메뉴 건너뛰기




Volumn 5, Issue 3, 2004, Pages 194-210

Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae

Author keywords

Class E; Endosome; ESCRT complexes; Multivesicular body; Protein sorting; Vacuole; VPS

Indexed keywords

CARRIER PROTEIN; FUNGAL PROTEIN; HYBRID PROTEIN; ISOPROTEIN; PROTEIN BRO1P; PROTEIN RIM20P; UNCLASSIFIED DRUG;

EID: 1642373357     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2004.00169.x     Document Type: Article
Times cited : (169)

References (82)
  • 1
    • 0031911736 scopus 로고    scopus 로고
    • Vacuole biogenesis in Saccharomyces cerevisiae: Protein transport pathways to the yeast vacuole
    • Bryant NJ, Stevens TH. Vacuole biogenesis in Saccharomyces cerevisiae: Protein transport pathways to the yeast vacuole. Microbiol Mol Biol Rev, 1998;62:230-247.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 230-247
    • Bryant, N.J.1    Stevens, T.H.2
  • 2
    • 0032516807 scopus 로고    scopus 로고
    • Multiple sorting pathways between the late Golgi and the vacuole in yeast
    • Conibear E, Stevens TH. Multiple sorting pathways between the late Golgi and the vacuole in yeast. Biochim Biophys Acta 1998;1404:211-230.
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 211-230
    • Conibear, E.1    Stevens, T.H.2
  • 3
    • 0036320668 scopus 로고    scopus 로고
    • Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevistae
    • Bonangelino CJ, Chavez EM, Bonifacino JS. Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevistae. Mol Biol Cell 2002;13:2486-2501.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2486-2501
    • Bonangelino, C.J.1    Chavez, E.M.2    Bonifacino, J.S.3
  • 4
    • 0027083496 scopus 로고
    • Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class E vps mutants
    • Raymond CK, Howald-Stevenson I, Vater CA, Stevens TH. Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class E vps mutants. Mol Biol Cell 1992;3:1389-1402.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1389-1402
    • Raymond, C.K.1    Howald-Stevenson, I.2    Vater, C.A.3    Stevens, T.H.4
  • 5
    • 0024095176 scopus 로고
    • Organelle assembly in yeast: Characterization of yeast mutants defective in vacuolar biogenesis and protein sorting
    • Banta LM, Robinson JS, Klionsky DJ, Emr SD. Organelle assembly in yeast: Characterization of yeast mutants defective in vacuolar biogenesis and protein sorting. J Cell Biol 1988;107:1369-1383.
    • (1988) J. Cell Biol. , vol.107 , pp. 1369-1383
    • Banta, L.M.1    Robinson, J.S.2    Klionsky, D.J.3    Emr, S.D.4
  • 6
    • 0034846497 scopus 로고    scopus 로고
    • Late endosomes: Sorting and partitioning in multivesicular bodies
    • Piper RC, Luzio JP. Late endosomes: Sorting and partitioning in multivesicular bodies. Traffic 2001;2:612-621.
    • (2001) Traffic , vol.2 , pp. 612-621
    • Piper, R.C.1    Luzio, J.P.2
  • 9
    • 0034852403 scopus 로고    scopus 로고
    • Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole
    • Urbanowski JL, Piper RC. Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole. Traffic 2001;2:622-630.
    • (2001) Traffic , vol.2 , pp. 622-630
    • Urbanowski, J.L.1    Piper, R.C.2
  • 10
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann DJ, Babst M, Emr SD. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 2001;106:145-155.
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 11
    • 0035903635 scopus 로고    scopus 로고
    • Sorting of proteins into multivesicular bodies: Ubiquitin-dependent and -independent targeting
    • Reggiori F, Pelham HR. Sorting of proteins into multivesicular bodies: Ubiquitin-dependent and -independent targeting. EMBO J 2001;20: 5176-5186.
    • (2001) EMBO J. , vol.20 , pp. 5176-5186
    • Reggiori, F.1    Pelham, H.R.2
  • 12
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke L, Riezman H. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 1996;84:277-287.
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 13
    • 0742288063 scopus 로고    scopus 로고
    • Multivesicular body sorting ubiquitin ligase Rsp5 is required for the modification and sorting of carboxylpeptidase S
    • Katzmann DJ, Sarkar S, Chu T, Audhya A, Emr SD. Multivesicular body sorting. ubiquitin ligase Rsp5 is required for the modification and sorting of carboxylpeptidase S. Mol Biol Cell 2004;15:468-480.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 468-480
    • Katzmann, D.J.1    Sarkar, S.2    Chu, T.3    Audhya, A.4    Emr, S.D.5
  • 14
    • 0034157875 scopus 로고    scopus 로고
    • Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking
    • Babst M, Odorizzi G, Estepa EJ, Emr SD. Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking. Traffic 2000;1:248-258.
    • (2000) Traffic , vol.1 , pp. 248-258
    • Babst, M.1    Odorizzi, G.2    Estepa, E.J.3    Emr, S.D.4
  • 15
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • Babst M, Katzmann DJ, Snyder WB, Wendland B, Emr SD. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev Cell 2002;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
  • 16
    • 0036696804 scopus 로고    scopus 로고
    • ESCRT-III: An endosome-associated heterooligomeric protein complex required for MVB sorting
    • Babst M, Katzmann DJ, Estepa-Sabal EJ, Meerloo T, Emr SD. ESCRT-III: An endosome-associated heterooligomeric protein complex required for MVB sorting. Dev Cell 2002;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
  • 17
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • Shih SC, Katzmann DJ, Schnell JD, Sutanto M, Emr SD, Hicke L. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat Cell Biol 2002;4:389-393.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 389-393
    • Shih, S.C.1    Katzmann, D.J.2    Schnell, J.D.3    Sutanto, M.4    Emr, S.D.5    Hicke, L.6
  • 19
    • 0042991262 scopus 로고    scopus 로고
    • Vps27 recruits ESCRT machinery to endosomes during MVB sorting
    • Katzmann DJ, Stefan CJ, Babst M, Emr SD. Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J Cell Biol 2003;162: 413-423.
    • (2003) J. Cell Biol. , vol.162 , pp. 413-423
    • Katzmann, D.J.1    Stefan, C.J.2    Babst, M.3    Emr, S.D.4
  • 20
    • 0242266922 scopus 로고    scopus 로고
    • Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome
    • Bilodeau PS, Winistorfer SC, Kearney WR, Robertson AD, Piper RC. Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome. J Cell Biol 2003;163: 237-243.
    • (2003) J. Cell Biol. , vol.163 , pp. 237-243
    • Bilodeau, P.S.1    Winistorfer, S.C.2    Kearney, W.R.3    Robertson, A.D.4    Piper, R.C.5
  • 22
    • 0033638350 scopus 로고    scopus 로고
    • The sodium/proton exchanger Nhx1p is required for endosomal protein trafficking in the yeast Saccharomyces cerevisiae
    • Bowers K, Levi BP, Patel FI, Stevens TH. The sodium/proton exchanger Nhx1p is required for endosomal protein trafficking in the yeast Saccharomyces cerevisiae. Mol Biol Cell 2000;11: 4277-4294.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4277-4294
    • Bowers, K.1    Levi, B.P.2    Patel, F.I.3    Stevens, T.H.4
  • 23
    • 0347379848 scopus 로고    scopus 로고
    • Permease recycling and ubiquitination status reveal a particular role for Bro1 in the multivesicular body pathway
    • Nikko E, Marini AM, Andre B. Permease recycling and ubiquitination status reveal a particular role for Bro1 in the multivesicular body pathway. J Biol Chem 2003;278:50732-50743.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50732-50743
    • Nikko, E.1    Marini, A.M.2    Andre, B.3
  • 24
    • 0038784064 scopus 로고    scopus 로고
    • Bro1 is an endosome-associated protein that functions in the MVB pathway in Saccharomyces cerevisiae
    • Odorizzi G, Katzmann DJ, Babst M, Audhya A, Emr SD. Bro1 is an endosome-associated protein that functions in the MVB pathway in Saccharomyces cerevisiae. J Cell Sci 2003;116:1893-1903.
    • (2003) J. Cell Sci. , vol.116 , pp. 1893-1903
    • Odorizzi, G.1    Katzmann, D.J.2    Babst, M.3    Audhya, A.4    Emr, S.D.5
  • 25
    • 0037165612 scopus 로고    scopus 로고
    • Yeast Npi3/Bro1 is involved in ubiquitin-dependent control of permease trafficking
    • Springael JY, Nikko E, Andre B, Marini AM. Yeast Npi3/Bro1 is involved in ubiquitin-dependent control of permease trafficking. FEBS Lett 2002;517:103-109.
    • (2002) FEBS Lett. , vol.517 , pp. 103-109
    • Springael, J.Y.1    Nikko, E.2    Andre, B.3    Marini, A.M.4
  • 27
    • 0035172587 scopus 로고    scopus 로고
    • A family of small coiled-coil-forming proteins functioning at the late endosome in yeast
    • Kranz A, Kinner A, Kolling R. A family of small coiled-coil-forming proteins functioning at the late endosome in yeast. Mol Biol Cell 2001;12:711-723.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 711-723
    • Kranz, A.1    Kinner, A.2    Kolling, R.3
  • 28
    • 0034926390 scopus 로고    scopus 로고
    • CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins
    • Howard TL, Stauffer DR, Degnin CR, Hollenberg SM. CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins. J Cell Sci 2001;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
  • 29
    • 0034916615 scopus 로고    scopus 로고
    • CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression
    • Stauffer DR, Howard TL, Nyun T, Hollenberg SM. CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression. J Cell Sci 2001;114:2383-2393.
    • (2001) J. Cell Sci. , vol.114 , pp. 2383-2393
    • Stauffer, D.R.1    Howard, T.L.2    Nyun, T.3    Hollenberg, S.M.4
  • 30
    • 0033214780 scopus 로고    scopus 로고
    • Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins
    • Hittelman AB, Burakov D, Iniguez-Lluhi JA, Freedman LP, Garabedian MJ. Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins. EMBO J 1999;18:5380-5388.
    • (1999) EMBO J. , vol.18 , pp. 5380-5388
    • Hittelman, A.B.1    Burakov, D.2    Iniguez-Lluhi, J.A.3    Freedman, L.P.4    Garabedian, M.J.5
  • 32
    • 0033618430 scopus 로고    scopus 로고
    • Cloning and characterization of the EAP30 subunit of the ELL complex that confers derepression of transcription by RNA polymerase II
    • Schmidt AE, Miller T, Schmidt SL, Shiekhattar R, Shilatifard A. Cloning and characterization of the EAP30 subunit of the ELL complex that confers derepression of transcription by RNA polymerase II. J Biol Chem 1999;274:21981-21985.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21981-21985
    • Schmidt, A.E.1    Miller, T.2    Schmidt, S.L.3    Shiekhattar, R.4    Shilatifard, A.5
  • 33
    • 0033043513 scopus 로고    scopus 로고
    • Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein
    • Missotten M, Nichols A, Rieger K, Sadoul R. Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein. Cell Death Differ 1999;6:124-129.
    • (1999) Cell Death Differ. , vol.6 , pp. 124-129
    • Missotten, M.1    Nichols, A.2    Rieger, K.3    Sadoul, R.4
  • 36
    • 0142123069 scopus 로고    scopus 로고
    • Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins
    • Martin-Serrano J, Yaravoy A, Perez-Caballero D, Bieniasz PD. Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. Proc Natl Acad Sci U S A 2003;100:12414-12419.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 12414-12419
    • Martin-Serrano, J.1    Yaravoy, A.2    Perez-Caballero, D.3    Bieniasz, P.D.4
  • 37
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack B, Calistri A, Craig S, Popova E, Gottlinger HG. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 2003;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
  • 38
    • 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, Shibata H, Suzuki H, Nara A, Ishidoh K, Kominami E, Yoshimori T, Maki M. 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 2003;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
  • 39
    • 0024445121 scopus 로고
    • Characterization of genes required for protein sorting and vacuolar function in the yeast Saccharomyces cerevisiae
    • Rothman JH, Howald I, Stevens TH. Characterization of genes required for protein sorting and vacuolar function in the yeast Saccharomyces cerevisiae. EMBO J 1989;8:2057-2065.
    • (1989) EMBO J. , vol.8 , pp. 2057-2065
    • Rothman, J.H.1    Howald, I.2    Stevens, T.H.3
  • 40
    • 0022898326 scopus 로고
    • Protein sorting in yeast: Mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway
    • Rothman JH, Stevens TH. Protein sorting in yeast: Mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway. Cell 1986;47:1041-1051.
    • (1986) Cell , vol.47 , pp. 1041-1051
    • Rothman, J.H.1    Stevens, T.H.2
  • 41
    • 0031916243 scopus 로고    scopus 로고
    • + homeostasis in the yeast Saccharomyces cerevisiae
    • + homeostasis in the yeast Saccharomyces cerevisiae. Genetics 1998;148:1787-1798.
    • (1998) Genetics , vol.148 , pp. 1787-1798
    • Paidhungat, M.1    Garrett, S.2
  • 42
    • 0035858866 scopus 로고    scopus 로고
    • Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease
    • Helliwell SB, Losko S, Kaiser CA. Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease. J Cell Biol 2001;153:649-662.
    • (2001) J. Cell Biol. , vol.153 , pp. 649-662
    • Helliwell, S.B.1    Losko, S.2    Kaiser, C.A.3
  • 43
    • 0033786796 scopus 로고    scopus 로고
    • The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways
    • Amerik AY, Nowak J, Swaminathan S, Hochstrasser M. The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways. Mol Biol Cell 2000;11:3365-3380.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3365-3380
    • Amerik, A.Y.1    Nowak, J.2    Swaminathan, S.3    Hochstrasser, M.4
  • 44
    • 0034955239 scopus 로고    scopus 로고
    • Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins crucial role of Doa4p ubiquitin isopeptidase
    • Dupre S, Haguenauer-Tsapis R. Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins. crucial role of Doa4p ubiquitin isopeptidase. Mol Cell Biol 2001;21:4482-4494.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 4482-4494
    • Dupre, S.1    Haguenauer-Tsapis, R.2
  • 45
    • 0035173239 scopus 로고    scopus 로고
    • Uptake of the ATP-binding cassette (ABC) transporter Ste6 into the yeast vacuole is blocked in the doa4 mutant
    • Losko S, Kopp F, Kranz A, Kolling R. Uptake of the ATP-binding cassette (ABC) transporter Ste6 into the yeast vacuole is blocked in the doa4 mutant. Mol Biol Cell 2001;12:1047-1059.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1047-1059
    • Losko, S.1    Kopp, F.2    Kranz, A.3    Kolling, R.4
  • 46
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James P, Halladay J, Craig EA. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 1996;144:1425-1436.
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 50
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst M, Wendland B, Estepa EJ, Emr SD. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J 1998;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
  • 51
    • 0028332917 scopus 로고
    • The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene
    • Marcusson EG, Horazdovsky BF, Cereghino JL, Gharakhanian E, Emr SD. The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene. Cell 1994;77:579-586.
    • (1994) Cell , vol.77 , pp. 579-586
    • Marcusson, E.G.1    Horazdovsky, B.F.2    Cereghino, J.L.3    Gharakhanian, E.4    Emr, S.D.5
  • 53
    • 0041488656 scopus 로고    scopus 로고
    • Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
    • Bache KG, Brech A, Mehlum A, Stenmark H. Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes. J Cell Biol 2003;162:435-442.
    • (2003) J. Cell Biol. , vol.162 , pp. 435-442
    • Bache, K.G.1    Brech, A.2    Mehlum, A.3    Stenmark, H.4
  • 54
    • 0033048856 scopus 로고    scopus 로고
    • +-induced down-regulation of the Saccharomyces cerevisiae Gap1p permease involves its ubiquitination with lysine-63-linked chains
    • +-induced down-regulation of the Saccharomyces cerevisiae Gap1p permease involves its ubiquitination with lysine-63-linked chains. J Cell Sci 1999;112:1375-1383.
    • (1999) J. Cell Sci. , vol.112 , pp. 1375-1383
    • Springael, J.Y.1    Galan, J.M.2    Haguenauer-Tsapis, R.3    Andre, B.4
  • 55
    • 0028971506 scopus 로고
    • NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein C, Springael JY, Volland C, Haguenauer-Tsapis R, Andre B. NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase, Mol Microbiol 1995;18:77-87.
    • (1995) Mol. Microbiol. , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    Andre, B.5
  • 56
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan JM, Moreau V, Andre B, Volland C, Haguenauer-Tsapis R. Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J Biol Chem 1996;271:10946-10952.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    Andre, B.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 58
    • 0035658016 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus: The getaway driver nabbed
    • Luban J. HIV-1 and Ebola virus: The getaway driver nabbed. Nat Mad 2001;7:1278-1280.
    • (2001) Nat. Mad. , vol.7 , pp. 1278-1280
    • Luban, J.1
  • 59
    • 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, Zang T, Bieniasz PD. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat Med 2001;7:1313-1319.
    • (2001) Nat. Med. , vol.7 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 63
    • 0036544559 scopus 로고    scopus 로고
    • Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates
    • Bishop N, Horman A, Woodman P. Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates. J Cell Biol 2002;157:91-101.
    • (2002) J. Cell Biol. , vol.157 , pp. 91-101
    • Bishop, N.1    Horman, A.2    Woodman, P.3
  • 65
    • 0032510559 scopus 로고    scopus 로고
    • A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
    • Kobayashi T, Stang E, Fang KS, de Moerloose P, Parton RG, Gruenberg J. A lipid associated with the antiphospholipid syndrome regulates endosome structure and function. Nature 1998;392:193-197.
    • (1998) Nature , vol.392 , pp. 193-197
    • Kobayashi, T.1    Stang, E.2    Fang, K.S.3    de Moerloose, P.4    Parton, R.G.5    Gruenberg, J.6
  • 67
    • 0032487577 scopus 로고    scopus 로고
    • Fab1p is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis
    • Gary JD, Wurmser AE, Bonangelino CJ, Weisman LS, Emr SD. Fab1p is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis. J Cell Biol 1998;143: 65-79.
    • (1998) J. Cell Biol. , vol.143 , pp. 65-79
    • Gary, J.D.1    Wurmser, A.E.2    Bonangelino, C.J.3    Weisman, L.S.4    Emr, S.D.5
  • 68
    • 0032217266 scopus 로고    scopus 로고
    • Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body
    • Odorizzi G, Babst M, Emr SD. Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body. Cell 1998; 95:847-858.
    • (1998) Cell , vol.95 , pp. 847-858
    • Odorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 69
    • 0038758990 scopus 로고    scopus 로고
    • PtdIns(3,5),P2 is required for delivery of endocytic cargo into the multivesicular body
    • Shaw JD, Hama H, Sohrabi F, DeWald DB, Wendland B. PtdIns(3,5),P2 is required for delivery of endocytic cargo into the multivesicular body. Traffic 2003:4:479-490.
    • (2003) Traffic , vol.4 , pp. 479-490
    • Shaw, J.D.1    Hama, H.2    Sohrabi, F.3    DeWald, D.B.4    Wendland, B.5
  • 70
    • 0037018842 scopus 로고    scopus 로고
    • Vac14 controls PtdIns(3,5)P(2) synthesis and Fab1-dependent protein trafficking to the multivesicular body
    • Dove SK, McEwen RK, Mayes A, Hughes DC, Beggs JD, Michell RH. Vac14 controls PtdIns(3,5)P(2) synthesis and Fab1-dependent protein trafficking to the multivesicular body. Curr Biol 2002: 12:885-893.
    • (2002) Curr. Biol. , vol.12 , pp. 885-893
    • Dove, S.K.1    McEwen, R.K.2    Mayes, A.3    Hughes, D.C.4    Beggs, J.D.5    Michell, R.H.6
  • 71
    • 0141532093 scopus 로고    scopus 로고
    • Identification of mammalian Vps24p as an effector of phosphatidylinositol 3,5-bisphosphate-dependent endosome compartmentalization
    • Whitley P, Reaves BJ, Hashimoto M, Riley AM, Potter BV, Holman GD. Identification of mammalian Vps24p as an effector of phosphatidylinositol 3,5-bisphosphate-dependent endosome compartmentalization. J Biol Chem 2003;278:38786-38795.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38786-38795
    • Whitley, P.1    Reaves, B.J.2    Hashimoto, M.3    Riley, A.M.4    Potter, B.V.5    Holman, G.D.6
  • 73
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski RS, Hieter P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 1989;122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 75
    • 0016836498 scopus 로고
    • Proteinase C (carboxypeptidase Y) mutant of yeast
    • Wolf DH, Fink GR. Proteinase C (carboxypeptidase Y) mutant of yeast. J Bacteriol 1975;123:1150-1156.
    • (1975) J. Bacteriol. , vol.123 , pp. 1150-1156
    • Wolf, D.H.1    Fink, G.R.2
  • 79
    • 1642414731 scopus 로고    scopus 로고
    • Diversity of the mammalian sodium/proton exchanger SLC9 gene family
    • in press. On-line: DOI: 10.1007/s00424-00003-01110-00423. ISSN. 00031-06768
    • Orlowski J, Grinstein S. Diversity of the mammalian sodium/proton exchanger SLC9 gene family. Pflugers Arch Eur J Phys 2003: in press. On-line: DOI: 10.1007/s00424-00003-01110-00423. ISSN. 00031-06768.
    • (2003) Pflugers Arch. Eur. J. Phys.
    • Orlowski, J.1    Grinstein, S.2
  • 80
    • 0034535340 scopus 로고    scopus 로고
    • A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP
    • Kato M, Miyazawa K, Kitamura N. A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP. J Biol Chem 2000;275: 37481-37487.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37481-37487
    • Kato, M.1    Miyazawa, K.2    Kitamura, N.3
  • 81
    • 0028953080 scopus 로고
    • Golgi and vacuolar membrane proteins reach the vacuole in vps1 mutant yeast cells via the plasma membrane
    • Nothwehr SF, Conibear E, Stevens TH. Golgi and vacuolar membrane proteins reach the vacuole in vps1 mutant yeast cells via the plasma membrane. J Cell Biol 1995;129:35-46.
    • (1995) J. Cell Biol. , vol.129 , pp. 35-46
    • Nothwehr, S.F.1    Conibear, E.2    Stevens, T.H.3
  • 82
    • 0023739386 scopus 로고
    • Protein sorting in Saccharomyces cerevisiae: Isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
    • Robinson JS, Klionsky DJ, Banta LM, Emr SD. Protein sorting in Saccharomyces cerevisiae: Isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol Cell Biol 1988;8: 4936-4948.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 4936-4948
    • Robinson, J.S.1    Klionsky, D.J.2    Banta, L.M.3    Emr, S.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.