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Volumn 45, Issue 1, 2013, Pages 11-17

Endosomal cholesterol trafficking: Protein factors at a glance

Author keywords

endosomal cholesterol transport; Hrs; NPC1; NPC2; OSBP ORP

Indexed keywords

CHOLESTEROL; PROTEIN;

EID: 84871807255     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gms095     Document Type: Review
Times cited : (20)

References (62)
  • 1
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D and Simons K. Lipid rafts as a membrane-organizing principle. Science 2010, 327:46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 2
    • 67349268463 scopus 로고    scopus 로고
    • Oxysterols: Sources, cellular storage and metabolism, and new insights into their roles in cholesterol homeostasis
    • Brown AJ and Jessup W. Oxysterols: sources, cellular storage and metabolism, and new insights into their roles in cholesterol homeostasis. Mol Aspects Med 2009, 30:111-122.
    • (2009) Mol Aspects Med , vol.30 , pp. 111-122
    • Brown, A.J.1    Jessup, W.2
  • 3
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown MS and Goldstein JL. A receptor-mediated pathway for cholesterol homeostasis. Science 1986, 232:34-47. (Pubitemid 16037973)
    • (1986) Science , vol.232 , Issue.4746 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 6
    • 44849131929 scopus 로고    scopus 로고
    • Feedback Regulation of Cholesterol Syn thesis: Sterol-accelerated ubiquitination and degradation of HMG CoA reductase
    • DeBose-Boyd RA. Feedback regulation of cholesterol synthesis: sterol-accelerated ubiquitination and degradation of HMG CoA reductase. Cell Res 2008, 18:609-621.
    • (2008) Cell Res , vol.18 , pp. 609-621
    • Debose-Boyd, R.A.1
  • 7
    • 79952174597 scopus 로고    scopus 로고
    • Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase
    • Gill S, Stevenson J, Kristiana I and Brown AJ. Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase. Cell Metab 2011, 13:260-273.
    • (2011) Cell Metab , vol.13 , pp. 260-273
    • Gill, S.1    Stevenson, J.2    Kristiana, I.3    Brown, A.J.4
  • 8
    • 84865278091 scopus 로고    scopus 로고
    • Controlling the size of lipid droplets: Lipid and protein factors
    • Yang H, Galea A, Sytnyk V and Crossley M. Controlling the size of lipid droplets: lipid and protein factors. Curr Opin Cell Biol 2012, 24:509-516.
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 509-516
    • Yang, H.1    Galea, A.2    Sytnyk, V.3    Crossley, M.4
  • 11
    • 60549084168 scopus 로고    scopus 로고
    • Reversal of defective lysosomal transport in NPC disease ameliorates liver dysfunction and neurodegeneration in the npc1-/-mouse
    • Liu B, Turley SD, Burns DK, Miller AM, Repa JJ and Dietschy JM. Reversal of defective lysosomal transport in NPC disease ameliorates liver dysfunction and neurodegeneration in the npc1-/-mouse. Proc Natl Acad Sci USA 2009, 106:2377-2382.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 2377-2382
    • Liu, B.1    Turley, S.D.2    Burns, D.K.3    Miller, A.M.4    Repa, J.J.5    Dietschy, J.M.6
  • 12
    • 77950402392 scopus 로고    scopus 로고
    • Endocytosis of beta-cyclodextrins is responsible for cholesterol reduction in Niemann-Pick type C mutant cells
    • Rosenbaum AI, Zhang G, Warren JD and Maxfield FR. Endocytosis of beta-cyclodextrins is responsible for cholesterol reduction in Niemann-Pick type C mutant cells. Proc Natl Acad Sci USA 2010, 107:5477-5482.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5477-5482
    • Rosenbaum, A.I.1    Zhang, G.2    Warren, J.D.3    Maxfield, F.R.4
  • 13
    • 0034637440 scopus 로고    scopus 로고
    • Topological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and sterol regulatory element binding protein cleavage-activating protein
    • DOI 10.1074/jbc.M002184200
    • Davies JP and Ioannou YA. Topological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and sterol regulatory element binding protein cleavage-activating protein. J Biol Chem 2000, 275:24367-24374. (Pubitemid 30626526)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.32 , pp. 24367-24374
    • Davies, J.P.1    Ioannou, Y.A.2
  • 14
    • 69449089892 scopus 로고    scopus 로고
    • Membrane topology of human NPC1L1, a key protein in enterohepatic cholesterol absorption
    • Wang J, Chu BB, Ge L, Li BL, Yan Y and Song BL. Membrane topology of human NPC1L1, a key protein in enterohepatic cholesterol absorption. J Lipid Res 2009, 50:1653-1662.
    • (2009) J Lipid Res , vol.50 , pp. 1653-1662
    • Wang, J.1    Chu, B.B.2    Ge, L.3    Li, B.L.4    Yan, Y.5    Song, B.L.6
  • 16
    • 0346101770 scopus 로고    scopus 로고
    • Insig-dependent Ubiquitination and Degradation of Mammalian 3-Hydroxy-3-methylglutaryl-CoA Reductase Stimulated by Sterols and Geranylgeraniol
    • DOI 10.1074/jbc.M310053200
    • Sever N, Song BL, Yabe D, Goldstein JL, Brown MS and DeBose-Boyd RA. Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3- methylglutaryl-CoA reductase stimulated by sterols and gera-nylgeraniol. J Biol Chem 2003, 278:52479-52490. (Pubitemid 38035841)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 52479-52490
    • Sever, N.1    Song, B.-L.2    Yabe, D.3    Goldstein, J.L.4    Brown, M.S.5    DeBose-Boydb, R.A.6
  • 17
    • 0037162719 scopus 로고    scopus 로고
    • Crucial step in cholesterol homeostasis: Sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER
    • DOI 10.1016/S0092-8674(02)00872-3
    • Yang T, Espenshade PJ, Wright ME, Yabe D, Gong Y, Aebersold R and Goldstein JL, et al. Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER. Cell 2002, 110:489-500. (Pubitemid 35232292)
    • (2002) Cell , vol.110 , Issue.4 , pp. 489-500
    • Yang, T.1    Espenshade, P.J.2    Wright, M.E.3    Yabe, D.4    Gong, Y.5    Aebersold, R.6    Goldstein, J.L.7    Brown, M.S.8
  • 20
    • 69149089283 scopus 로고    scopus 로고
    • Nogo-B receptor stabilizes Niemann-Pick type C2 protein and regulates intracellular cholesterol trafficking
    • Harrison KD, Miao RQ, Fernandez-Hernando C, Suarez Y, Davalos A and Sessa WC. Nogo-B receptor stabilizes Niemann-Pick type C2 protein and regulates intracellular cholesterol trafficking. Cell Metab 2009, 10:208-218.
    • (2009) Cell Metab , vol.10 , pp. 208-218
    • Harrison, K.D.1    Miao, R.Q.2    Fernandez-Hernando, C.3    Suarez, Y.4    Davalos, A.5    Sessa, W.C.6
  • 22
    • 38149069055 scopus 로고    scopus 로고
    • Purified NPC1 protein. I. Binding of cholesterol and oxyster-ols to a 1278-amino acid membrane protein
    • Infante RE, Abi-Mosleh L, Radhakrishnan A, Dale JD, Brown MS and Goldstein JL. Purified NPC1 protein. I. Binding of cholesterol and oxyster-ols to a 1278-amino acid membrane protein. J Biol Chem 2008, 283:1052-1063.
    • (2008) J Biol Chem , vol.283 , pp. 1052-1063
    • Infante, R.E.1    Abi-Mosleh, L.2    Radhakrishnan, A.3    Dale, J.D.4    Brown, M.S.5    Goldstein, J.L.6
  • 24
    • 67549105629 scopus 로고    scopus 로고
    • Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol
    • Kwon HJ, Abi-Mosleh L, Wang ML, Deisenhofer J, Goldstein JL, Brown MS and Infante RE. Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol. Cell 2009, 137:1213-1224.
    • (2009) Cell , vol.137 , pp. 1213-1224
    • Kwon, H.J.1    Abi-Mosleh, L.2    Wang, M.L.3    Deisenhofer, J.4    Goldstein, J.L.5    Brown, M.S.6    Infante, R.E.7
  • 25
    • 34548192003 scopus 로고    scopus 로고
    • Structural basis of sterol binding by NPC2, a lysosomal protein deficient in Niemann-Pick type C2 disease
    • DOI 10.1074/jbc.M703848200
    • Xu S, Benoff B, Liou HL, Lobel P and Stock AM. Structural basis of sterol binding by NPC2, a lysosomal protein deficient in Niemann-Pick type C2 disease. J Biol Chem 2007, 282:23525-23531. (Pubitemid 47311925)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.32 , pp. 23525-23531
    • Xu, S.1    Benoff, B.2    Liou, H.-L.3    Lobel, P.4    Stock, A.M.5
  • 26
    • 55749083068 scopus 로고    scopus 로고
    • NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes
    • Infante RE, Wang ML, Radhakrishnan A, Kwon HJ, Brown MS and Goldstein JL. NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes. Proc Natl Acad Sci USA 2008, 105:15287-15292.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15287-15292
    • Infante, R.E.1    Wang, M.L.2    Radhakrishnan, A.3    Kwon, H.J.4    Brown, M.S.5    Goldstein, J.L.6
  • 27
    • 78649916808 scopus 로고    scopus 로고
    • Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes
    • Wang ML, Motamed M, Infante RE, Abi-Mosleh L, Kwon HJ, Brown MS and Goldstein JL. Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes. Cell Metab 2010, 12:166-173.
    • (2010) Cell Metab , vol.12 , pp. 166-173
    • Wang, M.L.1    Motamed, M.2    Infante, R.E.3    Abi-Mosleh, L.4    Kwon, H.J.5    Brown, M.S.6    Goldstein, J.L.7
  • 28
    • 82755197370 scopus 로고    scopus 로고
    • Niemann-Pick type C 1 function requires lumenal domain residues that mediate cholesterol-dependent NPC2 binding
    • Deffieu MS and Pfeffer SR. Niemann-Pick type C 1 function requires lumenal domain residues that mediate cholesterol-dependent NPC2 binding. Proc Natl Acad Sci USA 2011, 108:18932-18936.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 18932-18936
    • Deffieu, M.S.1    Pfeffer, S.R.2
  • 29
    • 55749101385 scopus 로고    scopus 로고
    • NPC1/NPC2 function as a tag team duo to mobilize cholesterol
    • Subramanian K and Balch WE. NPC1/NPC2 function as a tag team duo to mobilize cholesterol. Proc Natl Acad Sci USA 2008, 105:15223-15224.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15223-15224
    • Subramanian, K.1    Balch, W.E.2
  • 30
    • 0035163949 scopus 로고    scopus 로고
    • Dynamic movements of organelles containing Niemann-Pick C1 protein: NPC1 involvement in late endocytic events
    • Ko DC, Gordon MD, Jin JY and Scott MP. Dynamic movements of orga-nelles containing Niemann-Pick C1 protein: NPC1 involvement in late endocytic events. Mol Biol Cell 2001, 12:601-614. (Pubitemid 33052015)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.3 , pp. 601-614
    • Ko, D.C.1    Gordon, M.D.2    Jin, J.Y.3    Scott, M.P.4
  • 31
  • 32
    • 0141876961 scopus 로고    scopus 로고
    • Telomerase immortalization upregulates Rab9 expression and restores LDL cholesterol egress from Niemann-Pick C1 late endosomes
    • DOI 10.1194/jlr.M200230-JLR200
    • Walter M, Davies JP and Ioannou YA. Telomerase immortalization upregulates Rab9 expression and restores LDL cholesterol egress from Niemann-Pick C1 late endosomes. J Lipid Res 2003, 44:243-253. (Pubitemid 37287767)
    • (2003) Journal of Lipid Research , vol.44 , Issue.2 , pp. 243-253
    • Walter, M.1    Davies, J.P.2    Ioannou, Y.A.3
  • 33
    • 84860687550 scopus 로고    scopus 로고
    • Niemann-Pick C1-Like 1 and cholesterol uptake
    • Wang LJ and Song BL. Niemann-Pick C1-Like 1 and cholesterol uptake. Biochim Biophys Acta 2012, 1821:964-972.
    • (2012) Biochim Biophys Acta , vol.1821 , pp. 964-972
    • Wang, L.J.1    Song, B.L.2
  • 34
    • 77649274212 scopus 로고    scopus 로고
    • Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor interaction
    • Eden ER, White IJ, Tsapara A and Futter CE. Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor interaction. Nat Cell Biol 2010, 12:267-272.
    • (2010) Nat Cell Biol , vol.12 , pp. 267-272
    • Eden, E.R.1    White, I.J.2    Tsapara, A.3    Futter, C.E.4
  • 35
    • 67649600680 scopus 로고    scopus 로고
    • Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning
    • Rocha N, Kuijl C, van der Kant R, Janssen L, Houben D, Janssen H and Zwart W, et al. Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning. J Cell Biol 2009, 185:1209-1225.
    • (2009) J Cell Biol , vol.185 , pp. 1209-1225
    • Rocha, N.1    Kuijl, C.2    Van Der Kant, R.3    Janssen, L.4    Houben, D.5    Janssen, H.6    Zwart, W.7
  • 36
    • 38949137379 scopus 로고    scopus 로고
    • Characteristics of Oxysterol Binding Proteins
    • DOI 10.1016/S0074-7696(07)65007-4, PII S0074769607650074, A Survey of Cell Biology
    • Yan D and Olkkonen VM. Characteristics of oxysterol binding proteins. Int Rev Cytol 2008, 265:253-285. (Pubitemid 351222733)
    • (2008) International Review of Cytology , vol.265 , pp. 253-285
    • Yan, D.1    Olkkonen, V.M.2
  • 37
    • 77954469729 scopus 로고    scopus 로고
    • Functional implications of sterol transport by the oxysterol-binding protein gene family
    • Ngo MH, Colbourne TR and Ridgway ND. Functional implications of sterol transport by the oxysterol-binding protein gene family. Biochem J 2010, 429:13-24.
    • (2010) Biochem J , vol.429 , pp. 13-24
    • Ngo, M.H.1    Colbourne, T.R.2    Ridgway, N.D.3
  • 38
    • 33747885070 scopus 로고    scopus 로고
    • Nonvesicular sterol transport: two protein families and a sterol sensor?
    • DOI 10.1016/j.tcb.2006.07.002, PII S0962892406001747
    • Yang H. Nonvesicular sterol transport: two protein families and a sterol sensor? Trends Cell Biol 2006, 16:427-432. (Pubitemid 44293398)
    • (2006) Trends in Cell Biology , vol.16 , Issue.9 , pp. 427-432
    • Yang, H.1
  • 39
    • 0035108917 scopus 로고    scopus 로고
    • Overlapping functions of the yeast oxysterol-binding protein homologues
    • Beh CT, Cool L, Phillips J and Rine J. Overlapping functions of the yeast oxysterol-binding protein homologues. Genetics 2001, 157:1117-1140. (Pubitemid 32225007)
    • (2001) Genetics , vol.157 , Issue.3 , pp. 1117-1140
    • Beh, C.T.1    Cool, L.2    Phillips, J.3    Rine, J.4
  • 41
    • 0021747172 scopus 로고
    • Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase
    • Taylor FR, Saucier SE, Shown EP, Parish EJ and Kandutsch AA. Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase. J Biol Chem 1984, 259:12382-12387. (Pubitemid 15204812)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.20 , pp. 12382-12387
    • Taylor, F.R.1    Saucier, S.E.2    Shown, E.P.3
  • 43
    • 14644391519 scopus 로고    scopus 로고
    • OSBP is a cholesterol-regulated scaffolding protein in control of ERK1/2 activation
    • DOI 10.1126/science.1107710
    • Wang PY, Weng J and Anderson RG. OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation. Science 2005, 307:1472-1476. (Pubitemid 40321946)
    • (2005) Science , vol.307 , Issue.5714 , pp. 1472-1476
    • Wang, P.-Y.1    Weng, J.2    Anderson, R.G.W.3
  • 44
    • 24344455560 scopus 로고    scopus 로고
    • Structural mechanism for sterol sensing and transport by OSBP-related proteins
    • DOI 10.1038/nature03923, PII N03923
    • Im YJ, Raychaudhuri S, Prinz WA and Hurley JH. Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature 2005, 437:154-158. (Pubitemid 41613443)
    • (2005) Nature , vol.437 , Issue.7055 , pp. 154-158
    • Im, Y.J.1    Raychaudhuri, S.2    Prinz, W.A.3    Hurley, J.H.4
  • 46
    • 0038558194 scopus 로고    scopus 로고
    • A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP
    • DOI 10.1093/emboj/cdg201
    • Loewen CJ, Roy A and Levine TP. A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP. EMBO J 2003, 22:2025-2035. (Pubitemid 36565528)
    • (2003) EMBO Journal , vol.22 , Issue.9 , pp. 2025-2035
    • Loewen, C.J.R.1    Roy, A.2    Levine, T.P.3
  • 47
    • 0037119364 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum
    • Wyles JP, McMaster CR and Ridgway ND. Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum. J Biol Chem 2002, 277:29908-29918.
    • (2002) J Biol Chem , vol.277 , pp. 29908-29918
    • Wyles, J.P.1    McMaster, C.R.2    Ridgway, N.D.3
  • 49
    • 78651328466 scopus 로고    scopus 로고
    • A role for oxysterol-binding protein-related protein 5 in endosomal cholesterol trafficking
    • Du X, Kumar J, Ferguson C, Schulz TA, Ong YS, Hong W and Prinz WA, et al. A role for oxysterol-binding protein-related protein 5 in endosomal cholesterol trafficking. J Cell Biol 2011, 192:121-135.
    • (2011) J Cell Biol , vol.192 , pp. 121-135
    • Du, X.1    Kumar, J.2    Ferguson, C.3    Schulz, T.A.4    Ong, Y.S.5    Hong, W.6    Prinz, W.A.7
  • 50
    • 25444529050 scopus 로고    scopus 로고
    • AAA ATPases regulate membrane association of yeast oxysterol binding proteins and sterol metabolism
    • DOI 10.1038/sj.emboj.7600764, PII 7600764
    • Wang P, Zhang Y, Li H, Chieu HK, Munn AL and Yang H. AAA ATPases regulate membrane association of yeast oxysterol binding proteins and sterol metabolism. EMBO J 2005, 24:2989-2999. (Pubitemid 41486336)
    • (2005) EMBO Journal , vol.24 , Issue.17 , pp. 2989-2999
    • Wang, P.1    Zhang, Y.2    Li, H.3    Hai, K.C.4    Munn, A.L.5    Yang, H.6
  • 51
    • 84873254851 scopus 로고    scopus 로고
    • The AAA ATPase VPS4/SKD1 Regulates Endosomal Cholesterol Trafficking Independently of ESCRT-III
    • doi:10.1111/tra.12015
    • Du X, Kazim AS, Dawes IW, Brown AJ and Yang H. The AAA ATPase VPS4/SKD1 Regulates Endosomal Cholesterol Trafficking Independently of ESCRT-III. Traffic 2012, doi:10.1111/tra.12015.
    • (2012) Traffic
    • Du, X.1    Kazim, A.S.2    Dawes, I.W.3    Brown, A.J.4    Yang, H.5
  • 53
    • 57649218879 scopus 로고    scopus 로고
    • Proteomic analysis reveals Hrs ubiquitin-interacting motif-mediated ubiquitin signaling in multiple cellular processes
    • Pridgeon JW, Webber EA, Sha D, Li L and Chin LS. Proteomic analysis reveals Hrs ubiquitin-interacting motif-mediated ubiquitin signaling in multiple cellular processes. FEBS J 2009, 276:118-131.
    • (2009) FEBS J , vol.276 , pp. 118-131
    • Pridgeon, J.W.1    Webber, E.A.2    Sha, D.3    Li, L.4    Chin, L.S.5
  • 54
    • 0038323973 scopus 로고    scopus 로고
    • STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes
    • DOI 10.1074/jbc.M210843200
    • Bache KG, Raiborg C, Mehlum A and Stenmark H. STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J Biol Chem 2003, 278:12513-12521. (Pubitemid 36800240)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 12513-12521
    • Bache, K.G.1    Raiborg, C.2    Mehlum, A.3    Stenmark, H.4
  • 55
    • 0036304360 scopus 로고    scopus 로고
    • The Vps27p-Hse1p complex binds ubiquitin and mediates endosomal protein sorting
    • DOI 10.1038/ncb815
    • Bilodeau PS, Urbanowski JL, Winistorfer SC and Piper RC. The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Nat Cell Biol 2002, 4:534-539. (Pubitemid 34752441)
    • (2002) Nature Cell Biology , vol.4 , Issue.7 , pp. 534-539
    • Bilodeau, P.S.1    Urbanowski, J.L.2    Winistorfer, S.C.3    Piper, R.C.4
  • 56
    • 0042991262 scopus 로고    scopus 로고
    • Vps27 recruits ESCRT machinery to endosomes during MVB sorting
    • DOI 10.1083/jcb.200302136
    • Katzmann DJ, Stefan CJ, Babst M and Emr SD. Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J Cell Biol 2003, 162:413-423. (Pubitemid 36988551)
    • (2003) Journal of Cell Biology , vol.162 , Issue.3 , pp. 413-423
    • Katzmann, D.J.1    Stefan, C.J.2    Babst, M.3    Emr, S.D.4
  • 57
    • 0041488656 scopus 로고    scopus 로고
    • Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
    • DOI 10.1083/jcb.200302131
    • Bache KG, Brech A, Mehlum A and Stenmark H. Hrs regulates multivesi-cular body formation via ESCRT recruitment to endosomes. J Cell Biol 2003, 162:435-442. (Pubitemid 36988552)
    • (2003) Journal of Cell Biology , vol.162 , Issue.3 , pp. 435-442
    • Bache, K.G.1    Brech, A.2    Mehlum, A.3    Stenmark, H.4
  • 58
    • 0242266922 scopus 로고    scopus 로고
    • Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome
    • DOI 10.1083/jcb.200305007
    • Bilodeau PS, Winistorfer SC, Kearney WR, Robertson AD and 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. (Pubitemid 37363125)
    • (2003) Journal of Cell Biology , vol.163 , Issue.2 , pp. 237-243
    • Bilodeau, P.S.1    Winistorfer, S.C.2    Kearney, W.R.3    Robertson, A.D.4    Piper, R.C.5
  • 60
    • 84861148125 scopus 로고    scopus 로고
    • An Essential Role of Hrs/Vps27 in Endosomal Cholesterol Trafficking
    • Du X, Kazim Abdulla S, Brown Andrew J and Yang H. An Essential Role of Hrs/Vps27 in Endosomal Cholesterol Trafficking. Cell Reports 2012, 1:29-35.
    • (2012) Cell Reports , vol.1 , pp. 29-35
    • Du, X.1    Kazim Abdulla, S.2    Brown Andrew, J.3    Yang, H.4
  • 61
    • 0038620205 scopus 로고    scopus 로고
    • Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway
    • Mobius W, van Donselaar E, Ohno-Iwashita Y, Shimada Y, Heijnen HF, Slot JW and Geuze HJ. Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway. Traffic 2003, 4:222-231. (Pubitemid 36665383)
    • (2003) Traffic , vol.4 , Issue.4 , pp. 222-231
    • Mobius, W.1    Van Donselaar, E.2    Ohno-Iwashita, Y.3    Shimada, Y.4    Heijnen, H.F.G.5    Slot, J.W.6    Geuze, H.J.7
  • 62
    • 33745451679 scopus 로고    scopus 로고
    • Endosomal cholesterol traffic: Vesicular and non-vesicular mechanisms meet
    • DOI 10.1042/BST0340392
    • Holtta-Vuori M and Ikonen E. Endosomal cholesterol traffic: vesicular and non-vesicular mechanisms meet. Biochem Soc Trans 2006, 34:392-394. (Pubitemid 43953995)
    • (2006) Biochemical Society Transactions , vol.34 , Issue.3 , pp. 392-394
    • Holtta-Vuori, M.1    Ikonen, E.2


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