, Z.4    Grigera, P.R.5    Wagner, R.R.6
  • 26
    • 0141643096 scopus 로고    scopus 로고
    • The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting
    • Katoh, K., H. Shibata, H. Suzuki, A. Nara, K. Ishidoh, E. Kominami, T. Yoshimori, and M. Maki. 2003. The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting. J. Biol. Chem. 278:39104-39113.
    • (2003) J. Biol. Chem , vol.278 , pp. 39104-39113
    • Katoh, K.1    Shibata, H.2    Suzuki, H.3    Nara, A.4    Ishidoh, K.5    Kominami, E.6    Yoshimori, T.7    Maki, M.8
  • 27
    • 0036148338 scopus 로고    scopus 로고
    • Functional replacement and positional dependence of homologous and heterologous L domains in equine infectious anemia virus replication
    • Li, F., C. Chen, B. A. Puffer, and R. C. Montelaro. 2002. Functional replacement and positional dependence of homologous and heterologous L domains in equine infectious anemia virus replication. J. Virol. 76:1569-1577.
    • (2002) J. Virol , vol.76 , pp. 1569-1577
    • Li, F.1    Chen, C.2    Puffer, B.A.3    Montelaro, R.C.4
  • 28
    • 0027299296 scopus 로고
    • Viral liposomes released from insect cells infected with recombinant baculovirus expressing the matrix protein of vesicular stomatitis virus
    • Li, Y., L. Luo, M. Schubert, R. R. Wagner, and C. Y. Kang. 1993. Viral liposomes released from insect cells infected with recombinant baculovirus expressing the matrix protein of vesicular stomatitis virus. J. Virol. 67:4415-4420.
    • (1993) J. Virol , vol.67 , pp. 4415-4420
    • Li, Y.1    Luo, L.2    Schubert, M.3    Wagner, R.R.4    Kang, C.Y.5
  • 29
    • 3142710288 scopus 로고    scopus 로고
    • Contribution of Ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 virus-like particles
    • Licata, J. M., R. F. Johnson, Z. Han, and R. N. Harty. 2004. Contribution of Ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 virus-like particles. J. Virol. 78:7344-7351.
    • (2004) J. Virol , vol.78 , pp. 7344-7351
    • Licata, J.M.1    Johnson, R.F.2    Han, Z.3    Harty, R.N.4
  • 30
    • 2442670346 scopus 로고    scopus 로고
    • Context-dependent effects of L domains and ubiquitination on viral budding
    • Martin-Serrano, J., D. Perez-Caballero, and P. D. Bieniasz. 2004. Context-dependent effects of L domains and ubiquitination on viral budding. J. Virol. 78:5554-5563.
    • (2004) J. Virol , vol.78 , pp. 5554-5563
    • Martin-Serrano, J.1    Perez-Caballero, D.2    Bieniasz, P.D.3
  • 31
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano, J., T. Zang, and P. D. Bieniasz. 2001. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat. Med. 7:1313-1319.
    • (2001) Nat. Med , vol.7 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 32
    • 0037383128 scopus 로고    scopus 로고
    • Role of ESCRT-I in retroviral budding
    • Martin-Serrano, J., T. Zang, and P. D. Bieniasz. 2003. Role of ESCRT-I in retroviral budding. J. Virol. 77:4794-4804.
    • (2003) J. Virol , vol.77 , pp. 4794-4804
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 34
    • 0036235725 scopus 로고    scopus 로고
    • Ebola virus VP40 drives the formation of virus-like filamentous particles along with GP
    • Noda, T., H. Sagara, E. Suzuki, A. Takada, H. Kida, and Y. Kawaoka. 2002. Ebola virus VP40 drives the formation of virus-like filamentous particles along with GP. J. Virol. 76:4855-865.
    • (2002) J. Virol , vol.76 , pp. 4855-4865
    • Noda, T.1    Sagara, H.2    Suzuki, E.3    Takada, A.4    Kida, H.5    Kawaoka, Y.6
  • 36
    • 18144371606 scopus 로고    scopus 로고
    • Identification of domains in gag important for prototypic foamy virus egress
    • Patton, G. S., S. A. Morris, W. Chung, P. D. Bieniasz, and M. O. McClure. 2005. Identification of domains in gag important for prototypic foamy virus egress. J. Virol. 79:6392-6399.
    • (2005) J. Virol , vol.79 , pp. 6392-6399
    • Patton, G.S.1    Morris, S.A.2    Chung, W.3    Bieniasz, P.D.4    McClure, M.O.5
  • 37
    • 0033965544 scopus 로고    scopus 로고
    • The membrane-proximal stem region of vesicular stomatitis virus G protein confers efficient virus assembly
    • Robison, C. S., and M. A. Whitt. 2000. The membrane-proximal stem region of vesicular stomatitis virus G protein confers efficient virus assembly. J. Virol. 74:2239-2246.
    • (2000) J. Virol , vol.74 , pp. 2239-2246
    • Robison, C.S.1    Whitt, M.A.2
  • 39
    • 0033543982 scopus 로고    scopus 로고
    • Double-layered membrane vesicles released from mammalian cells infected with Sendai virus expressing the matrix protein of vesicular stomatitis virus
    • Sakaguchi, T., T. Uchiyama, Y. Fujii, K. Kiyotani, A. Kato, Y. Nagai, A. Kawai, and T. Yoshida. 1999. Double-layered membrane vesicles released from mammalian cells infected with Sendai virus expressing the matrix protein of vesicular stomatitis virus. Virology 263:230-243.
    • (1999) Virology , vol.263 , pp. 230-243
    • Sakaguchi, T.1    Uchiyama, T.2    Fujii, Y.3    Kiyotani, K.4    Kato, A.5    Nagai, Y.6    Kawai, A.7    Yoshida, T.8
  • 40
    • 0031720833 scopus 로고    scopus 로고
    • Molecular events in the assembly of retrovirus particles
    • Sakalian, M., and E. Hunter. 1998. Molecular events in the assembly of retrovirus particles. Adv. Exp. Med. Biol. 440:329-339.
    • (1998) Adv. Exp. Med. Biol , vol.440 , pp. 329-339
    • Sakalian, M.1    Hunter, E.2
  • 41
    • 13944252828 scopus 로고    scopus 로고
    • Evidence for a new viral late-domain core sequence, FPIV, necessary for budding of a paramyxovirus
    • Schmitt, A. P., G. P. Leser, E. Morita, W. I. Sundquist, and R. A. Lamb. 2005. Evidence for a new viral late-domain core sequence, FPIV, necessary for budding of a paramyxovirus. J. Virol. 79:2988-2997.
    • (2005) J. Virol , vol.79 , pp. 2988-2997
    • Schmitt, A.P.1    Leser, G.P.2    Morita, E.3    Sundquist, W.I.4    Lamb, R.A.5
  • 42
    • 0036194519 scopus 로고    scopus 로고
    • Requirements for budding of paramyxovirus simian virus 5 virus-like particles
    • Schmitt, A. P., G. P. Leser, D. L. Waning, and R. A. Lamb. 2002. Requirements for budding of paramyxovirus simian virus 5 virus-like particles. J. Virol. 76:3952-3964.
    • (2002) J. Virol , vol.76 , pp. 3952-3964
    • Schmitt, A.P.1    Leser, G.P.2    Waning, D.L.3    Lamb, R.A.4
  • 43
    • 0032473424 scopus 로고    scopus 로고
    • Requirement for a non-specific glycoprotein cytoplasmic domain sequence to drive efficient budding of vesicular stomatitis virus
    • Schnell, M. J., L. Buonocore, E. Boritz, H. P. Ghosh, R. Chernish, and J. K. Rose. 1998. Requirement for a non-specific glycoprotein cytoplasmic domain sequence to drive efficient budding of vesicular stomatitis virus. EMBO J. 17:1289-1296.
    • (1998) EMBO J , vol.17 , pp. 1289-1296
    • Schnell, M.J.1    Buonocore, L.2    Boritz, E.3    Ghosh, H.P.4    Chernish, R.5    Rose, J.K.6
  • 44
  • 45
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack, B., A. Calistri, S. Craig, E. Popova, and H. G. Gottlinger. 2003. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114:689-699.
    • (2003) Cell , vol.114 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 47
    • 0035163813 scopus 로고    scopus 로고
    • Role of matrix and fusion proteins in budding of Sendai virus
    • Takimoto, T., K. G. Murti, T. Bousse, R. A. Scroggs, and A. Portner. 2001. Role of matrix and fusion proteins in budding of Sendai virus. J. Virol. 75:11384-11391.
    • (2001) J. Virol , vol.75 , pp. 11384-11391
    • Takimoto, T.1    Murti, K.G.2    Bousse, T.3    Scroggs, R.A.4    Portner, A.5
  • 48
    • 0035877018 scopus 로고    scopus 로고
    • Proteomic analysis of dendritic cell-derived exosomes: A secreted subcellular compartment distinct from apoptotic vesicles
    • Théry, C., M. Boussac, P. Veron, P. Ricciardi-Castagnoli, G. Raposo, J. Garin, and S. Amigorena. 2001. Proteomic analysis of dendritic cell-derived exosomes: a secreted subcellular compartment distinct from apoptotic vesicles. J. Immunol. 166:7309-7318.
    • (2001) J. Immunol , vol.166 , pp. 7309-7318
    • Théry, C.1    Boussac, M.2    Veron, P.3    Ricciardi-Castagnoli, P.4    Raposo, G.5    Garin, J.6    Amigorena, S.7
  • 52
    • 0033854158 scopus 로고    scopus 로고
    • Infectivity of Moloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses
    • Yuan, B., S. Campbell, E. Bacharach, A. Rein, and S. P. Goff. 2000. Infectivity of Moloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses. J. Virol. 74:7250-7260.
    • (2000) J. Virol , vol.74 , pp. 7250-7260
    • Yuan, B.1    Campbell, S.2    Bacharach, E.3    Rein, A.4    Goff, S.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.