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Volumn 25, Issue 1, 2010, Pages 99-112

The early endosome: A busy sorting station for proteins at the crossroads

Author keywords

Disease; Endocytosis; Golgi; Traffic

Indexed keywords

PROTEIN;

EID: 74749099537     PISSN: 02133911     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (298)

References (157)
  • 1
    • 0028859410 scopus 로고
    • Rab4, but not the transferrin receptor, is colocalized with GLUT4 in an insulin-sensitive intracellular compartment in rat skeletal muscle
    • Aledo J.C., Darakhshan F. and Hundal H.S. (1995). Rab4, but not the transferrin receptor, is colocalized with GLUT4 in an insulin-sensitive intracellular compartment in rat skeletal muscle. Biochem. Biophys. Res. Commun. 215, 321-328.
    • (1995) Biochem. Biophys. Res. Commun , vol.215 , pp. 321-328
    • Aledo, J.C.1    Darakhshan, F.2    Hundal, H.S.3
  • 2
    • 2442530398 scopus 로고    scopus 로고
    • Role of the mammalian retromer in sorting of the cationindependent mannose 6-phosphate receptor
    • Arighi C.N., Hartnell L.M., Aguilar R.C., Haft C.R. and Bonifacino J.S. (2004). Role of the mammalian retromer in sorting of the cationindependent mannose 6-phosphate receptor. J. Cell Biol. 165, 123-33.
    • (2004) J. Cell Biol , vol.165 , pp. 123-133
    • Arighi, C.N.1    Hartnell, L.M.2    Aguilar, R.C.3    Haft, C.R.4    Bonifacino, J.S.5
  • 3
    • 33745596421 scopus 로고    scopus 로고
    • Rab10 regulates membrane transport through early endosomes of polarized Madin-Darby canine kidney cells
    • Babbey C.M., Ahktar N., Wang E., Chen C.C., Grant B.D. and Dunn K.W. (2006). Rab10 regulates membrane transport through early endosomes of polarized Madin-Darby canine kidney cells. Mol. Biol. Cell 17, 3156-3175.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3156-3175
    • Babbey, C.M.1    Ahktar, N.2    Wang, E.3    Chen, C.C.4    Grant, B.D.5    Dunn, K.W.6
  • 4
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: An endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst M., Katzmann D.J., Estepa-Sabal E.J., Meerloo T. and Emr S.D. (2002a). 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
  • 5
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • Babst M., Katzmann, D.J., Snyder W.B., Wendland B. and Emr S.D. (2002b). 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
  • 6
    • 0041488656 scopus 로고    scopus 로고
    • Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
    • Bache K.G., Brech A., Mehlum A. and Stenmark H. (2003a). Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes. J. Cell Biol. 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
  • 7
    • 0038323973 scopus 로고    scopus 로고
    • STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes
    • Bache K.G., Raiborg C., Mehlum A. and Stenmark H. (2003b). STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J. Biol. Chem. 278, 12513-12521.
    • (2003) J. Biol. Chem , vol.278 , pp. 12513-12521
    • Bache, K.G.1    Raiborg, C.2    Mehlum, A.3    Stenmark, H.4
  • 9
    • 27944470541 scopus 로고    scopus 로고
    • The structure and regulation of myotubularin phosphatases
    • Begley M.J. and Dixon J.E. (2005). The structure and regulation of myotubularin phosphatases. Curr. Opin. Struct. Biol. 15, 614-620.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 614-620
    • Begley, M.J.1    Dixon, J.E.2
  • 10
    • 1942445085 scopus 로고    scopus 로고
    • Endocytosis: Signaling from endocytic membranes to the nucleus
    • Benmerah A. (2004). Endocytosis: signaling from endocytic membranes to the nucleus. Curr. Biol. 14, R314-316.
    • (2004) Curr. Biol , vol.14
    • Benmerah, A.1
  • 11
    • 0029127250 scopus 로고
    • SNAREs and the specificity of transport vesicle targeting
    • Bennett M.K. (1995). SNAREs and the specificity of transport vesicle targeting. Curr. Opin. Cell Biol. 7, 581-586.
    • (1995) Curr. Opin. Cell Biol , vol.7 , pp. 581-586
    • Bennett, M.K.1
  • 12
    • 0034703432 scopus 로고    scopus 로고
    • Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway
    • Blondeau F., Laporte J., Bodin S., Superti-Furga G., Payrastre B. and Mandel J.L. (2000). Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway. Hum. Mol. Genet. 9, 2223-2229.
    • (2000) Hum. Mol. Genet , vol.9 , pp. 2223-2229
    • Blondeau, F.1    Laporte, J.2    Bodin, S.3    Superti-Furga, G.4    Payrastre, B.5    Mandel, J.L.6
  • 13
    • 0035865345 scopus 로고    scopus 로고
    • A genomic perspective on membrane compartment organization
    • Bock J.B., Matern H.T., Peden A.A. and Scheller R.H. (2001). A genomic perspective on membrane compartment organization. Nature 409, 839-841.
    • (2001) Nature , vol.409 , pp. 839-841
    • Bock, J.B.1    Matern, H.T.2    Peden, A.A.3    Scheller, R.H.4
  • 15
    • 33748313351 scopus 로고    scopus 로고
    • Retrograde transport from endosomes to the trans-Golgi network
    • Bonifacino J.S. and Rojas R. (2006). Retrograde transport from endosomes to the trans-Golgi network. Nat. Rev. Mol. Cell Biol. 7, 568-579.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 568-579
    • Bonifacino, J.S.1    Rojas, R.2
  • 17
    • 0026744303 scopus 로고
    • The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway
    • Bucci C., Parton R.G., Mather I.H., Stunnenberg H., Simons K., Hoflack B. and Zerial M. (1992). The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell 70, 715-728.
    • (1992) Cell , vol.70 , pp. 715-728
    • Bucci, C.1    Parton, R.G.2    Mather, I.H.3    Stunnenberg, H.4    Simons, K.5    Hoflack, B.6    Zerial, M.7
  • 18
    • 0037107491 scopus 로고    scopus 로고
    • Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase
    • Burda P., Padilla S.M., Sarkar S. and Emr S.D. (2002). Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase. J. Cell Sci. 115, 3889-3900.
    • (2002) J. Cell Sci , vol.115 , pp. 3889-3900
    • Burda, P.1    Padilla, S.M.2    Sarkar, S.3    Emr, S.D.4
  • 19
    • 33645230242 scopus 로고    scopus 로고
    • Cloning and subcellular localization of a human phosphatidylinositol 3-phosphate 5-kinase, PIKfyve/Fab1
    • Cabezas A., Pattni K. and Stenmark H. (2006). Cloning and subcellular localization of a human phosphatidylinositol 3-phosphate 5-kinase, PIKfyve/Fab1. Gene 371, 34-41.
    • (2006) Gene , vol.371 , pp. 34-41
    • Cabezas, A.1    Pattni, K.2    Stenmark, H.3
  • 20
    • 0033575916 scopus 로고    scopus 로고
    • A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor
    • Cao T.T., Deacon H.W., Reczek D., Bretscher A. and von Zastrow M. (1999). A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor. Nature 401, 286-290.
    • (1999) Nature , vol.401 , pp. 286-290
    • Cao, T.T.1    Deacon, H.W.2    Reczek, D.3    Bretscher, A.4    von Zastrow, M.5
  • 21
    • 34447543013 scopus 로고    scopus 로고
    • Myotubularin lipid phosphatase binds the hVPS15/hVPS34 lipid kinase complex on endosomes
    • Cao C., Laporte J., Backer J.M., Wandinger-Ness A. and Stein M.P. (2007). Myotubularin lipid phosphatase binds the hVPS15/hVPS34 lipid kinase complex on endosomes. Traffic 8, 1052-1067.
    • (2007) Traffic , vol.8 , pp. 1052-1067
    • Cao, C.1    Laporte, J.2    Backer, J.M.3    Wandinger-Ness, A.4    Stein, M.P.5
  • 22
    • 54249096642 scopus 로고    scopus 로고
    • Sequential actions of myotubularin lipid phosphatases regulate endosomal PI(3)P and growth factor receptor trafficking
    • Cao C., Backer J.M., Laporte J., Bedrick E.J. and Wandinger-Ness A. (2008). Sequential actions of myotubularin lipid phosphatases regulate endosomal PI(3)P and growth factor receptor trafficking. Mol. Biol. Cell 19, 3334-3346.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3334-3346
    • Cao, C.1    Backer, J.M.2    Laporte, J.3    Bedrick, E.J.4    Wandinger-Ness, A.5
  • 23
    • 0037013961 scopus 로고    scopus 로고
    • A tubular EHD1-containing compartment involved in the recycling of major histocompatibility complex class I molecules to the plasma membrane
    • Caplan S., Naslavsky N., Hartnell L.M., Lodge R., Polishchuk R.S., Donaldson J.G. and Bonifacino J.S. (2002). A tubular EHD1-containing compartment involved in the recycling of major histocompatibility complex class I molecules to the plasma membrane. EMBO J. 21, 2557-2567.
    • (2002) EMBO J , vol.21 , pp. 2557-2567
    • Caplan, S.1    Naslavsky, N.2    Hartnell, L.M.3    Lodge, R.4    Polishchuk, R.S.5    Donaldson, J.G.6    Bonifacino, J.S.7
  • 24
    • 6944255481 scopus 로고    scopus 로고
    • Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides
    • Carlton J., Bujny M., Peter B.J., Oorschot V.M., Rutherford A., Mellor H., Klumperman J., McMahon H.T. and Cullen P.J. (2004). Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides. Curr. Biol. 14, 1791-1800.
    • (2004) Curr. Biol , vol.14 , pp. 1791-1800
    • Carlton, J.1    Bujny, M.2    Peter, B.J.3    Oorschot, V.M.4    Rutherford, A.5    Mellor, H.6    Klumperman, J.7    McMahon, H.T.8    Cullen, P.J.9
  • 25
    • 0030836345 scopus 로고    scopus 로고
    • Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: Neuropathologic evidence for a mechanism of increased beta-amyloidogenesis
    • Cataldo A.M., Barnett J.L., Pieroni C. and Nixon R.A. (1997). Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: neuropathologic evidence for a mechanism of increased beta-amyloidogenesis. J. Neurosci. 17, 6142-6151.
    • (1997) J. Neurosci , vol.17 , pp. 6142-6151
    • Cataldo, A.M.1    Barnett, J.L.2    Pieroni, C.3    Nixon, R.A.4
  • 29
    • 38349010745 scopus 로고    scopus 로고
    • Myosin VI and its interacting protein LMTK2 regulate tubule formation and transport to the endocytic recycling compartment
    • Chibalina M.V., Seaman M.N., Miller C.C., Kendrick-Jones J. and Buss F. (2007). Myosin VI and its interacting protein LMTK2 regulate tubule formation and transport to the endocytic recycling compartment. J. Cell Sci. 120, 4278-4288.
    • (2007) J. Cell Sci , vol.120 , pp. 4278-4288
    • Chibalina, M.V.1    Seaman, M.N.2    Miller, C.C.3    Kendrick-Jones, J.4    Buss, F.5
  • 32
    • 53849101821 scopus 로고    scopus 로고
    • The structure and function of the retromer protein complex
    • Collins B.M. (2008). The structure and function of the retromer protein complex. Traffic 9, 1811-1822.
    • (2008) Traffic , vol.9 , pp. 1811-1822
    • Collins, B.M.1
  • 33
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner S.D. and Schmid S.L. (2003). Regulated portals of entry into the cell. Nature 422, 37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 35
    • 0037073673 scopus 로고    scopus 로고
    • The phox homology (PX) domaindependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation
    • Cozier G.E., Carlton J., McGregor A.H., Gleeson P.A., Teasdale R.D., Mellor H. and Cullen P.J. (2002). The phox homology (PX) domaindependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation. J. Biol. Chem. 277, 48730-48736.
    • (2002) J. Biol. Chem , vol.277 , pp. 48730-48736
    • Cozier, G.E.1    Carlton, J.2    McGregor, A.H.3    Gleeson, P.A.4    Teasdale, R.D.5    Mellor, H.6    Cullen, P.J.7
  • 36
    • 45849124923 scopus 로고    scopus 로고
    • Endosomal sorting and signalling: An emerging role for sorting nexins
    • Cullen P.J. (2008). Endosomal sorting and signalling: an emerging role for sorting nexins. Nat. Rev. Mol. Cell Biol. 9, 574-582.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 574-582
    • Cullen, P.J.1
  • 38
    • 0029819555 scopus 로고    scopus 로고
    • Rab4 and cellubrevin define different early endosome populations on the pathway of transferrin receptor recycling
    • Daro E., van der Sluijs P., Galli T. and Mellman I. (1996). Rab4 and cellubrevin define different early endosome populations on the pathway of transferrin receptor recycling. Proc. Natl. Acad. Sci. USA 93, 9559-9564.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9559-9564
    • Daro, E.1    van der Sluijs, P.2    Galli, T.3    Mellman, I.4
  • 39
    • 0000241799 scopus 로고
    • pH and the recycling of transferrin during receptor-mediated endocytosis
    • Dautry-Varsat A., Ciechanover A. and Lodish H.F. (1983). pH and the recycling of transferrin during receptor-mediated endocytosis. Proc. Natl. Acad. Sci. USA 80, 2258-2262.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2258-2262
    • Dautry-Varsat, A.1    Ciechanover, A.2    Lodish, H.F.3
  • 40
    • 0036172652 scopus 로고    scopus 로고
    • Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes
    • de Renzis S., Sonnichsen B. and Zerial M. (2002). Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes. Nat. Cell Biol. 4, 124-133.
    • (2002) Nat. Cell Biol , vol.4 , pp. 124-133
    • de Renzis, S.1    Sonnichsen, B.2    Zerial, M.3
  • 42
    • 0036167649 scopus 로고    scopus 로고
    • Rab'ing up endosomal membrane transport
    • Deneka M. and van der Sluijs P. (2002). 'Rab'ing up endosomal membrane transport. Nat. Cell Biol. 4, E33-35.
    • (2002) Nat. Cell Biol , vol.4
    • Deneka, M.1    van der Sluijs, P.2
  • 43
    • 0038605239 scopus 로고    scopus 로고
    • Rabaptin-5alpha/rabaptin-4 serves as a linker between rab4 and gamma(1)-adaptin in membrane recycling from endosomes
    • Deneka M., Neeft M., Popa I., van Oort M., Sprong H., Oorschot V., Klumperman J., Schu P. and van der Sluijs P. (2003). Rabaptin-5alpha/rabaptin-4 serves as a linker between rab4 and gamma(1)-adaptin in membrane recycling from endosomes. EMBO J. 22, 2645-2657.
    • (2003) EMBO J , vol.22 , pp. 2645-2657
    • Deneka, M.1    Neeft, M.2    Popa, I.3    van Oort, M.4    Sprong, H.5    Oorschot, V.6    Klumperman, J.7    Schu, P.8    van der Sluijs, P.9
  • 45
    • 46349097361 scopus 로고    scopus 로고
    • Membrane traffic and muscle: Lessons from human disease
    • Dowling J.J., Gibbs E.M. and Feldman E.L. (2008). Membrane traffic and muscle: lessons from human disease. Traffic 9, 1035-1043.
    • (2008) Traffic , vol.9 , pp. 1035-1043
    • Dowling, J.J.1    Gibbs, E.M.2    Feldman, E.L.3
  • 46
    • 0024842857 scopus 로고
    • Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome
    • Dunn K.W., McGraw T.E. and Maxfield F.R. (1989). Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome. J. Cell Biol. 109, 3303-3314.
    • (1989) J. Cell Biol , vol.109 , pp. 3303-3314
    • Dunn, K.W.1    McGraw, T.E.2    Maxfield, F.R.3
  • 48
    • 0041659220 scopus 로고    scopus 로고
    • Structural insights into the SNARE mechanism
    • Fasshauer D. (2003). Structural insights into the SNARE mechanism. Biochim. Biophys. Acta 1641, 87-97.
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 87-97
    • Fasshauer, D.1
  • 49
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer D., Sutton R.B., Brunger A.T. and Jahn R. (1998). Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Natl. Acad. Sci. USA 95, 15781-15786.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 51
    • 35948968787 scopus 로고    scopus 로고
    • EHD1 interacts with retromer to stabilize SNX1 tubules and facilitate endosome-to-Golgi retrieval
    • Gokool S., Tattersall D. and Seaman M.N. (2007). EHD1 interacts with retromer to stabilize SNX1 tubules and facilitate endosome-to-Golgi retrieval. Traffic 8, 1873-1886.
    • (2007) Traffic , vol.8 , pp. 1873-1886
    • Gokool, S.1    Tattersall, D.2    Seaman, M.N.3
  • 52
    • 0025974686 scopus 로고
    • rab5 controls early endosome fusion in vitro
    • Gorvel J.P., Chavrier P., Zerial M. and Gruenberg J. (1991). rab5 controls early endosome fusion in vitro. Cell 64, 915-925.
    • (1991) Cell , vol.64 , pp. 915-925
    • Gorvel, J.P.1    Chavrier, P.2    Zerial, M.3    Gruenberg, J.4
  • 53
    • 56149084770 scopus 로고    scopus 로고
    • Mechanisms of EHD/RME-1 protein function in endocytic transport
    • Grant B.D. and Caplan S. (2008). Mechanisms of EHD/RME-1 protein function in endocytic transport. Traffic 9, 2043-2052.
    • (2008) Traffic , vol.9 , pp. 2043-2052
    • Grant, B.D.1    Caplan, S.2
  • 54
    • 33747066132 scopus 로고    scopus 로고
    • Rabs and their effectors: Achieving specificity in membrane traffic
    • Grosshans B.L., Ortiz D. and Novick P. (2006). Rabs and their effectors: achieving specificity in membrane traffic. Proc. Natl. Acad. Sci. USA 103, 11821-11827.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11821-11827
    • Grosshans, B.L.1    Ortiz, D.2    Novick, P.3
  • 55
    • 0035490884 scopus 로고    scopus 로고
    • The endocytic pathway: A mosaic of domains
    • Gruenberg J. (2001). The endocytic pathway: a mosaic of domains. Nat. Rev. Mol. Cell Biol. 2, 721-730.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 721-730
    • Gruenberg, J.1
  • 56
    • 0042266431 scopus 로고    scopus 로고
    • Lipids in endocytic membrane transport and sorting
    • Gruenberg J. (2003). Lipids in endocytic membrane transport and sorting. Curr. Opin. Cell Biol. 15, 382-388.
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 382-388
    • Gruenberg, J.1
  • 57
    • 0024517745 scopus 로고
    • Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in vitro
    • Gruenberg J., Griffiths G. and Howell K.E. (1989). Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in vitro. J. Cell Biol. 108, 1301-1316.
    • (1989) J. Cell Biol , vol.108 , pp. 1301-1316
    • Gruenberg, J.1    Griffiths, G.2    Howell, K.E.3
  • 58
    • 0038394715 scopus 로고    scopus 로고
    • Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
    • Haglund K., Sigismund S., Polo S., Szymkiewicz I., Di Fiore P.P. and Dikic I. (2003). Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat. Cell Biol. 5, 461-466.
    • (2003) Nat. Cell Biol , vol.5 , pp. 461-466
    • Haglund, K.1    Sigismund, S.2    Polo, S.3    Szymkiewicz, I.4    Di Fiore, P.P.5    Dikic, I.6
  • 59
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson P.I., Roth R., Morisaki H., Jahn R. and Heuser J.E. (1997). Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 61
    • 22744455819 scopus 로고    scopus 로고
    • Essential role of Hrs in a recycling mechanism mediating functional resensitization of cell signaling
    • Hanyaloglu A.C., McCullagh E. and von Zastrow M. (2005). Essential role of Hrs in a recycling mechanism mediating functional resensitization of cell signaling. EMBO J. 24, 2265-2283.
    • (2005) EMBO J , vol.24 , pp. 2265-2283
    • Hanyaloglu, A.C.1    McCullagh, E.2    von Zastrow, M.3
  • 62
    • 0029193585 scopus 로고
    • Wortmannin, an inhibitor of phosphatidylinositol 3-kinase
    • In Japanese
    • Hazeki O. (1995). Wortmannin, an inhibitor of phosphatidylinositol 3-kinase. Seikagaku 67, 33-36 (In Japanese).
    • (1995) Seikagaku , vol.67 , pp. 33-36
    • Hazeki, O.1
  • 63
    • 0028335378 scopus 로고
    • Regulation of postendocytic trafficking of the epidermal growth factor receptor through endosomal retention
    • Herbst J.J., Opresko L.K., Walsh B.J., Lauffenburger D.A. and Wiley H.S. (1994). Regulation of postendocytic trafficking of the epidermal growth factor receptor through endosomal retention. J. Biol. Chem. 269, 12865-12873.
    • (1994) J. Biol. Chem , vol.269 , pp. 12865-12873
    • Herbst, J.J.1    Opresko, L.K.2    Walsh, B.J.3    Lauffenburger, D.A.4    Wiley, H.S.5
  • 65
    • 0020601856 scopus 로고
    • Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells
    • Hopkins C.R. and Trowbridge I.S. (1983). Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells. J. Cell Biol. 97, 508-521.
    • (1983) J. Cell Biol , vol.97 , pp. 508-521
    • Hopkins, C.R.1    Trowbridge, I.S.2
  • 66
    • 0030921812 scopus 로고    scopus 로고
    • A sorting nexin-1 homologue, Vps5p, forms a complex with Vps17p and is required for recycling the vacuolar protein-sorting receptor
    • Horazdovsky B.F., Davies B.A. Seaman M.N., McLaughlin S.A., Yoon S. and Emr S.D. (1997). A sorting nexin-1 homologue, Vps5p, forms a complex with Vps17p and is required for recycling the vacuolar protein-sorting receptor. Mol. Biol. Cell 8, 1529-1541.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1529-1541
    • Horazdovsky, B.F.1    Davies, B.A.2    Seaman, M.N.3    McLaughlin, S.A.4    Yoon, S.5    Emr, S.D.6
  • 67
    • 17344377424 scopus 로고    scopus 로고
    • A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function
    • Horiuchi H., Lippe R., McBride H.M., Rubino M., Woodman P., Stenmark H., Rybin V., Wilm M., Ashman K., Mann M. et al. (1997). A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function. Cell 90, 1149-1159.
    • (1997) Cell , vol.90 , pp. 1149-1159
    • Horiuchi, H.1    Lippe, R.2    McBride, H.M.3    Rubino, M.4    Woodman, P.5    Stenmark, H.6    Rybin, V.7    Wilm, M.8    Ashman, K.9    Mann, M.10
  • 68
    • 0035854730 scopus 로고    scopus 로고
    • Mammalian cell morphology and endocytic membrane homeostasis require enzymatically active phosphoinositide 5-kinase PIKfyve
    • Ikonomov O.C., Sbrissa D. and Shisheva A. (2001). Mammalian cell morphology and endocytic membrane homeostasis require enzymatically active phosphoinositide 5-kinase PIKfyve. J. Biol. Chem. 276, 26141-26147.
    • (2001) J. Biol. Chem , vol.276 , pp. 26141-26147
    • Ikonomov, O.C.1    Sbrissa, D.2    Shisheva, A.3
  • 69
    • 0037088590 scopus 로고    scopus 로고
    • Functional dissection of lipid and protein kinase signals of PIKfyve reveals the role of PtdIns 3,5-P2 production for endomembrane integrity
    • Ikonomov O.C., Sbrissa D., Mlak K., Kanzaki M., Pessin J. and Shisheva A. (2002). Functional dissection of lipid and protein kinase signals of PIKfyve reveals the role of PtdIns 3,5-P2 production for endomembrane integrity. J. Biol. Chem. 277, 9206-9211.
    • (2002) J. Biol. Chem , vol.277 , pp. 9206-9211
    • Ikonomov, O.C.1    Sbrissa, D.2    Mlak, K.3    Kanzaki, M.4    Pessin, J.5    Shisheva, A.6
  • 70
    • 0345687290 scopus 로고    scopus 로고
    • PIKfyve controls fluid phase endocytosis but not recycling/degradation of endocytosed receptors or sorting of procathepsin D by regulating multivesicular body morphogenesis
    • Ikonomov O.C., Sbrissa D., Foti M., Carpentier J.L. and Shisheva A. (2003). PIKfyve controls fluid phase endocytosis but not recycling/degradation of endocytosed receptors or sorting of procathepsin D by regulating multivesicular body morphogenesis. Mol. Biol. Cell 14, 4581-4591.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4581-4591
    • Ikonomov, O.C.1    Sbrissa, D.2    Foti, M.3    Carpentier, J.L.4    Shisheva, A.5
  • 71
    • 0027764386 scopus 로고
    • Endosome acidification and receptor trafficking: Bafilomycin A1 slows receptor externalization by a mechanism involving the receptor's internalization motif
    • Johnson L.S., Dunn K.W., Pytowski B. and McGraw T.E. (1993). Endosome acidification and receptor trafficking: bafilomycin A1 slows receptor externalization by a mechanism involving the receptor's internalization motif. Mol. Biol. Cell 4, 1251-1266.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1251-1266
    • Johnson, L.S.1    Dunn, K.W.2    Pytowski, B.3    McGraw, T.E.4
  • 72
    • 34047155597 scopus 로고    scopus 로고
    • EHD1 regulates beta1 integrin endosomal transport: Effects on focal adhesions, cell spreading and migration
    • Jovic M., Naslavsky N., Rapaport D., Horowitz M. and Caplan S. (2007). EHD1 regulates beta1 integrin endosomal transport: effects on focal adhesions, cell spreading and migration. J. Cell Sci. 120, 802-814.
    • (2007) J. Cell Sci , vol.120 , pp. 802-814
    • Jovic, M.1    Naslavsky, N.2    Rapaport, D.3    Horowitz, M.4    Caplan, S.5
  • 75
  • 76
    • 0034602964 scopus 로고    scopus 로고
    • The FYVE domain of early endosome antigen 1 is required for both phosphatidylinositol 3-phosphate and Rab5 binding. Critical role of this dual interaction for endosomal localization
    • Lawe D.C., Patki V., Heller-Harrison R., Lambright D. and Corvera S. (2000). The FYVE domain of early endosome antigen 1 is required for both phosphatidylinositol 3-phosphate and Rab5 binding. Critical role of this dual interaction for endosomal localization. J. Biol. Chem. 275, 3699-3705.
    • (2000) J. Biol. Chem , vol.275 , pp. 3699-3705
    • Lawe, D.C.1    Patki, V.2    Heller-Harrison, R.3    Lambright, D.4    Corvera, S.5
  • 77
    • 0032538989 scopus 로고    scopus 로고
    • The monomeric guanosine triphosphatase rab4 controls an essential step on the pathway of receptor-mediated antigen processing in B cells
    • Lazzarino D.A., Blier P. and Mellman I. (1998). The monomeric guanosine triphosphatase rab4 controls an essential step on the pathway of receptor-mediated antigen processing in B cells. J. Exp. Med. 188, 1769-1774.
    • (1998) J. Exp. Med , vol.188 , pp. 1769-1774
    • Lazzarino, D.A.1    Blier, P.2    Mellman, I.3
  • 78
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • Lin R.C. and Scheller R.H. (1997). Structural organization of the synaptic exocytosis core complex. Neuron 19, 1087-1094.
    • (1997) Neuron , vol.19 , pp. 1087-1094
    • Lin, R.C.1    Scheller, R.H.2
  • 79
    • 0034965057 scopus 로고    scopus 로고
    • Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells
    • Lin S.X., Grant B., Hirsh D. and Maxfield F.R. (2001). Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells. Nat. Cell Biol. 3, 567-572.
    • (2001) Nat. Cell Biol , vol.3 , pp. 567-572
    • Lin, S.X.1    Grant, B.2    Hirsh, D.3    Maxfield, F.R.4
  • 80
    • 0035171352 scopus 로고    scopus 로고
    • Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex
    • Lippe R., Miaczynska M., Rybin V., Runge A. and Zerial M. (2001). Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex. Mol. Biol. Cell 12, 2219-2228.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2219-2228
    • Lippe, R.1    Miaczynska, M.2    Rybin, V.3    Runge, A.4    Zerial, M.5
  • 83
    • 53549094933 scopus 로고    scopus 로고
    • Ubiquitin binding and conjugation regulate the recruitment of Rabex-5 to early endosomes
    • Mattera R. and Bonifacino J.S. (2008). Ubiquitin binding and conjugation regulate the recruitment of Rabex-5 to early endosomes. EMBO J. 27, 2484-2494.
    • (2008) EMBO J , vol.27 , pp. 2484-2494
    • Mattera, R.1    Bonifacino, J.S.2
  • 85
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer A., Wickner W. and Haas A. (1996). Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85, 83-94.
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 86
    • 0027243406 scopus 로고
    • Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process
    • Mayor S., Presley J.F. and Maxfield F.R. (1993). Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process. J. Cell Biol. 121, 1257-1269.
    • (1993) J. Cell Biol , vol.121 , pp. 1257-1269
    • Mayor, S.1    Presley, J.F.2    Maxfield, F.R.3
  • 87
    • 0033529564 scopus 로고    scopus 로고
    • Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13
    • McBride H.M., Rybin V., Murphy C., Giner A., Teasdale R. and Zerial M. (1999). Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell 98, 377-386.
    • (1999) Cell , vol.98 , pp. 377-386
    • McBride, H.M.1    Rybin, V.2    Murphy, C.3    Giner, A.4    Teasdale, R.5    Zerial, M.6
  • 89
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman I. (1996). Endocytosis and molecular sorting. Annu. Rev. Cell Dev. Biol. 12, 575-625.
    • (1996) Annu. Rev. Cell Dev. Biol , vol.12 , pp. 575-625
    • Mellman, I.1
  • 90
    • 0035202869 scopus 로고    scopus 로고
    • Rab22a affects the morphology and function of the endocytic pathway
    • Mesa R., Salomon C., Roggero M., Stahl P.D. and Mayorga L.S. (2001). Rab22a affects the morphology and function of the endocytic pathway. J. Cell. Sci. 114, 4041-4049.
    • (2001) J. Cell. Sci , vol.114 , pp. 4041-4049
    • Mesa, R.1    Salomon, C.2    Roggero, M.3    Stahl, P.D.4    Mayorga, L.S.5
  • 91
    • 14644437060 scopus 로고    scopus 로고
    • Overexpression of Rab22a hampers the transport between endosomes and the Golgi apparatus
    • Mesa R., Magadan J., Barbieri A., Lopez C., Stahl P.D. and Mayorga L.S. (2005). Overexpression of Rab22a hampers the transport between endosomes and the Golgi apparatus. Exp. Cell Res. 304, 339-353.
    • (2005) Exp. Cell Res , vol.304 , pp. 339-353
    • Mesa, R.1    Magadan, J.2    Barbieri, A.3    Lopez, C.4    Stahl, P.D.5    Mayorga, L.S.6
  • 93
    • 0032537835 scopus 로고    scopus 로고
    • Involvement of the endosomal autoantigen EEA1 in homotypic fusion of early endosomes
    • Mills I.G., Jones A.T. and Clague M.J. (1998). Involvement of the endosomal autoantigen EEA1 in homotypic fusion of early endosomes. Curr. Biol. 8, 881-884.
    • (1998) Curr. Biol , vol.8 , pp. 881-884
    • Mills, I.G.1    Jones, A.T.2    Clague, M.J.3
  • 95
    • 0034988109 scopus 로고    scopus 로고
    • Relationships between EEA1 binding partners and their role in endosome fusion
    • Mills I.G., Urbe S. and Clague M.J. (2001). Relationships between EEA1 binding partners and their role in endosome fusion. J. Cell Sci. 114, 1959-1965.
    • (2001) J. Cell Sci , vol.114 , pp. 1959-1965
    • Mills, I.G.1    Urbe, S.2    Clague, M.J.3
  • 97
    • 2942736876 scopus 로고    scopus 로고
    • A role for Hrs in endosomal sorting of ligand-stimulated and unstimulated epidermal growth factor receptor
    • Morino C., Kato M., Yamamoto A., Mizuno E., Hayakawa A., Komada M. and Kitamura N. (2004). A role for Hrs in endosomal sorting of ligand-stimulated and unstimulated epidermal growth factor receptor. Exp. Cell Res. 297, 380-391.
    • (2004) Exp. Cell Res , vol.297 , pp. 380-391
    • Morino, C.1    Kato, M.2    Yamamoto, A.3    Mizuno, E.4    Hayakawa, A.5    Komada, M.6    Kitamura, N.7
  • 98
    • 0037677208 scopus 로고    scopus 로고
    • Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation
    • Mosesson Y., Shtiegman K., Katz M., Zwang Y., Vereb G., Szollosi J. and Yarden Y. (2003). Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation. J. Biol. Chem. 278, 21323-21326.
    • (2003) J. Biol. Chem , vol.278 , pp. 21323-21326
    • Mosesson, Y.1    Shtiegman, K.2    Katz, M.3    Zwang, Y.4    Vereb, G.5    Szollosi, J.6    Yarden, Y.7
  • 100
    • 0035968220 scopus 로고    scopus 로고
    • SopE acts as an Rab5-specific nucleotide exchange factor and recruits non-prenylated Rab5 on Salmonella-containing phagosomes to promote fusion with early endosomes
    • Mukherjee K., Parashuraman S., Raje M. and Mukhopadhyay A. (2001). SopE acts as an Rab5-specific nucleotide exchange factor and recruits non-prenylated Rab5 on Salmonella-containing phagosomes to promote fusion with early endosomes. J. Biol. Chem. 276, 23607-23615.
    • (2001) J. Biol. Chem , vol.276 , pp. 23607-23615
    • Mukherjee, K.1    Parashuraman, S.2    Raje, M.3    Mukhopadhyay, A.4
  • 101
    • 0036300306 scopus 로고    scopus 로고
    • Role of Rab5 in the recruitment of hVps34/p150 to the early endosome
    • Murray J.T., Panaretou C., Stenmark H., Miaczynska M. and Backer J.M. (2002). Role of Rab5 in the recruitment of hVps34/p150 to the early endosome. Traffic 3, 416-427.
    • (2002) Traffic , vol.3 , pp. 416-427
    • Murray, J.T.1    Panaretou, C.2    Stenmark, H.3    Miaczynska, M.4    Backer, J.M.5
  • 102
    • 27144515960 scopus 로고    scopus 로고
    • C-terminal EH-domain-containing proteins: Consensus for a role in endocytic trafficking, EH?
    • Naslavsky N. and Caplan S. (2005). C-terminal EH-domain-containing proteins: consensus for a role in endocytic trafficking, EH? J. Cell Sci. 118, 4093-4101.
    • (2005) J. Cell Sci , vol.118 , pp. 4093-4101
    • Naslavsky, N.1    Caplan, S.2
  • 103
    • 2342489409 scopus 로고    scopus 로고
    • Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane
    • Naslavsky N., Boehm M., Backlund P.S. Jr. and Caplan S. (2004). Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane. Mol. Biol. Cell 15, 2410-2422.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2410-2422
    • Naslavsky, N.1    Boehm, M.2    Backlund Jr., P.S.3    Caplan, S.4
  • 104
    • 65249113299 scopus 로고    scopus 로고
    • EHD3 regulates early-endosome-to-Golgi transport and preserves Golgi morphology
    • Naslavsky N., McKenzie J., Altan-Bonnet N., Sheff D. and Caplan S. (2009). EHD3 regulates early-endosome-to-Golgi transport and preserves Golgi morphology. J. Cell Sci. 122, 389-400.
    • (2009) J. Cell Sci , vol.122 , pp. 389-400
    • Naslavsky, N.1    McKenzie, J.2    Altan-Bonnet, N.3    Sheff, D.4    Caplan, S.5
  • 105
    • 30044449424 scopus 로고    scopus 로고
    • Interactions between EHD proteins and Rab11-FIP2: A role for EHD3 in early endosomal transport
    • Naslavsky N., Rahajeng J., Sharma M., Jovic M. and Caplan S. (2006). Interactions between EHD proteins and Rab11-FIP2: a role for EHD3 in early endosomal transport. Mol. Biol. Cell 17, 163-177.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 163-177
    • Naslavsky, N.1    Rahajeng, J.2    Sharma, M.3    Jovic, M.4    Caplan, S.5
  • 106
    • 47649106149 scopus 로고    scopus 로고
    • Endosomal phosphoinositides and human diseases
    • Nicot A.S., and Laporte J. (2008). Endosomal phosphoinositides and human diseases. Traffic 9, 1240-1249.
    • (2008) Traffic , vol.9 , pp. 1240-1249
    • Nicot, A.S.1    Laporte, J.2
  • 109
    • 0034675999 scopus 로고    scopus 로고
    • Sorting of yeast membrane proteins into an endosome-to-Golgi pathway involves direct interaction of their cytosolic domains with Vps35p
    • Nothwehr S.F., Ha S.A. and Bruinsma P. (2000). Sorting of yeast membrane proteins into an endosome-to-Golgi pathway involves direct interaction of their cytosolic domains with Vps35p. J. Cell Biol. 151, 297-310.
    • (2000) J. Cell Biol , vol.151 , pp. 297-310
    • Nothwehr, S.F.1    Ha, S.A.2    Bruinsma, P.3
  • 111
    • 6344273112 scopus 로고    scopus 로고
    • In vitro formation of recycling vesicles from endosomes requires adaptor protein-1/clathrin and is regulated by rab4 and the connector rabaptin-5
    • Pagano A., Crottet P., Prescianotto-Baschong C. and Spiess M. (2004). In vitro formation of recycling vesicles from endosomes requires adaptor protein-1/clathrin and is regulated by rab4 and the connector rabaptin-5. Mol. Biol. Cell 15, 4990-5000.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4990-5000
    • Pagano, A.1    Crottet, P.2    Prescianotto-Baschong, C.3    Spiess, M.4
  • 112
    • 45549087226 scopus 로고    scopus 로고
    • Regulation of endosome dynamics by Rab5 and Huntingtin-HAP40 effector complex in physiological versus pathological conditions
    • Pal A., Severin F., Hopfner S. and Zerial M. (2008). Regulation of endosome dynamics by Rab5 and Huntingtin-HAP40 effector complex in physiological versus pathological conditions. Methods Enzymol. 438, 239-257.
    • (2008) Methods Enzymol , vol.438 , pp. 239-257
    • Pal, A.1    Severin, F.2    Hopfner, S.3    Zerial, M.4
  • 113
    • 32644434386 scopus 로고    scopus 로고
    • Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is up-regulated in Huntington's disease
    • Pal A., Severin F., Lommer B., Shevchenko A. and Zerial M. (2006). Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is up-regulated in Huntington's disease. J. Cell Biol. 172, 605-618.
    • (2006) J. Cell Biol , vol.172 , pp. 605-618
    • Pal, A.1    Severin, F.2    Lommer, B.3    Shevchenko, A.4    Zerial, M.5
  • 115
    • 74749109515 scopus 로고    scopus 로고
    • Pattni K. and Stenmark H. (2006). Protein sorting in endosomes. In: Endosomes. Dikic I. (ed). Landes Bioscience and Springer. Austin, TX. pp 76-88.
    • Pattni K. and Stenmark H. (2006). Protein sorting in endosomes. In: Endosomes. Dikic I. (ed). Landes Bioscience and Springer. Austin, TX. pp 76-88.
  • 116
    • 0037087512 scopus 로고    scopus 로고
    • Rab5a GTPase regulates fusion between pathogen-containing phagosomes and cytoplasmic organelles in human neutrophils
    • Perskvist N., Roberg K., Kulyte A. and Stendahl O. (2002). Rab5a GTPase regulates fusion between pathogen-containing phagosomes and cytoplasmic organelles in human neutrophils. J. Cell Sci. 115, 1321-1330.
    • (2002) J. Cell Sci , vol.115 , pp. 1321-1330
    • Perskvist, N.1    Roberg, K.2    Kulyte, A.3    Stendahl, O.4
  • 117
    • 0141433284 scopus 로고    scopus 로고
    • PI3P signaling regulates receptor sorting but not transport in the endosomal pathway
    • Petiot A., Faure J., Stenmark H. and Gruenberg J. (2003). PI3P signaling regulates receptor sorting but not transport in the endosomal pathway. J. Cell Biol. 162, 971-979.
    • (2003) J. Cell Biol , vol.162 , pp. 971-979
    • Petiot, A.1    Faure, J.2    Stenmark, H.3    Gruenberg, J.4
  • 118
    • 0035575616 scopus 로고    scopus 로고
    • Rab GTPases: Specifying and deciphering organelle identity and function
    • Pfeffer S.R. (2001). Rab GTPases: specifying and deciphering organelle identity and function. Trends Cell Biol. 11, 487-491.
    • (2001) Trends Cell Biol , vol.11 , pp. 487-491
    • Pfeffer, S.R.1
  • 120
    • 33748770378 scopus 로고    scopus 로고
    • Rab14 is part of the early endosomal clathrin-coated TGN microdomain
    • Proikas-Cezanne T., Gaugel A., Frickey T. and Nordheim A. (2006). Rab14 is part of the early endosomal clathrin-coated TGN microdomain. FEBS Lett. 580, 5241-5246.
    • (2006) FEBS Lett , vol.580 , pp. 5241-5246
    • Proikas-Cezanne, T.1    Gaugel, A.2    Frickey, T.3    Nordheim, A.4
  • 122
  • 123
    • 0035172729 scopus 로고    scopus 로고
    • Vps26p, a component of retromer, directs the interactions of Vps35p in endosome-to-Golgi retrieval
    • Reddy J.V. and Seaman M.N. (2001). Vps26p, a component of retromer, directs the interactions of Vps35p in endosome-to-Golgi retrieval. Mol. Biol. Cell 12, 3242-3256.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3242-3256
    • Reddy, J.V.1    Seaman, M.N.2
  • 124
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink J., Ghigo E., Kalaidzidis Y. and Zerial M. (2005). Rab conversion as a mechanism of progression from early to late endosomes. Cell 122, 735-749.
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 126
    • 33750485772 scopus 로고    scopus 로고
    • The mammalian phosphatidylinositol 3-phosphate 5-kinase (PIKfyve) regulates endosome-to-TGN retrograde transport
    • Rutherford A.C., Traer C., Wassmer T., Pattni K., Bujny M.V., Carlton J.G., Stenmark H. and Cullen P.J. (2006). The mammalian phosphatidylinositol 3-phosphate 5-kinase (PIKfyve) regulates endosome-to-TGN retrograde transport. J. Cell Sci. 119, 3944-3957.
    • (2006) J. Cell Sci , vol.119 , pp. 3944-3957
    • Rutherford, A.C.1    Traer, C.2    Wassmer, T.3    Pattni, K.4    Bujny, M.V.5    Carlton, J.G.6    Stenmark, H.7    Cullen, P.J.8
  • 127
    • 0037155216 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate-interacting domains in PIKfyve. Binding specificity and role in PIKfyve. Endomenbrane localization
    • Sbrissa D., Ikonomov O.C. and Shisheva A. (2002). Phosphatidylinositol 3-phosphate-interacting domains in PIKfyve. Binding specificity and role in PIKfyve. Endomenbrane localization. J. Biol. Chem. 277, 6073-6079.
    • (2002) J. Biol. Chem , vol.277 , pp. 6073-6079
    • Sbrissa, D.1    Ikonomov, O.C.2    Shisheva, A.3
  • 128
    • 42949092018 scopus 로고    scopus 로고
    • The endosomal protein Appl1 mediates Akt substrate specificity and cell survival in vertebrate development
    • Schenck A., Goto-Silva L., Collinet C., Rhinn M., Giner A., Habermann B., Brand M. and Zerial M. (2008). The endosomal protein Appl1 mediates Akt substrate specificity and cell survival in vertebrate development. Cell 133, 486-497.
    • (2008) Cell , vol.133 , pp. 486-497
    • Schenck, A.1    Goto-Silva, L.2    Collinet, C.3    Rhinn, M.4    Giner, A.5    Habermann, B.6    Brand, M.7    Zerial, M.8
  • 129
    • 2442509574 scopus 로고    scopus 로고
    • Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer
    • Seaman M.N. (2004). Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J. Cell Biol. 165, 111-122.
    • (2004) J. Cell Biol , vol.165 , pp. 111-122
    • Seaman, M.N.1
  • 130
    • 0031823307 scopus 로고    scopus 로고
    • A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast
    • Seaman M.N., McCaffery J.M. and Emr S.D. (1998). A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. J. Cell Biol. 142, 665-681.
    • (1998) J. Cell Biol , vol.142 , pp. 665-681
    • Seaman, M.N.1    McCaffery, J.M.2    Emr, S.D.3
  • 131
    • 43149116767 scopus 로고    scopus 로고
    • A role for EHD4 in the regulation of early endosomal transport
    • Sharma M., Naslavsky N. and Caplan S. (2008). A role for EHD4 in the regulation of early endosomal transport. Traffic 9, 995-1018.
    • (2008) Traffic , vol.9 , pp. 995-1018
    • Sharma, M.1    Naslavsky, N.2    Caplan, S.3
  • 132
    • 0033525930 scopus 로고    scopus 로고
    • The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions
    • Sheff D.R., Daro E.A., Hull M. and Mellman I. (1999a). The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions. J. Cell Biol. 145, 123-139.
    • (1999) J. Cell Biol , vol.145 , pp. 123-139
    • Sheff, D.R.1    Daro, E.A.2    Hull, M.3    Mellman, I.4
  • 133
    • 0033525930 scopus 로고    scopus 로고
    • The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions
    • Sheff D.R., Daro E.A., Hull M. and Mellman I. (1999b). The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions. J. Cell Biol. 145, 123-139.
    • (1999) J. Cell Biol , vol.145 , pp. 123-139
    • Sheff, D.R.1    Daro, E.A.2    Hull, M.3    Mellman, I.4
  • 134
  • 135
    • 43249117879 scopus 로고    scopus 로고
    • PIKfyve: Partners, significance, debates and paradoxes
    • Shisheva A. (2008). PIKfyve: Partners, significance, debates and paradoxes. Cell Biol. Int. 32, 591-604.
    • (2008) Cell Biol. Int , vol.32 , pp. 591-604
    • Shisheva, A.1
  • 136
    • 0032879685 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 interacts directly with syntaxin-6
    • Simonsen A., Gaullier J.M., D'Arrigo A. and Stenmark H. (1999). The Rab5 effector EEA1 interacts directly with syntaxin-6. J. Biol. Chem. 274, 28857-28960.
    • (1999) J. Biol. Chem , vol.274 , pp. 28857-28960
    • Simonsen, A.1    Gaullier, J.M.2    D'Arrigo, A.3    Stenmark, H.4
  • 140
    • 0029143193 scopus 로고
    • SNAREs and targeted membrane fusion
    • Sollner T. (1995). SNAREs and targeted membrane fusion. FEBS Lett. 369, 80-93.
    • (1995) FEBS Lett , vol.369 , pp. 80-93
    • Sollner, T.1
  • 141
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11
    • Sonnichsen B., De Renzis S., Nielsen E., Rietdorf J. and Zerial M. (2000). Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J. Cell Biol. 149, 901-914.
    • (2000) J. Cell Biol , vol.149 , pp. 901-914
    • Sonnichsen, B.1    De Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 142
    • 0028791634 scopus 로고
    • Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion
    • Stenmark H., Vitale G., Ullrich O. and Zerial M. (1995). Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion. Cell 83, 423-432.
    • (1995) Cell , vol.83 , pp. 423-432
    • Stenmark, H.1    Vitale, G.2    Ullrich, O.3    Zerial, M.4
  • 143
    • 34247559591 scopus 로고    scopus 로고
    • Participation of rab5, an early endosome protein, in hepatitis C virus RNA replication machinery
    • Stone M., Jia S., Heo W.D., Meyer T., and Konan K.V. (2007). Participation of rab5, an early endosome protein, in hepatitis C virus RNA replication machinery. J. Virol. 81, 4551-4563.
    • (2007) J. Virol , vol.81 , pp. 4551-4563
    • Stone, M.1    Jia, S.2    Heo, W.D.3    Meyer, T.4    Konan, K.V.5
  • 144
    • 34247143246 scopus 로고    scopus 로고
    • Grd19/Snx3p functions as a cargo-specific adapter for retromerdependent endocytic recycling
    • Strochlic T.I., Setty T.G., Sitaram A. and Burd C.G. (2007). Grd19/Snx3p functions as a cargo-specific adapter for retromerdependent endocytic recycling. J. Cell Biol. 177, 115-125.
    • (2007) J. Cell Biol , vol.177 , pp. 115-125
    • Strochlic, T.I.1    Setty, T.G.2    Sitaram, A.3    Burd, C.G.4
  • 145
    • 33746579876 scopus 로고    scopus 로고
    • Targeting the role of the endosome in the pathophysiology of Alzheimer's disease: A strategy for treatment
    • Tate B.A., and Mathews P.M. (2006). Targeting the role of the endosome in the pathophysiology of Alzheimer's disease: a strategy for treatment. Sci. Aging Knowledge Environ. 10, re2.
    • (2006) Sci. Aging Knowledge Environ , vol.10
    • Tate, B.A.1    Mathews, P.M.2
  • 146
    • 0033379104 scopus 로고    scopus 로고
    • Biochemical analysis of distinct Rab5- and Rab11-positive endosomes along the transferrin pathway
    • Trischler M., Stoorvogel W. and Ullrich O. (1999). Biochemical analysis of distinct Rab5- and Rab11-positive endosomes along the transferrin pathway. J. Cell Sci. 112, 4773-4783.
    • (1999) J. Cell Sci , vol.112 , pp. 4773-4783
    • Trischler, M.1    Stoorvogel, W.2    Ullrich, O.3
  • 147
    • 0032756658 scopus 로고    scopus 로고
    • Role of dynactin in endocytic traffic: Effects of dynamitin overexpression and colocalization with CLIP-170
    • Valetti C., Wetzel D.M., Schrader M., Hasbani M.J., Gill S.R., Kreis T.E. and Schroer T.A. (1999). Role of dynactin in endocytic traffic: effects of dynamitin overexpression and colocalization with CLIP-170. Mol. Biol. Cell 10, 4107-4120.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4107-4120
    • Valetti, C.1    Wetzel, D.M.2    Schrader, M.3    Hasbani, M.J.4    Gill, S.R.5    Kreis, T.E.6    Schroer, T.A.7
  • 148
    • 0037073739 scopus 로고    scopus 로고
    • Endocytosed transferrin receptors recycle via distinct dynamin and phosphatidylinositol 3-kinase-dependent pathways
    • van Dam E.M., Ten Broeke T., Jansen K., Spijkers P. and Stoorvogel W. (2002). Endocytosed transferrin receptors recycle via distinct dynamin and phosphatidylinositol 3-kinase-dependent pathways. J. Biol. Chem. 277, 48876-48883.
    • (2002) J. Biol. Chem , vol.277 , pp. 48876-48883
    • van Dam, E.M.1    Ten Broeke, T.2    Jansen, K.3    Spijkers, P.4    Stoorvogel, W.5
  • 149
    • 0026730464 scopus 로고
    • The small GTP-binding protein rab4 controls an early sorting event on the endocytic pathway
    • van der Sluijs P., Hull M., Webster P., Male P., Goud B. and Mellman I. (1992). The small GTP-binding protein rab4 controls an early sorting event on the endocytic pathway. Cell 70, 729-740.
    • (1992) Cell , vol.70 , pp. 729-740
    • van der Sluijs, P.1    Hull, M.2    Webster, P.3    Male, P.4    Goud, B.5    Mellman, I.6
  • 151
    • 0032055405 scopus 로고    scopus 로고
    • Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5
    • Vitale G., Rybin V., Christoforidis S., Thornqvist P., McCaffrey M., Stenmark H. and Zerial M. (1998). Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5. EMBO J. 17, 1941-1951.
    • (1998) EMBO J , vol.17 , pp. 1941-1951
    • Vitale, G.1    Rybin, V.2    Christoforidis, S.3    Thornqvist, P.4    McCaffrey, M.5    Stenmark, H.6    Zerial, M.7
  • 152
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1- benzopyran-4-one (LY294002)
    • Vlahos C.J., Matter W.F., Hui K.Y. and Brown R.F. (1994). A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1- benzopyran-4-one (LY294002). J. Biol. Chem. 269, 5241-5248.
    • (1994) J. Biol. Chem , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 153
    • 0030780582 scopus 로고    scopus 로고
    • The small guanosine triphosphate-binding protein Rab4 is involved in insulin-induced GLUT4 translocation and actin filament rearrangement in 3T3-L1 cells
    • Vollenweider P., Martin S.S., Haruta T., Morris A.J., Nelson J.G., Cormont M., Le Marchand-Brustel Y., Rose D.W. and Olefsky J.M. (1997). The small guanosine triphosphate-binding protein Rab4 is involved in insulin-induced GLUT4 translocation and actin filament rearrangement in 3T3-L1 cells. Endocrinology 138, 4941-4949.
    • (1997) Endocrinology , vol.138 , pp. 4941-4949
    • Vollenweider, P.1    Martin, S.S.2    Haruta, T.3    Morris, A.J.4    Nelson, J.G.5    Cormont, M.6    Le Marchand-Brustel, Y.7    Rose, D.W.8    Olefsky, J.M.9
  • 154
    • 0032498639 scopus 로고    scopus 로고
    • Retrieval of resident late-Golgi membrane proteins from the prevacuolar compartment of Saccharomyces cerevisiae is dependent on the function of Grd19p
    • Voos W. and Stevens T.H. (1998). Retrieval of resident late-Golgi membrane proteins from the prevacuolar compartment of Saccharomyces cerevisiae is dependent on the function of Grd19p. J. Cell Biol. 140, 577-590.
    • (1998) J. Cell Biol , vol.140 , pp. 577-590
    • Voos, W.1    Stevens, T.H.2
  • 155
    • 33846811334 scopus 로고    scopus 로고
    • A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer
    • Wassmer T., Attar N., Bujny M.V., Oakley J., Traer C.J. and Cullen P.J. (2007). A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer. J. Cell Sci. 120, 45-54.
    • (2007) J. Cell Sci , vol.120 , pp. 45-54
    • Wassmer, T.1    Attar, N.2    Bujny, M.V.3    Oakley, J.4    Traer, C.J.5    Cullen, P.J.6
  • 156
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • Zerial M. and McBride H. (2001). Rab proteins as membrane organizers. Nat. Rev. Mol. Cell Biol. 2, 107-117.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 107-117
    • Zerial, M.1    McBride, H.2
  • 157
    • 33846207952 scopus 로고    scopus 로고
    • Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies
    • Zwilling D., Cypionka A., Pohl W.H., Fasshauer D., Walla P.J., Wahl M.C. and Jahn R. (2007). Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. EMBO J. 26, 9-18.
    • (2007) EMBO J , vol.26 , pp. 9-18
    • Zwilling, D.1    Cypionka, A.2    Pohl, W.H.3    Fasshauer, D.4    Walla, P.J.5    Wahl, M.C.6    Jahn, R.7


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