메뉴 건너뛰기




Volumn 7, Issue 8, 2006, Pages 568-579

Retrograde transport from endosomes to the trans-Golgi network

Author keywords

[No Author keywords available]

Indexed keywords

ABRIN; ADAPTOR PROTEIN; BACTERIAL PROTEIN; CARBOXYPEPTIDASE D; CARRIER PROTEIN; CHITIN SYNTHASE; CHOLERA TOXIN; CLATHRIN; DYNAMIN; EPSIN; FURIN; MEMBRANE ENZYME; MEMBRANE PROTEIN; PEPTIDASE; PROCESSING PEPTIDASE; PROTEIN ACID HYDROLASE RECEPTOR; PROTEIN CATION DEPENDENT MANNOSE 6 PHOSPHATE RECEPTOR; PROTEIN CATION INDEPENDENT MANNOSE 6 PHOSPHATE RECEPTOR; PROTEIN KILLER EXPRESSION 2; PROTEIN PHOSPHOFURIN ACIDIC CLUSTER SORTING PROTEIN 1; PROTEIN SORTING NEXIN1; PROTEIN STERILE 13; PROTEIN T-SNARE AFFECTING A LATE GOLGI COMPRTMENT 1; PROTEIN TRANS GOLGI NETWORK PROTEIN OF 38KDA; PROTEIN TRANS GOLGI NETWORK PROTEIN OF 46KDA; PROTEIN VACUOLAR PROTEIN SORTING 10; RICIN; SHIGA TOXIN; SNARE PROTEIN; SYNTAXIN; UNCLASSIFIED DRUG;

EID: 33748313351     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm1985     Document Type: Review
Times cited : (537)

References (99)
  • 1
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino, J. S. & Glick, B. S. The mechanisms of vesicle budding and fusion. Cell 116, 153-166 (2004).
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 2
    • 0022975133 scopus 로고
    • The trans Golgi network: Sorting at the exit site of the Golgi complex
    • Griffiths, G. & Simons, K. The trans Golgi network: sorting at the exit site of the Golgi complex. Science 234, 438-443 (1986).
    • (1986) Science , vol.234 , pp. 438-443
    • Griffiths, G.1    Simons, K.2
  • 3
    • 20544431747 scopus 로고    scopus 로고
    • Protein sorting in the Golgi complex: Shifting paradigms
    • Rodriguez-Boulan, E. & Musch, A. Protein sorting in the Golgi complex: shifting paradigms. Biochim. Biophys. Acta 1744, 455-464 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 455-464
    • Rodriguez-Boulan, E.1    Musch, A.2
  • 4
    • 0033933026 scopus 로고    scopus 로고
    • Bi-directional trafficking between the trans-Golgi network and the endosomal/lysosomal system
    • Rohn, W. M., Rouille, Y., Waguri, S. & Hoflack, B. Bi-directional trafficking between the trans-Golgi network and the endosomal/lysosomal system. J. Cell Sci. 113, 2093-2101 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 2093-2101
    • Rohn, W.M.1    Rouille, Y.2    Waguri, S.3    Hoflack, B.4
  • 5
    • 0021955354 scopus 로고
    • Intracellular movement of cell surface receptors after endocytosis: Resialylation of asialo-transferrin receptor in human erythroleukemia cells
    • Snider, M. D. & Rogers, O. C. Intracellular movement of cell surface receptors after endocytosis: resialylation of asialo-transferrin receptor in human erythroleukemia cells. J. Cell Biol. 100, 826-834 (1985).
    • (1985) J. Cell Biol. , vol.100 , pp. 826-834
    • Snider, M.D.1    Rogers, O.C.2
  • 6
    • 20544447129 scopus 로고    scopus 로고
    • Protein transport from the late Golgi to the vacuole in the yeast Saccharomyces cerevisiae
    • Bowers, K. & Stevens, T. H. Protein transport from the late Golgi to the vacuole in the yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 1744, 438-454 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 438-454
    • Bowers, K.1    Stevens, T.H.2
  • 7
    • 0037336348 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors: New twists in the tale
    • Ghosh, P., Dahms, N. M. & Kornfeld, S. Mannose 6-phosphate receptors: new twists in the tale. Nature Rev. Mol. Cell Biol. 4, 202-212 (2003). References 6 and 7 are comprehensive reviews on the transport of acid hydrolases from the late Golgi to the vacuole in S. cerevisiae and from the TGN to lysosomes in mammalian cells, respectively.
    • (2003) Nature Rev. Mol. Cell Biol. , vol.4 , pp. 202-212
    • Ghosh, P.1    Dahms, N.M.2    Kornfeld, S.3
  • 8
    • 0033059994 scopus 로고    scopus 로고
    • Bi-cycling the furin pathway: From TGN localization to pathogen activation and embryogenesis
    • Molloy, S. S., Anderson, E. D., Jean, F. & Thomas, G. Bi-cycling the furin pathway: from TGN localization to pathogen activation and embryogenesis. Trends Cell Biol. 9, 28-35 (1999).
    • (1999) Trends Cell Biol. , vol.9 , pp. 28-35
    • Molloy, S.S.1    Anderson, E.D.2    Jean, F.3    Thomas, G.4
  • 9
    • 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. & Stevens, T. H. 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).
    • (1998) J. Cell Biol. , vol.140 , pp. 577-590
    • Voos, W.1    Stevens, T.H.2
  • 10
    • 0031956333 scopus 로고    scopus 로고
    • Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: Localization to the trans-Golgi network and recycling from the cell surface
    • Varlamov, O. & Fricker, L. D. Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: localization to the trans-Golgi network and recycling from the cell surface. J. Cell Sci. 111, 877-885 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 877-885
    • Varlamov, O.1    Fricker, L.D.2
  • 11
    • 0036199384 scopus 로고    scopus 로고
    • The yeast clathrin adaptor protein complex 1 is required for the efficient retention of a subset of late Golgi membrane proteins
    • Valdivia, R. H., Baggott, D., Chuang, J. S. & Schekman, R. W. The yeast clathrin adaptor protein complex 1 is required for the efficient retention of a subset of late Golgi membrane proteins. Dev. Cell 2, 283-294 (2002). Together with references 35 and 36, this article shows a requirement for the clathrin adaptor AP1 in the sorting of some proteins from endosomes to the TGN.
    • (2002) Dev. Cell , vol.2 , pp. 283-294
    • Valdivia, R.H.1    Baggott, D.2    Chuang, J.S.3    Schekman, R.W.4
  • 12
    • 0033984893 scopus 로고    scopus 로고
    • Specific retrieval of the exocytic SNARE Snc1p from early yeast endosomes
    • Lewis, M. J., Nichols, B. J., Prescianotto-Baschong, C., Riezman, H. & Pelham, H. R. Specific retrieval of the exocytic SNARE Snc1p from early yeast endosomes. Mol. Biol. Cell 11, 23-38 (2000). Together with reference 32, this paper describes the molecular machinery that is involved in the recycling of the SNAREs Snc1 and Pep12 from endosomes to the late Golgi complex in S. cerevisiae.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 23-38
    • Lewis, M.J.1    Nichols, B.J.2    Prescianotto-Baschong, C.3    Riezman, H.4    Pelham, H.R.5
  • 13
    • 20444407298 scopus 로고    scopus 로고
    • SNAREs and traffic
    • Hong, W. SNAREs and traffic. Biochim. Biophys. Acta 1744, 493-517 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 493-517
    • Hong, W.1
  • 14
    • 4344599512 scopus 로고    scopus 로고
    • Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport from the early/recycling endosome to the trans-Golgi network
    • Tai, G. et al. Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport from the early/recycling endosome to the trans-Golgi network. Mol. Biol. Cell 15, 4011-4022 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4011-4022
    • Tai, G.1
  • 15
    • 0037128205 scopus 로고    scopus 로고
    • Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform
    • Mallard, F. et al. Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform. J. Cell Biol. 156, 653-664 (2002). References 14 and 15 describe two SNARE complexes that are involved in the fusion of endosome-derived retrograde carriers with the TGN.
    • (2002) J. Cell Biol. , vol.156 , pp. 653-664
    • Mallard, F.1
  • 16
    • 20744450629 scopus 로고    scopus 로고
    • Delivery into cells: Lessons learned from plant and bacterial toxins
    • Sandvig, K. & van Deurs, B. Delivery into cells: lessons learned from plant and bacterial toxins. Gene Ther. 12, 865-872 (2005). This article reviews how exotoxins exploit the cell's trafficking machinery to gain access to the cell.
    • (2005) Gene Ther. , vol.12 , pp. 865-872
    • Sandvig, K.1    Van Deurs, B.2
  • 17
    • 13244275069 scopus 로고    scopus 로고
    • Recycle your receptors with retromer
    • Seaman, M. N. Recycle your receptors with retromer. Trends Cell Biol. 15, 68-75 (2005). A comprehensive review on the structure and function of the S. cerevisiae and mammalian retromer complexes.
    • (2005) Trends Cell Biol. , vol.15 , pp. 68-75
    • Seaman, M.N.1
  • 18
    • 0033634771 scopus 로고    scopus 로고
    • Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: Assembly into multimeric complexes
    • Haft, C. R. et al. Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes. Mol. Biol. Cell 11, 4105-4116 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4105-4116
    • Haft, C.R.1
  • 19
    • 26944480746 scopus 로고    scopus 로고
    • A novel mammalian retromer component, Vps26B
    • Kerr, M. C. et al. A novel mammalian retromer component, Vps26B. Traffic 6, 991-1001 (2005).
    • (2005) Traffic , vol.6 , pp. 991-1001
    • Kerr, M.C.1
  • 20
    • 12744281102 scopus 로고    scopus 로고
    • Sorting nexins - Unifying trends and new perspectives
    • Carlton, J., Bujny, M., Rutherford, A. & Cullen, P. Sorting nexins - unifying trends and new perspectives. Traffic 6, 75-82 (2005).
    • (2005) Traffic , vol.6 , pp. 75-82
    • Carlton, J.1    Bujny, M.2    Rutherford, A.3    Cullen, P.4
  • 21
    • 33744943284 scopus 로고    scopus 로고
    • Human Vps26 has an arrestin fold and is integrated into the retromer complex through its C-terminal domain
    • Shi, H., Rojas, R., Bonifacino, J. S. & Hurley, J. H. Human Vps26 has an arrestin fold and is integrated into the retromer complex through its C-terminal domain. Nature Struct. Mol. Biol. 13, 540-548 (2006). X-ray crystallography reveals an unexpected structural homology of the VPS26 subunit of mammalian retromer to arrestins.
    • (2006) Nature Struct. Mol. Biol. , vol.13 , pp. 540-548
    • Shi, H.1    Rojas, R.2    Bonifacino, J.S.3    Hurley, J.H.4
  • 22
    • 22144490854 scopus 로고    scopus 로고
    • Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly
    • Collins, B. M., Skinner, C. F., Watson, P. J., Seaman, M. N. & Owen, D. J. Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly. Nature Struct. Mol. Biol. 12, 594-602 (2005).
    • (2005) Nature Struct. Mol. Biol. , vol.12 , pp. 594-602
    • Collins, B.M.1    Skinner, C.F.2    Watson, P.J.3    Seaman, M.N.4    Owen, D.J.5
  • 23
    • 20744460043 scopus 로고    scopus 로고
    • Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites
    • Wang, D. et al. Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites. J. Biol. Chem. 280, 22962-22967 (2005). References 22 and 23 report that the VPS29 subunit of mammalian retromer has structural homology to divalent-metal-containing phosphoesterases.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22962-22967
    • Wang, D.1
  • 24
    • 2442530398 scopus 로고    scopus 로고
    • Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor
    • Arighi, C. N., Hartnell, L. M., Aguilar, R. C., Haft, C. R. & Bonifacino, J. S. Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor. J. Cell Biol. 165, 123-133 (2004).
    • (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
  • 25
    • 2442509574 scopus 로고    scopus 로고
    • Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer
    • Seaman, M. N. Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J. Cell Biol. 165, 111-122 (2004).
    • (2004) J. Cell Biol. , vol.165 , pp. 111-122
    • Seaman, M.N.1
  • 26
    • 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. et al. 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). References 24-26 report that the mammalian retromer complex mediates the sorting of MPRs from endosomes to the TGN.
    • (2004) Curr. Biol. , vol.14 , pp. 1791-1800
    • Carlton, J.1
  • 27
    • 0035911146 scopus 로고    scopus 로고
    • Distinct protein sorting and localization to premelanosomes, melanosomes, and lysosomes in pigmented melanocytic cells
    • Raposo, G., Tenza, D., Murphy, D. M., Berson, J. F. & Marks, M. S. Distinct protein sorting and localization to premelanosomes, melanosomes, and lysosomes in pigmented melanocytic cells. J. Cell Biol. 152, 809-824 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 809-824
    • Raposo, G.1    Tenza, D.2    Murphy, D.M.3    Berson, J.F.4    Marks, M.S.5
  • 28
    • 1842509099 scopus 로고    scopus 로고
    • Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins
    • Peden, A. A. et al. Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins. J. Cell Biol. 164, 1065-1076 (2004).
    • (2004) J. Cell Biol. , vol.164 , pp. 1065-1076
    • Peden, A.A.1
  • 29
    • 27744576858 scopus 로고    scopus 로고
    • Model-guided microarray implicates the retromer complex in Alzheimer's disease
    • Small, S. A. et al. Model-guided microarray implicates the retromer complex in Alzheimer's disease. Ann. Neurol. 58, 909-919 (2005). Decreased levels of retromer are linked to the development of Alzheimer's disease.
    • (2005) Ann. Neurol. , vol.58 , pp. 909-919
    • Small, S.A.1
  • 30
    • 1442264828 scopus 로고    scopus 로고
    • Take five - BACE and the γ-secretase quartet conduct Alzheimer's amyloid β-peptide generation
    • Haass, C. Take five - BACE and the γ-secretase quartet conduct Alzheimer's amyloid β-peptide generation. EMBO J. 23, 483-488 (2004).
    • (2004) EMBO J. , vol.23 , pp. 483-488
    • Haass, C.1
  • 31
    • 33748311050 scopus 로고    scopus 로고
    • The gene hunters
    • 12 December
    • Halpern, S. The gene hunters. The New Yorker, 84-93 (12 December 2005).
    • (2005) The New Yorker , pp. 84-93
    • Halpern, S.1
  • 32
    • 0037415752 scopus 로고    scopus 로고
    • Retromer and the sorting nexins Snx4/41/42 mediate distinct retrieval pathways from yeast endosomes
    • Hettema, E. H., Lewis, M. J., Black, M. W. & Pelham, H. R. Retromer and the sorting nexins Snx4/41/42 mediate distinct retrieval pathways from yeast endosomes. EMBO J. 22, 548-557 (2003).
    • (2003) EMBO J. , vol.22 , pp. 548-557
    • Hettema, E.H.1    Lewis, M.J.2    Black, M.W.3    Pelham, H.R.4
  • 33
    • 0032563306 scopus 로고    scopus 로고
    • PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization
    • Wan, L. et al. PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization. Cell 94, 205-216 (1998).
    • (1998) Cell , vol.94 , pp. 205-216
    • Wan, L.1
  • 34
    • 0035341464 scopus 로고    scopus 로고
    • PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic
    • Crump, C. M. et al. PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic. EMBO J. 20, 2191-2201 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2191-2201
    • Crump, C.M.1
  • 35
    • 0034657033 scopus 로고    scopus 로고
    • μ1A-adaptin-deficient mice: Lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors
    • Meyer, C. et al. μ1A-adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors. EMBO J. 19, 2193-2203 (2000).
    • (2000) EMBO J. , vol.19 , pp. 2193-2203
    • Meyer, C.1
  • 36
    • 0242363236 scopus 로고    scopus 로고
    • Characterization of the in vitro retrograde transport of MPR46
    • Medigeshi, G. R. & Schu, P. Characterization of the in vitro retrograde transport of MPR46. Traffic 4, 802-811 (2003).
    • (2003) Traffic , vol.4 , pp. 802-811
    • Medigeshi, G.R.1    Schu, P.2
  • 37
    • 11144357792 scopus 로고    scopus 로고
    • Clathrin adaptor epsinR is required for retrograde sorting on early endosomal membranes
    • Saint-Pol, A. et al. Clathrin adaptor epsinR is required for retrograde sorting on early endosomal membranes. Dev. Cell 6, 525-538 (2004). Clathrin and epsinR are implicated in the retrograde transport of Shiga toxin, TGN38, TGN46 and MPRs from endosomes to the TGN.
    • (2004) Dev. Cell , vol.6 , pp. 525-538
    • Saint-Pol, A.1
  • 38
    • 0027398577 scopus 로고
    • Rab9 functions in transport between late endosomes and the trans Golgi network
    • Lombardi, D. et al. Rab9 functions in transport between late endosomes and the trans Golgi network. EMBO J. 12, 677-682 (1993).
    • (1993) EMBO J. , vol.12 , pp. 677-682
    • Lombardi, D.1
  • 39
    • 0032076636 scopus 로고    scopus 로고
    • TIP47: A cargo selection device for mannose 6-phosphate receptor trafficking
    • Diaz, E. & Pfeffer, S. R. TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking. Cell 93, 433-443 (1998).
    • (1998) Cell , vol.93 , pp. 433-443
    • Diaz, E.1    Pfeffer, S.R.2
  • 40
    • 0037017395 scopus 로고    scopus 로고
    • Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells
    • Barbero, P., Bittova, L. & Pfeffer, S. R. Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells. J. Cell Biol. 156, 511-518 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 511-518
    • Barbero, P.1    Bittova, L.2    Pfeffer, S.R.3
  • 41
    • 0028224561 scopus 로고
    • Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network
    • Riederer, M. A., Soldati, T., Shapiro, A. D., Lin, J. & Pfeffer, S. R. Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans-Golgi network. J. Cell Biol. 125, 573-582 (1994).
    • (1994) J. Cell Biol. , vol.125 , pp. 573-582
    • Riederer, M.A.1    Soldati, T.2    Shapiro, A.D.3    Lin, J.4    Pfeffer, S.R.5
  • 42
    • 0035906951 scopus 로고    scopus 로고
    • Role of Rab9 GTPase in facilitating receptor recruitment by TIP47
    • Carroll, K. S. et al. Role of Rab9 GTPase in facilitating receptor recruitment by TIP47. Science 292, 1373-1376 (2001).
    • (2001) Science , vol.292 , pp. 1373-1376
    • Carroll, K.S.1
  • 43
    • 3142640798 scopus 로고    scopus 로고
    • Structure of a lipid droplet protein; the PAT family member TIP47
    • Hickenbottom, S. J., Kimmel, A. R., Londos, C. & Hurley, J. H. Structure of a lipid droplet protein; the PAT family member TIP47. Structure 12, 1199-1207 (2004).
    • (2004) Structure , vol.12 , pp. 1199-1207
    • Hickenbottom, S.J.1    Kimmel, A.R.2    Londos, C.3    Hurley, J.H.4
  • 44
    • 0035895982 scopus 로고    scopus 로고
    • TIP47 associates with lipid droplets
    • Wolins, N. E., Rubin, B. & Brasaemle, D. L. TIP47 associates with lipid droplets. J. Biol. Chem. 276, 5101-5108 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 5101-5108
    • Wolins, N.E.1    Rubin, B.2    Brasaemle, D.L.3
  • 45
    • 0032538927 scopus 로고    scopus 로고
    • Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of Shiga toxin B-fragment transport
    • Mallard, F. et al. Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of Shiga toxin B-fragment transport. J. Cell Biol. 143, 973-990 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 973-990
    • Mallard, F.1
  • 46
    • 0035150144 scopus 로고    scopus 로고
    • Endosome to Golgi transport of ricin is independent of clathrin and of the Rab9- And Rab11-GTPases
    • Iversen, T. G. et al. Endosome to Golgi transport of ricin is independent of clathrin and of the Rab9- and Rab11-GTPases. Mol. Biol. Cell 12, 2099-2107 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2099-2107
    • Iversen, T.G.1
  • 47
    • 3042639390 scopus 로고    scopus 로고
    • Efficient endosome-to-Golgi transport of Shiga toxin is dependent on dynamin and clathrin
    • Lauvrak, S. U., Torgersen, M. L. & Sandvig, K. Efficient endosome-to-Golgi transport of Shiga toxin is dependent on dynamin and clathrin. J. Cell Sci. 117, 2321-2331 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 2321-2331
    • Lauvrak, S.U.1    Torgersen, M.L.2    Sandvig, K.3
  • 48
    • 0033634889 scopus 로고    scopus 로고
    • Endosome to Golgi transport of ricin is regulated by cholesterol
    • Grimmer, S., Iversen, T. G., van Deurs, B. & Sandvig, K. Endosome to Golgi transport of ricin is regulated by cholesterol. Mol. Biol. Cell 11, 4205-4216 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4205-4216
    • Grimmer, S.1    Iversen, T.G.2    Van Deurs, B.3    Sandvig, K.4
  • 49
    • 0035168061 scopus 로고    scopus 로고
    • Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes
    • Falguieres, T. et al. Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes. Mol. Biol. Cell 12, 2453-2468 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2453-2468
    • Falguieres, T.1
  • 50
    • 0029670903 scopus 로고    scopus 로고
    • 34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting
    • 34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting. J. Cell Biol. 132, 577-584 (1996).
    • (1996) J. Cell Biol. , vol.132 , pp. 577-584
    • Schweizer, A.1    Kornfeld, S.2    Rohrer, J.3
  • 51
    • 33644816187 scopus 로고    scopus 로고
    • Role of tethering factors in secretory membrane traffic
    • Sztul, E. & Lupashin, V. Role of tethering factors in secretory membrane traffic. Am. J. Physiol. Cell Physiol. 290, C11-C26 (2006). This review, as well as references 52-54 and 56-60, describe the properties of proteins that mediate the tethering of endosome-derived carriers to the TGN.
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290
    • Sztul, E.1    Lupashin, V.2
  • 52
    • 0033972955 scopus 로고    scopus 로고
    • Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi
    • Conibear, E. & Stevens, T. H. Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi. Mol. Biol. Cell 11, 305-323 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 305-323
    • Conibear, E.1    Stevens, T.H.2
  • 53
    • 0035503740 scopus 로고    scopus 로고
    • An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes
    • Siniossoglou, S. & Pelham, H. R. An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes. EMBO J. 20, 5991-5998 (2001).
    • (2001) EMBO J. , vol.20 , pp. 5991-5998
    • Siniossoglou, S.1    Pelham, H.R.2
  • 54
    • 0013468039 scopus 로고    scopus 로고
    • Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p
    • Conibear, E., Cleck, J. N. & Stevens, T. H. Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p. Mol. Biol. Cell 14, 1610-1623 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1610-1623
    • Conibear, E.1    Cleck, J.N.2    Stevens, T.H.3
  • 55
    • 0037428439 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments
    • Luo, Z. & Gallwitz, D. Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments. J. Biol. Chem. 278, 791-799 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 791-799
    • Luo, Z.1    Gallwitz, D.2
  • 57
    • 28544431984 scopus 로고    scopus 로고
    • Mutants in trs120 disrupt traffic from the early endosome to the late Golgi
    • Cai, H., Zhang, Y., Pypaert, M., Walker, L. & Ferro-Novick, S. Mutants in trs120 disrupt traffic from the early endosome to the late Golgi. J. Cell Biol. 171, 823-833 (2005).
    • (2005) J. Cell Biol. , vol.171 , pp. 823-833
    • Cai, H.1    Zhang, Y.2    Pypaert, M.3    Walker, L.4    Ferro-Novick, S.5
  • 58
    • 0032948290 scopus 로고    scopus 로고
    • Structural and functional analysis of a novel coiled-coil protein involved in Ypt6 GTPase-regulated protein transport in yeast
    • Tsukada, M., Will, E. & Gallwitz, D. Structural and functional analysis of a novel coiled-coil protein involved in Ypt6 GTPase-regulated protein transport in yeast. Mol. Biol. Cell 10, 63-75 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 63-75
    • Tsukada, M.1    Will, E.2    Gallwitz, D.3
  • 59
    • 21044446690 scopus 로고    scopus 로고
    • TGolgin-1 (p230, golgin-245) modulates Shiga-toxin transport to the Golgi and Golgi motility towards the microtubule-organizing centre
    • Yoshino, A. et al. tGolgin-1 (p230, golgin-245) modulates Shiga-toxin transport to the Golgi and Golgi motility towards the microtubule-organizing centre. J. Cell Sci. 118, 2279-2293 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 2279-2293
    • Yoshino, A.1
  • 60
    • 4644352428 scopus 로고    scopus 로고
    • Autoantigen Golgin-97, an effector of Arl1 GTPase, participates in traffic from the endosome to the trans-Golgi network
    • Lu, L., Tai, G. & Hong, W. Autoantigen Golgin-97, an effector of Arl1 GTPase, participates in traffic from the endosome to the trans-Golgi network. Mol. Biol. Cell 15, 4426-4443 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4426-4443
    • Lu, L.1    Tai, G.2    Hong, W.3
  • 61
    • 0037418595 scopus 로고    scopus 로고
    • The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus
    • Panic, B., Whyte, J. R. & Munro, S. The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus. Curr. Biol. 13, 405-410 (2003). References 61, 62, 64 and 96 describe the mechanism of recruitment and interaction with tethering factors for the Arl1 and Arl3 GTPases at the TGN.
    • (2003) Curr. Biol. , vol.13 , pp. 405-410
    • Panic, B.1    Whyte, J.R.2    Munro, S.3
  • 62
    • 2342497804 scopus 로고    scopus 로고
    • Golgi targeting of ARF-like GTPase Arl3p requires its Nα-acetylation and the integral membrane protein Sys1p
    • Setty, S. R., Strochlic, T. I., Tong, A. H., Boone, C. & Burd, C. G. Golgi targeting of ARF-like GTPase Arl3p requires its Nα-acetylation and the integral membrane protein Sys1p. Nature Cell Biol. 6, 414-419 (2004).
    • (2004) Nature Cell Biol. , vol.6 , pp. 414-419
    • Setty, S.R.1    Strochlic, T.I.2    Tong, A.H.3    Boone, C.4    Burd, C.G.5
  • 63
    • 0036320668 scopus 로고    scopus 로고
    • Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae
    • Bonangelino, C. J., Chavez, E. M. & Bonifacino, J. S. Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol. Biol. Cell 13, 2486-2501 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2486-2501
    • Bonangelino, C.J.1    Chavez, E.M.2    Bonifacino, J.S.3
  • 64
    • 26244468567 scopus 로고    scopus 로고
    • Roles of ARFRP1 (ADP-ribosylation factor-related protein 1) in post-Golgi membrane trafficking
    • Shin, H. W. et al. Roles of ARFRP1 (ADP-ribosylation factor-related protein 1) in post-Golgi membrane trafficking. J. Cell Sci. 118, 4039-4048 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 4039-4048
    • Shin, H.W.1
  • 65
    • 0032472324 scopus 로고    scopus 로고
    • Two syntaxin homologues in the TGN/endosomal system of yeast
    • Holthuis, J. C., Nichols, B. J., Dhruvakumar, S. & Pelham, H. R. Two syntaxin homologues in the TGN/endosomal system of yeast. EMBO J. 17, 113-126 (1998).
    • (1998) EMBO J. , vol.17 , pp. 113-126
    • Holthuis, J.C.1    Nichols, B.J.2    Dhruvakumar, S.3    Pelham, H.R.4
  • 67
    • 0036059819 scopus 로고    scopus 로고
    • Mosaic organization of the endocytic pathway
    • Miaczynska, M. & Zerial, M. Mosaic organization of the endocytic pathway. Exp. Cell Res. 272, 8-14 (2002).
    • (2002) Exp. Cell Res. , vol.272 , pp. 8-14
    • Miaczynska, M.1    Zerial, M.2
  • 69
    • 0018958518 scopus 로고
    • The galactosespecific recognition system of mammalian liver: The route of ligand internalization in rat hepatocytes
    • Wall, D. A., Wilson, G. & Hubbard, A. L. The galactosespecific recognition system of mammalian liver: the route of ligand internalization in rat hepatocytes. Cell 21, 79-93 (1980).
    • (1980) Cell , vol.21 , pp. 79-93
    • Wall, D.A.1    Wilson, G.2    Hubbard, A.L.3
  • 70
    • 0345349786 scopus 로고
    • Morphologic characterization of the pathway of transferrin endocytosis and recycling in human KB cells
    • Willingham, M. C., Hanover, J. A., Dickson, R. B. & Pastan, I. Morphologic characterization of the pathway of transferrin endocytosis and recycling in human KB cells. Proc. Natl Acad. Sci. USA 81, 175-179 (1984).
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 175-179
    • Willingham, M.C.1    Hanover, J.A.2    Dickson, R.B.3    Pastan, I.4
  • 73
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: Structure and mechanism of a membrane-trafficking network
    • Hurley, J. H. & Emr, S. D. The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Annu. Rev. Biophys. Biomol. Struct. 35, 277-298 (2006).
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 74
    • 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. et al. 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).
    • (2002) EMBO J. , vol.21 , pp. 2557-2567
    • Caplan, S.1
  • 75
    • 27644512056 scopus 로고    scopus 로고
    • Sorting nexin-2 is associated with tubular elements of the early endosome, but is not essential for retromer-mediated endosome-to-TGN transport
    • Carlton, J. G. et al. Sorting nexin-2 is associated with tubular elements of the early endosome, but is not essential for retromer-mediated endosome-to-TGN transport. J. Cell Sci. 118, 4527-4539 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 4527-4539
    • Carlton, J.G.1
  • 76
    • 17944367436 scopus 로고    scopus 로고
    • The crystal structure of the PX domain from p40phox bound to phosphatidylinositol 3-phosphate
    • Bravo, J. et al. The crystal structure of the PX domain from p40phox bound to phosphatidylinositol 3-phosphate. Mol Cell. 8, 829-839 (2001).
    • (2001) Mol Cell. , vol.8 , pp. 829-839
    • Bravo, J.1
  • 77
    • 1442317538 scopus 로고    scopus 로고
    • BAR domains as sensors of membrane curvature: The amphiphysin BAR structure
    • Peter, B. J. et al. BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science 303, 495-499 (2004).
    • (2004) Science , vol.303 , pp. 495-499
    • Peter, B.J.1
  • 78
    • 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. et al. 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).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1529-1541
    • Horazdovsky, B.F.1
  • 79
    • 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. & Bruinsma, P. 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).
    • (2000) J. Cell Biol. , vol.151 , pp. 297-310
    • Nothwehr, S.F.1    Ha, S.A.2    Bruinsma, P.3
  • 80
    • 0031823307 scopus 로고    scopus 로고
    • A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast
    • Seaman, M. N., McCaffery, J. M. & Emr, S. D. A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. J. Cell Biol. 142, 665-681 (1998). A landmark paper that first characterized the retromer complex.
    • (1998) J. Cell Biol. , vol.142 , pp. 665-681
    • Seaman, M.N.1    McCaffery, J.M.2    Emr, S.D.3
  • 81
    • 27644555189 scopus 로고    scopus 로고
    • Functions of adaptor protein (AP)-3 and AP-1 in tyrosinase sorting from endosomes to melanosomes
    • Theos, A. C. et al. Functions of adaptor protein (AP)-3 and AP-1 in tyrosinase sorting from endosomes to melanosomes. Mol. Biol. Cell 16, 5356-5372 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5356-5372
    • Theos, A.C.1
  • 82
    • 4143090605 scopus 로고    scopus 로고
    • The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor
    • Verges, M. et al. The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor. Nature Cell Biol. 6, 763-769 (2004).
    • (2004) Nature Cell Biol. , vol.6 , pp. 763-769
    • Verges, M.1
  • 83
    • 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. & Spiess, M. 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).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4990-5000
    • Pagano, A.1    Crottet, P.2    Prescianotto-Baschong, C.3    Spiess, M.4
  • 84
    • 0032692619 scopus 로고    scopus 로고
    • A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells
    • Fölsch, H., Ohno, H., Bonifacino, J. S. & Mellman, I. A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. Cell 99, 189-198 (1999).
    • (1999) Cell , vol.99 , pp. 189-198
    • Fölsch, H.1    Ohno, H.2    Bonifacino, J.S.3    Mellman, I.4
  • 85
    • 0036045770 scopus 로고    scopus 로고
    • The epithelial-specific adaptor AP1B mediates postendocytic recycling to the basolateral membrane
    • Gan, Y., McGraw, T. E. & Rodriguez-Boulan, E. The epithelial-specific adaptor AP1B mediates postendocytic recycling to the basolateral membrane. Nature Cell Biol. 4, 605-609 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 605-609
    • Gan, Y.1    McGraw, T.E.2    Rodriguez-Boulan, E.3
  • 86
    • 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. & Maxfield, F. R. Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells. Nature Cell Biol. 3, 567-572 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 567-572
    • Lin, S.X.1    Grant, B.2    Hirsh, D.3    Maxfield, F.R.4
  • 87
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich, O., Reinsch, S., Urbe, S., Zerial, M. & Parton, R. G. Rab11 regulates recycling through the pericentriolar recycling endosome. J. Cell Biol. 135, 913-924 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 88
    • 28544450844 scopus 로고    scopus 로고
    • Glucose transporter 4: Cycling, compartments and controversies
    • Dugani, C. B. & Klip, A. Glucose transporter 4: cycling, compartments and controversies. EMBO Rep. 6, 1137-1142 (2005).
    • (2005) EMBO Rep. , vol.6 , pp. 1137-1142
    • Dugani, C.B.1    Klip, A.2
  • 89
    • 0028332917 scopus 로고
    • The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene
    • Marcusson, E. G., Horazdovsky, B. F., Cereghino, J. L., Gharakhanian, E. & Emr, S. D. The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene. Cell 77, 579-586 (1994).
    • (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
  • 90
    • 0031055434 scopus 로고    scopus 로고
    • Two separate signals act independently to localize a yeast late Golgi membrane protein through a combination of retrieval and retention
    • Bryant, N. J. & Stevens, T. H. Two separate signals act independently to localize a yeast late Golgi membrane protein through a combination of retrieval and retention. J. Cell Biol. 136, 287-297 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 287-297
    • Bryant, N.J.1    Stevens, T.H.2
  • 91
    • 0027178838 scopus 로고
    • TGN38/41: A molecule on the move
    • Stanley, K. K. & Howell, K. E. TGN38/41: a molecule on the move. Trends Cell Biol. 3, 252-255 (1993).
    • (1993) Trends Cell Biol. , vol.3 , pp. 252-255
    • Stanley, K.K.1    Howell, K.E.2
  • 92
    • 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. & Emr, S. D. Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase. J. Cell Sci. 115, 3889-3900 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 3889-3900
    • Burda, P.1    Padilla, S.M.2    Sarkar, S.3    Emr, S.D.4
  • 93
    • 23044490771 scopus 로고    scopus 로고
    • Lowe syndrome protein OCRL1 interacts with clathrin and regulates protein trafficking between endosomes and the trans-Golgi network
    • Choudhury, R. et al. Lowe syndrome protein OCRL1 interacts with clathrin and regulates protein trafficking between endosomes and the trans-Golgi network. Mol. Biol. Cell 16, 3467-3479 (2005). References 92 and 93 implicate phosphoinositidemetabolizing enzymes in the regulation of retrograde transport.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3467-3479
    • Choudhury, R.1
  • 94
    • 0029904263 scopus 로고    scopus 로고
    • Mutation of the Rab6 homologue of Saccharomyces cerevisiae, YPT6, inhibits both early Golgi function and ribosome biosynthesis
    • Li, B. & Warner, J. R. Mutation of the Rab6 homologue of Saccharomyces cerevisiae, YPT6, inhibits both early Golgi function and ribosome biosynthesis. J. Biol. Chem. 271, 16813-16819 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 16813-16819
    • Li, B.1    Warner, J.R.2
  • 95
    • 0034665261 scopus 로고    scopus 로고
    • Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p
    • Siniossoglou, S., Peak-Chew, S. Y. & Pelham, H. R. Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p. EMBO J. 19, 4885-4894 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4885-4894
    • Siniossoglou, S.1    Peak-Chew, S.Y.2    Pelham, H.R.3
  • 96
    • 23844460551 scopus 로고    scopus 로고
    • The Arf-like GTPase Arl1 and its role in membrane traffic
    • Munro, S. The Arf-like GTPase Arl1 and its role in membrane traffic. Biochem. Soc. Trans. 33, 601-605 (2005).
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 601-605
    • Munro, S.1
  • 97
    • 0032734240 scopus 로고    scopus 로고
    • The yeast GRD20 gene is required for protein sorting in the trans-Golgi network/endosomal system and for polarization of the actin cytoskeleton
    • Spelbrink, R. G. & Nothwehr, S. F. The yeast GRD20 gene is required for protein sorting in the trans-Golgi network/endosomal system and for polarization of the actin cytoskeleton. Mol. Biol. Cell 10, 4263-4281 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4263-4281
    • Spelbrink, R.G.1    Nothwehr, S.F.2
  • 98
    • 0030736629 scopus 로고    scopus 로고
    • A novel assay reveals a role for soluble N-ethylmaleimide-sensitive fusion attachment protein in mannose 6-phosphate receptor transport from endosomes to the trans Golgi network
    • Itin, C., Rancano, C., Nakajima, Y. & Pfeffer, S. R. A novel assay reveals a role for soluble N-ethylmaleimide-sensitive fusion attachment protein in mannose 6-phosphate receptor transport from endosomes to the trans Golgi network. J. Biol. Chem. 272, 27737-27744 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 27737-27744
    • Itin, C.1    Rancano, C.2    Nakajima, Y.3    Pfeffer, S.R.4
  • 99
    • 14744272136 scopus 로고    scopus 로고
    • Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells
    • Zolov, S. N. & Lupashin, V. V. Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells. J. Cell Biol. 168, 747-759 (2005).
    • (2005) J. Cell Biol. , vol.168 , pp. 747-759
    • Zolov, S.N.1    Lupashin, V.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.