-
1
-
-
0032538927
-
Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of Shiga toxin B-fragment transport
-
Mallard F., Antony C., Tenza D., Salamero J., Goud B., Johannes L. Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of Shiga toxin B-fragment transport. J. Cell Biol. 143:1998;973-990.
-
(1998)
J. Cell Biol.
, vol.143
, pp. 973-990
-
-
Mallard, F.1
Antony, C.2
Tenza, D.3
Salamero, J.4
Goud, B.5
Johannes, L.6
-
2
-
-
0037017395
-
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. 156:2002;511-518.
-
(2002)
J. Cell Biol.
, vol.156
, pp. 511-518
-
-
Barbero, P.1
Bittova, L.2
Pfeffer, S.R.3
-
3
-
-
0035906951
-
Role of Rab9 GTPase in facilitating receptor recruitment by TIP47
-
Carroll K.S., Hanna J., Simon I., Krise J., Barbero P., Pfeffer S.R. Role of Rab9 GTPase in facilitating receptor recruitment by TIP47. Science. 292:2001;1373-1376.
-
(2001)
Science
, vol.292
, pp. 1373-1376
-
-
Carroll, K.S.1
Hanna, J.2
Simon, I.3
Krise, J.4
Barbero, P.5
Pfeffer, S.R.6
-
4
-
-
0033606772
-
Chimeric forms of furin and TGN38 are transported from the plasma membrane to the trans-Golgi network via distinct endosomal pathways
-
Mallet W.G., Maxfield F.R. Chimeric forms of furin and TGN38 are transported from the plasma membrane to the trans-Golgi network via distinct endosomal pathways. J. Cell Biol. 146:1999;345-359.
-
(1999)
J. Cell Biol.
, vol.146
, pp. 345-359
-
-
Mallet, W.G.1
Maxfield, F.R.2
-
5
-
-
0035341464
-
PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic
-
Crump C.M., Xiang Y., Thomas L., Gu F., Austin C., Tooze S.A., Thomas G. PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic. EMBO J. 20:2001;2191-2201.
-
(2001)
EMBO J.
, vol.20
, pp. 2191-2201
-
-
Crump, C.M.1
Xiang, Y.2
Thomas, L.3
Gu, F.4
Austin, C.5
Tooze, S.A.6
Thomas, G.7
-
6
-
-
0034682804
-
Quantitative analysis of TIP47 (tail-interacting protein of 47 kDa)-receptor cytoplasmic domain interactions: Implications for endosome-to-trans-Golgi network trafficking
-
Krise J.P., Sincock P.M., Orsel J.G., Pfeffer S.R. Quantitative analysis of TIP47 (tail-interacting protein of 47 kDa)-receptor cytoplasmic domain interactions: implications for endosome-to-trans-Golgi network trafficking. J. Biol. Chem. 275:2000;25188-25193.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 25188-25193
-
-
Krise, J.P.1
Sincock, P.M.2
Orsel, J.G.3
Pfeffer, S.R.4
-
7
-
-
0036862775
-
Characterisation of the lumenal domain of TGN38 and effects of elevated expression of TGN38 on glycoprotein secretion
-
Lee S.S., Banting G. Characterisation of the lumenal domain of TGN38 and effects of elevated expression of TGN38 on glycoprotein secretion. Eur. J. Cell Biol. 81:2002;609-621.
-
(2002)
Eur. J. Cell Biol.
, vol.81
, pp. 609-621
-
-
Lee, S.S.1
Banting, G.2
-
8
-
-
0032563568
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An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells
-
Ghosh R.N., Mallet W.G., Soe T.T., McGraw T.E., Maxfield F.R. An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells. J. Cell Biol. 142:1998;923-936.
-
(1998)
J. Cell Biol.
, vol.142
, pp. 923-936
-
-
Ghosh, R.N.1
Mallet, W.G.2
Soe, T.T.3
McGraw, T.E.4
Maxfield, F.R.5
-
9
-
-
0034657033
-
μ1A-adaptin-deficient mice: Lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors
-
Meyer C., Zizioli D., Lausmann S., Eskelinen E.L., Hamann J., Saftig P., von Figura K., Schu P. μ1A-adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors. EMBO J. 19:2000;2193-2203.
-
(2000)
EMBO J.
, vol.19
, pp. 2193-2203
-
-
Meyer, C.1
Zizioli, D.2
Lausmann, S.3
Eskelinen, E.L.4
Hamann, J.5
Saftig, P.6
Von Figura, K.7
Schu, P.8
-
10
-
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0035168061
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Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes
-
Falguieres T., Mallard F., Baron C., Hanau D., Lingwood C., Goud B., Salamero J., Johannes L. Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes. Mol. Biol. Cell. 12:2001;2453-2468.
-
(2001)
Mol. Biol. Cell
, vol.12
, pp. 2453-2468
-
-
Falguieres, T.1
Mallard, F.2
Baron, C.3
Hanau, D.4
Lingwood, C.5
Goud, B.6
Salamero, J.7
Johannes, L.8
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11
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0034638828
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Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-Golgi network
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Wilcke M., Johannes L., Galli T., Mayau V., Goud B., Salamero J. Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-Golgi network. J. Cell Biol. 151:2000;1207-1220.
-
(2000)
J. Cell Biol.
, vol.151
, pp. 1207-1220
-
-
Wilcke, M.1
Johannes, L.2
Galli, T.3
Mayau, V.4
Goud, B.5
Salamero, J.6
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12
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0037128205
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Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform
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This paper identifies components of the molecular machinery of the early/recycling endosomes-to-TGN (trans-Golgi network) route, used by internalised Shiga toxin B-fragment. Two endosome-associated v-SNAREs (VAMP3/cellubrevin and VAMP4) and one TGN-associated t-SNARE complex (consisting of syntaxin 6, syntaxin 16 and Vti1a) are involved, suggesting the existence of two parallel pathways between endosomes and Golgi (see Figure 1). The function of one of the two Rab6 isoforms ubiquitously expressed in mammalian cells, Rab6A′, is also required for this transport step
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Mallard F., Tang B.L., Galli T., Tenza D., Saint-Pol A., Yue X., Antony C., Hong W., Goud B., Johannes L. Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform. J. Cell Biol. 156:2002;653-664 This paper identifies components of the molecular machinery of the early/recycling endosomes-to-TGN (trans-Golgi network) route, used by internalised Shiga toxin B-fragment. Two endosome-associated v-SNAREs (VAMP3/cellubrevin and VAMP4) and one TGN-associated t-SNARE complex (consisting of syntaxin 6, syntaxin 16 and Vti1a) are involved, suggesting the existence of two parallel pathways between endosomes and Golgi (see Figure 1). The function of one of the two Rab6 isoforms ubiquitously expressed in mammalian cells, Rab6A′, is also required for this transport step.
-
(2002)
J. Cell Biol.
, vol.156
, pp. 653-664
-
-
Mallard, F.1
Tang, B.L.2
Galli, T.3
Tenza, D.4
Saint-Pol, A.5
Yue, X.6
Antony, C.7
Hong, W.8
Goud, B.9
Johannes, L.10
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13
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0037073694
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Vps51p Links the VFT Complex to the SNARE Tlg1p
-
Siniossoglou S., Pelham H.R. Vps51p Links the VFT Complex to the SNARE Tlg1p. J. Biol. Chem. 277:2002;48318-48324.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 48318-48324
-
-
Siniossoglou, S.1
Pelham, H.R.2
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14
-
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85031135188
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Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p
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in press
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Conibear E, Cleck JN, Stevens TH: Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p. Mol Biol Cell in press.
-
Mol Biol Cell
-
-
Conibear, E.1
Cleck, J.N.2
Stevens, T.H.3
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15
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0035503740
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An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes
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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. 20:2001;5991-5998.
-
(2001)
EMBO J.
, vol.20
, pp. 5991-5998
-
-
Siniossoglou, S.1
Pelham, H.R.2
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16
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0037428439
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Biochemical and genetic evidence for the involvement of yeast Ypt6 GTPase in protein retrieval to different Golgi compartments
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The biochemical and genetic analysis of new temperature-sensitive mutants of Ypt6p, the yeast counterpart of mammalian Rab6, demonstrated the primary role of Ypt6p in retrograde endosome-to-Golgi transport and protein recycling between late and early Golgi compartments. Ypt6p could also be involved in Golgi-to-ER transport. This study clarifies the role of Ypt6p, previously shown to regulate forward traffic, and indicates that Ypt6p and Rab6 fulfil similar functions
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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. 278:2003;791-799 The biochemical and genetic analysis of new temperature-sensitive mutants of Ypt6p, the yeast counterpart of mammalian Rab6, demonstrated the primary role of Ypt6p in retrograde endosome-to-Golgi transport and protein recycling between late and early Golgi compartments. Ypt6p could also be involved in Golgi-to-ER transport. This study clarifies the role of Ypt6p, previously shown to regulate forward traffic, and indicates that Ypt6p and Rab6 fulfil similar functions.
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 791-799
-
-
Luo, Z.1
Gallwitz, D.2
-
17
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0033634771
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Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: Assembly into multimeric complexes
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Haft C.R., Sierra M.L., Bafford R., Lesniak M.A., Barr V.A., Taylor S.I. Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes. Mol. Biol. Cell. 11:2000;4105-4116.
-
(2000)
Mol. Biol. Cell
, vol.11
, pp. 4105-4116
-
-
Haft, C.R.1
Sierra, M.L.2
Bafford, R.3
Lesniak, M.A.4
Barr, V.A.5
Taylor, S.I.6
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18
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0036796970
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Genetic analysis of sorting nexins 1 and 2 reveals a redundant and essential function in mice
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Schwarz D.G., Griffin C.T., Schneider E.A., Yee D., Magnuson T. Genetic analysis of sorting nexins 1 and 2 reveals a redundant and essential function in mice. Mol. Biol. Cell. 13:2002;3588-3600.
-
(2002)
Mol. Biol. Cell
, vol.13
, pp. 3588-3600
-
-
Schwarz, D.G.1
Griffin, C.T.2
Schneider, E.A.3
Yee, D.4
Magnuson, T.5
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19
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0035972147
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Rapid cycling of lipid raft markers between the cell surface and Golgi complex
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Nichols B.J., Kenworthy A.K., Polishchuk R.S., Lodge R., Roberts T.H., Hirschberg K., Phair R.D., Lippincott-Schwartz J. Rapid cycling of lipid raft markers between the cell surface and Golgi complex. J. Cell Biol. 153:2001;529-541.
-
(2001)
J. Cell Biol.
, vol.153
, pp. 529-541
-
-
Nichols, B.J.1
Kenworthy, A.K.2
Polishchuk, R.S.3
Lodge, R.4
Roberts, T.H.5
Hirschberg, K.6
Phair, R.D.7
Lippincott-Schwartz, J.8
-
21
-
-
0036704669
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The Golgi apparatus: Balancing new with old
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Storrie B., Nilsson T. The Golgi apparatus: balancing new with old. Traffic. 3:2002;521-529.
-
(2002)
Traffic
, vol.3
, pp. 521-529
-
-
Storrie, B.1
Nilsson, T.2
-
22
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0037071543
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The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins
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The authors have identified three new subunits of the yeast Sec34-Sec35 tethering complex, designated Tfi1p, Tfi2p and Tf13p. They demonstrate a direct interaction of the Sec34-Sec35 complex with the active form of Ypt1, a subset of SNAREs involved in intra-Golgi recycling, and with COPI coats (but not ER-to-Golgi COPII coats), suggesting a role for the complex in retrograde transport within the yeast Golgi complex. Two possible models for Sec34-Sec35 function in intra-Golgi retrograde traffic are discussed
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Suvorova E.S., Duden R., Lupashin V.V. The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins. J. Cell Biol. 157:2002;631-643 The authors have identified three new subunits of the yeast Sec34-Sec35 tethering complex, designated Tfi1p, Tfi2p and Tf13p. They demonstrate a direct interaction of the Sec34-Sec35 complex with the active form of Ypt1, a subset of SNAREs involved in intra-Golgi recycling, and with COPI coats (but not ER-to-Golgi COPII coats), suggesting a role for the complex in retrograde transport within the yeast Golgi complex. Two possible models for Sec34-Sec35 function in intra-Golgi retrograde traffic are discussed.
-
(2002)
J. Cell Biol.
, vol.157
, pp. 631-643
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-
Suvorova, E.S.1
Duden, R.2
Lupashin, V.V.3
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23
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0037193464
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Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function
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•] represent two of several recent studies on this novel tethering complex (reviewed in [55]), which share homology to the yeast exocyst and the trans-Golgi-network-associated GARP complex
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•] represent two of several recent studies on this novel tethering complex (reviewed in [55]), which share homology to the yeast exocyst and the trans-Golgi-network-associated GARP complex.
-
(2002)
J. Cell Biol.
, vol.157
, pp. 405-415
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-
Ungar, D.1
Oka, T.2
Brittle, E.E.3
Vasile, E.4
Lupashin, V.V.5
Chatterton, J.E.6
Heuser, J.E.7
Krieger, M.8
Waters, M.G.9
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24
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0037013292
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Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum
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Velloso L.M., Svensson K., Schneider G., Pettersson R., Lindqvist Y. Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum. J. Biol. Chem. 277:2002;15979-15984.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 15979-15984
-
-
Velloso, L.M.1
Svensson, K.2
Schneider, G.3
Pettersson, R.4
Lindqvist, Y.5
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25
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-
0037101946
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Vesicular transport: The core machinery of COPI recruitment and budding
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Nickel W., Wieland F.T. Vesicular transport: the core machinery of COPI recruitment and budding. J. Cell Sci. 115:2002;3235-3240.
-
(2002)
J. Cell Sci.
, vol.115
, pp. 3235-3240
-
-
Nickel, W.1
Wieland, F.T.2
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26
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0037339919
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The KDEL and KKXX retrieval signals appended to the same reporter protein determine different trafficking between endoplasmic reticulum, intermediate compartment and Golgi complex
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Using an in vitro budding assay to measure ER exit, in combination with cell fractionation, biochemical and morphological methods, the authors studied the transport of two forms of the same reporter protein, CD8 antigen, appended with different carboxy-terminal retrieval signals. Unexpectedly, KDEL-tagged CD8 (soluble CD8-K), which is mainly restricted to the ER, is rapidly incorporated into ER-derived transport vesicles, but it is poorly O-glycosylated, showing that it is efficiently recycled from the intermediate compartment (IC) back to the ER. CD8 carrying a dibasic KKMP-motif (transmembrane CD-E19) displays much slower ER exit, but is efficiently O-glycosylated, suggesting that its retrieval mostly takes place from cis-Golgi. The authors propose that the site of retrieval is determined by different ionic environments prevailing in the lumen of the IC and early Golgi, affecting the affinities between the reporter molecules and the COPI machinery
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Stornaiulo M., Lotti L.V., Borgese N., Torrisi M.R., Mottola G., Martire G., Bonatti S. The KDEL and KKXX retrieval signals appended to the same reporter protein determine different trafficking between endoplasmic reticulum, intermediate compartment and Golgi complex. Mol. Biol. Cell. 14:2003;889-902 Using an in vitro budding assay to measure ER exit, in combination with cell fractionation, biochemical and morphological methods, the authors studied the transport of two forms of the same reporter protein, CD8 antigen, appended with different carboxy-terminal retrieval signals. Unexpectedly, KDEL-tagged CD8 (soluble CD8-K), which is mainly restricted to the ER, is rapidly incorporated into ER-derived transport vesicles, but it is poorly O-glycosylated, showing that it is efficiently recycled from the intermediate compartment (IC) back to the ER. CD8 carrying a dibasic KKMP-motif (transmembrane CD-E19) displays much slower ER exit, but is efficiently O-glycosylated, suggesting that its retrieval mostly takes place from cis-Golgi. The authors propose that the site of retrieval is determined by different ionic environments prevailing in the lumen of the IC and early Golgi, affecting the affinities between the reporter molecules and the COPI machinery.
-
(2003)
Mol. Biol. Cell
, vol.14
, pp. 889-902
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Stornaiulo, M.1
Lotti, L.V.2
Borgese, N.3
Torrisi, M.R.4
Mottola, G.5
Martire, G.6
Bonatti, S.7
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27
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0036749797
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2+ storage
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2+ depletion results in the redistribution of the KDEL receptor from the Golgi complex to IC elements
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2+ depletion results in the redistribution of the KDEL receptor from the Golgi complex to IC elements.
-
(2002)
Eur. J. Cell Biol.
, vol.81
, pp. 469-483
-
-
Ying, M.1
Sannerud, R.2
Flatmark, T.3
Saraste, J.4
-
29
-
-
0033615098
-
The Croonian lecture. Intracellular membrane traffic: Getting proteins sorted
-
Pelham H.R.B. The Croonian lecture. Intracellular membrane traffic: getting proteins sorted. Philos. Trans. R Soc. Lond. B Biol. Sci. 354:1999;1471-1478.
-
(1999)
Philos. Trans. R Soc. Lond. B Biol. Sci.
, vol.354
, pp. 1471-1478
-
-
Pelham, H.R.B.1
-
30
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0028791675
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The brefeldin A-induced retrograde transport from the Golgi apparatus to the endoplasmic reticulum depends on calcium sequestered to intracellular stores
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Ivessa N.E., De Lemos-Chiarandini C., Gravotta D., Sabatini D.D., Kreibich G. The brefeldin A-induced retrograde transport from the Golgi apparatus to the endoplasmic reticulum depends on calcium sequestered to intracellular stores. J. Biol. Chem. 270:1995;25960-25967.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 25960-25967
-
-
Ivessa, N.E.1
De Lemos-Chiarandini, C.2
Gravotta, D.3
Sabatini, D.D.4
Kreibich, G.5
-
31
-
-
0037144587
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Selective effects of calcium chelators on anterograde and retrograde protein transport in the cell
-
Chen J.-L., Ahluwalia J.P., Stamnes M. Selective effects of calcium chelators on anterograde and retrograde protein transport in the cell. J. Biol. Chem. 277:2002;35682-35687.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 35682-35687
-
-
Chen, J.-L.1
Ahluwalia, J.P.2
Stamnes, M.3
-
32
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0037112329
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Forward transport: 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals
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Many transmembrane proteins destined to post-Golgi locations and the plasma membrane contain dibasic retention motifs in their cytoplasmic tails that interact with COPI coats, resulting in retention of these proteins in the early secretory pathway. This paper shows that, in addition to such a motif, KCNK3 potassium channels contain another site for phosphorylation-dependent (protein kinase A) binding of 14-3-3β, a cytoplasmic 30 kDa protein. Binding of 14-3-3β inhibits the interaction of KCNK3 with β-COP, resulting in inhibition of its retention, and leading to its transport to the plasma membrane. A similar system was shown to apply to another potassium channel (KCNK9), acetylcholine receptor, as well as the invariant chain (Iip35) binding to class II MHC molecules, suggesting that it represents a general mechanism to regulate forward versus retrograde trafficking
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O'Kelly I., Butler M.H., Zilberberg N., Goldstein S.A.N. Forward transport: 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell. 111:2002;577-588 Many transmembrane proteins destined to post-Golgi locations and the plasma membrane contain dibasic retention motifs in their cytoplasmic tails that interact with COPI coats, resulting in retention of these proteins in the early secretory pathway. This paper shows that, in addition to such a motif, KCNK3 potassium channels contain another site for phosphorylation-dependent (protein kinase A) binding of 14-3-3β, a cytoplasmic 30 kDa protein. Binding of 14-3-3β inhibits the interaction of KCNK3 with β-COP, resulting in inhibition of its retention, and leading to its transport to the plasma membrane. A similar system was shown to apply to another potassium channel (KCNK9), acetylcholine receptor, as well as the invariant chain (Iip35) binding to class II MHC molecules, suggesting that it represents a general mechanism to regulate forward versus retrograde trafficking.
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(2002)
Cell
, vol.111
, pp. 577-588
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O'Kelly, I.1
Butler, M.H.2
Zilberberg, N.3
Goldstein, S.A.N.4
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33
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0037078331
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ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat
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This paper addresses the function of the GTPase-activating protein of ARF1 (ARFGAP1) in the biogenesis of COPI vesicles, providing important new information that clarifies previous conflicting data. Vesicle formation was reconstituted in a modified in vitro assay in the presence GTP and purified components, including recombinant ARPGAP1. In contrast to previous views, emphasising a role for ARFGAP1 in vesicle uncoating via deactivation of ARF1, the authors have obtained convincing results showing that ARFGAP1 in fact promotes vesicle formation and participates in cargo recruitment. Purified vesicles were shown to contain large amounts of ARFGAP1, suggesting that the protein also plays a structural role in vesicle formation
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Yang J.-S., Lee S.Y., Gao M., Bourgoin S., Randazzo P.A., Premont R.T., Hsu V.W. ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat. J. Cell Biol. 159:2002;69-78 This paper addresses the function of the GTPase-activating protein of ARF1 (ARFGAP1) in the biogenesis of COPI vesicles, providing important new information that clarifies previous conflicting data. Vesicle formation was reconstituted in a modified in vitro assay in the presence GTP and purified components, including recombinant ARPGAP1. In contrast to previous views, emphasising a role for ARFGAP1 in vesicle uncoating via deactivation of ARF1, the authors have obtained convincing results showing that ARFGAP1 in fact promotes vesicle formation and participates in cargo recruitment. Purified vesicles were shown to contain large amounts of ARFGAP1, suggesting that the protein also plays a structural role in vesicle formation.
-
(2002)
J. Cell Biol.
, vol.159
, pp. 69-78
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Yang, J.-S.1
Lee, S.Y.2
Gao, M.3
Bourgoin, S.4
Randazzo, P.A.5
Premont, R.T.6
Hsu, V.W.7
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34
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0037046592
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Dissection of COPI and Arf1 dynamics in vivo and role in Golgi membrane transport
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Live-cell imaging (FRAP and FLIP), brefeldin-A-induced coat release and mathematical modelling were used to study and compare the kinetics of association of fluorescently labelled ARF1 and ε-COP with pre-Golgi and Golgi membranes. The authors show that the two proteins have different residence times on Golgi membranes. In addition, ARF1 and COPI bind and are released from membranes in a continuous process that can be uncoupled from vesicle formation. The experimental data fits with a model that takes into account that ARF1 has multiple effector systems, and suggests that Arf1 and coatomer function in the formation of stable membrane domains
-
Presley J., Ward T.H., Pfeifer A.C., Siggia E.D., Phair R.D., Lippincott-Schwartz J. Dissection of COPI and Arf1 dynamics in vivo and role in Golgi membrane transport. Nature. 417:2002;187-193 Live-cell imaging (FRAP and FLIP), brefeldin-A-induced coat release and mathematical modelling were used to study and compare the kinetics of association of fluorescently labelled ARF1 and ε-COP with pre-Golgi and Golgi membranes. The authors show that the two proteins have different residence times on Golgi membranes. In addition, ARF1 and COPI bind and are released from membranes in a continuous process that can be uncoupled from vesicle formation. The experimental data fits with a model that takes into account that ARF1 has multiple effector systems, and suggests that Arf1 and coatomer function in the formation of stable membrane domains.
-
(2002)
Nature
, vol.417
, pp. 187-193
-
-
Presley, J.1
Ward, T.H.2
Pfeifer, A.C.3
Siggia, E.D.4
Phair, R.D.5
Lippincott-Schwartz, J.6
-
35
-
-
0028926819
-
Localization of the small GTP-binding protein Rab1p to early compartments of the secretory pathway
-
Saraste J., Lahtinen U., Goud B. Localization of the small GTP-binding protein Rab1p to early compartments of the secretory pathway. J. Cell Sci. 108:1995;1541-1552.
-
(1995)
J. Cell Sci.
, vol.108
, pp. 1541-1552
-
-
Saraste, J.1
Lahtinen, U.2
Goud, B.3
-
36
-
-
0028239912
-
GTPases: Multifunctional molecular switches regulating vesicular traffic
-
Nuoffer C., Balch W.E. GTPases: Multifunctional molecular switches regulating vesicular traffic. Annu. Rev. Biochem. 63:1994;949-990.
-
(1994)
Annu. Rev. Biochem.
, vol.63
, pp. 949-990
-
-
Nuoffer, C.1
Balch, W.E.2
-
37
-
-
0034698202
-
Rab1 recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion
-
Allan B.B., Moyer B.D., Balch W.E. Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion. Science. 289:2000;444-448.
-
(2000)
Science
, vol.289
, pp. 444-448
-
-
Allan, B.B.1
Moyer, B.D.2
Balch, W.E.3
-
38
-
-
0035035657
-
The Golgi matrix protein GM130: A specific interacting partner of the small GTPase Rab1
-
Weide T., Bayer M., Koster M., Siebrasse J.P., Peters R., Barnekow A. The Golgi matrix protein GM130: a specific interacting partner of the small GTPase Rab1. EMBO Rep. 2:2001;336-341.
-
(2001)
EMBO Rep.
, vol.2
, pp. 336-341
-
-
Weide, T.1
Bayer, M.2
Koster, M.3
Siebrasse, J.P.4
Peters, R.5
Barnekow, A.6
-
39
-
-
0035024551
-
Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis-Golgi tethering
-
Moyer B.D., Allan B.B., Balch W.E. Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis-Golgi tethering. Traffic. 2:2001;268-276.
-
(2001)
Traffic
, vol.2
, pp. 268-276
-
-
Moyer, B.D.1
Allan, B.B.2
Balch, W.E.3
-
41
-
-
0034139657
-
Facing inward from compartment shores: How many pathways were we looking for?
-
Johannes L., Goud B. Facing inward from compartment shores: How many pathways were we looking for? Traffic. 1:2000;119-123.
-
(2000)
Traffic
, vol.1
, pp. 119-123
-
-
Johannes, L.1
Goud, B.2
-
43
-
-
0037012521
-
Retrograde transport of protein toxins under conditions of COPI dysfunction
-
The authors studied the role of the COPI machinery in retrograde transport of protein toxins using mutant Chinese hamster ovary (ldlF) cells with a temperature-sensitive defect in the ε-COP subunit of COPI coats, and cyclohexane-bismethylamine, a compound that blocks COPI binding to membranes. Unexpectedly, they find that cells under these conditions remain sensitive to toxins, irrespective of whether or not they contain a KDEL (or KDEL-like) sequence. These data support the existence of a COPI-independent pathway from the trans-Golgi network to the ER, and suggest that the mechanisms of the COPI-dependent and -independent pathways are closely linked
-
Chen A., Mikoryak C., Draper R.K. Retrograde transport of protein toxins under conditions of COPI dysfunction. Biochim. Biophys. Acta. 1589:2002;124-139 The authors studied the role of the COPI machinery in retrograde transport of protein toxins using mutant Chinese hamster ovary (ldlF) cells with a temperature-sensitive defect in the ε-COP subunit of COPI coats, and cyclohexane-bismethylamine, a compound that blocks COPI binding to membranes. Unexpectedly, they find that cells under these conditions remain sensitive to toxins, irrespective of whether or not they contain a KDEL (or KDEL-like) sequence. These data support the existence of a COPI-independent pathway from the trans-Golgi network to the ER, and suggest that the mechanisms of the COPI-dependent and -independent pathways are closely linked.
-
(2002)
Biochim. Biophys. Acta
, vol.1589
, pp. 124-139
-
-
Chen, A.1
Mikoryak, C.2
Draper, R.K.3
-
44
-
-
0033224214
-
Evidence for a COPI-independent transport route from the Golgi complex to the endoplasmic reticulum
-
Girod A., Storrie B., Simpson J., Johannes L., Goud B., Roberts L.M., Lord J.M., Nilsson T., Pepperkok R. Evidence for a COPI-independent transport route from the Golgi complex to the endoplasmic reticulum. Nat. Cell Biol. 1:1999;423-430.
-
(1999)
Nat. Cell Biol.
, vol.1
, pp. 423-430
-
-
Girod, A.1
Storrie, B.2
Simpson, J.3
Johannes, L.4
Goud, B.5
Roberts, L.M.6
Lord, J.M.7
Nilsson, T.8
Pepperkok, R.9
-
45
-
-
0033571602
-
Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells
-
White J., Johannes L., Mallard F., Girod A., Grill S., Reinsch S., Keller P., Tzschaschel B., Eckard A., Goud B., Stelzer E.H.K. Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells. J. Cell Biol. 147:1999;743-759.
-
(1999)
J. Cell Biol.
, vol.147
, pp. 743-759
-
-
White, J.1
Johannes, L.2
Mallard, F.3
Girod, A.4
Grill, S.5
Reinsch, S.6
Keller, P.7
Tzschaschel, B.8
Eckard, A.9
Goud, B.10
Stelzer, E.H.K.11
-
46
-
-
0036902478
-
Bicaudal regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex
-
This paper shows that Rab6 directly interacts with Bicaudal-D1 (BICD1), one of the two mammalian homologues of Drosophila Bicaudal-D. Rab6 may serve as a receptor for BICD1, which then recruits the dynein-dynactin complex on Golgi and/or Golgi-derived membranes. This study provides a molecular basis for the bidirectional movement along microtubules of Golgi-to-ER transport intermediates defined by Rab6A (COPI-independent transport)
-
Matanis T., Akhmanova A., Wulf P., Del Nery E., Weide T., Stepanova T., Galjart N., Grosveld F., Goud B., De Zeeuw C.I.et al. Bicaudal regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex. Nat. Cell Biol. 4:2002;986-992 This paper shows that Rab6 directly interacts with Bicaudal-D1 (BICD1), one of the two mammalian homologues of Drosophila Bicaudal-D. Rab6 may serve as a receptor for BICD1, which then recruits the dynein-dynactin complex on Golgi and/or Golgi-derived membranes. This study provides a molecular basis for the bidirectional movement along microtubules of Golgi-to-ER transport intermediates defined by Rab6A (COPI-independent transport).
-
(2002)
Nat. Cell Biol.
, vol.4
, pp. 986-992
-
-
Matanis, T.1
Akhmanova, A.2
Wulf, P.3
Del Nery, E.4
Weide, T.5
Stepanova, T.6
Galjart, N.7
Grosveld, F.8
Goud, B.9
De Zeeuw, C.I.10
-
47
-
-
0037108473
-
The Rab6 GTPase regulates recruitment of the dynactin complex to Golgi membranes
-
Short B., Preisinger C., Schaletzky J., Kopajtich R., Barr F. The Rab6 GTPase regulates recruitment of the dynactin complex to Golgi membranes. Curr. Biol. 12:2002;1792-1795.
-
(2002)
Curr. Biol.
, vol.12
, pp. 1792-1795
-
-
Short, B.1
Preisinger, C.2
Schaletzky, J.3
Kopajtich, R.4
Barr, F.5
-
48
-
-
0036678493
-
Structure of the Golgi and distribution of reporter molecules at 20°C reveals the complexity of the exit compartments
-
Rapid freezing techniques, high-resolution electron microscope tomography, and three-dimensional reconstruction of serial sections were applied to investigate Golgi structure in NRK cells incubated at 20°C, which blocks protein exit from the Golgi complex. The disappearance of trans-Golgi tubules was accompanied by lateral bulging of the three trans-most cisternae, suggesting that exit occurs from multiple trans-cisternae. In this study, the authors also characterise further a specialised ER domain that intimately associates with several trans-cisternae, suggesting a direct route for exchange of material between trans-Golgi and the ER
-
Ladinsky M.S., Wu C.C., McIntosh S., McIntosh J.R., Howell K.E. Structure of the Golgi and distribution of reporter molecules at 20°C reveals the complexity of the exit compartments. Mol. Biol. Cell. 13:2002;2810-2825 Rapid freezing techniques, high-resolution electron microscope tomography, and three-dimensional reconstruction of serial sections were applied to investigate Golgi structure in NRK cells incubated at 20°C, which blocks protein exit from the Golgi complex. The disappearance of trans-Golgi tubules was accompanied by lateral bulging of the three trans-most cisternae, suggesting that exit occurs from multiple trans-cisternae. In this study, the authors also characterise further a specialised ER domain that intimately associates with several trans-cisternae, suggesting a direct route for exchange of material between trans-Golgi and the ER.
-
(2002)
Mol. Biol. Cell
, vol.13
, pp. 2810-2825
-
-
Ladinsky, M.S.1
Wu, C.C.2
McIntosh, S.3
McIntosh, J.R.4
Howell, K.E.5
-
49
-
-
0034493602
-
Dynamics of transitional endoplasmic reticulum sites in vertebrate cells
-
Hammond A.T., Glick B.S. Dynamics of transitional endoplasmic reticulum sites in vertebrate cells. Mol. Biol. Cell. 11:2000;3013-3030.
-
(2000)
Mol. Biol. Cell
, vol.11
, pp. 3013-3030
-
-
Hammond, A.T.1
Glick, B.S.2
-
50
-
-
0037328573
-
Myosin motors and not actin comets are mediators of the actin-based Golgi-to-ER protein transport
-
in press
-
Duran JM, Valderrama F, Castel S, Magdalena J, Tomas M, Hosoya H, Renau-Piqueras J, Malhotra V, Egea G: Myosin motors and not actin comets are mediators of the actin-based Golgi-to-ER protein transport. Mol Biol Cell 2003, in press.
-
(2003)
Mol Biol Cell
-
-
Duran, J.M.1
Valderrama, F.2
Castel, S.3
Magdalena, J.4
Tomas, M.5
Hosoya, H.6
Renau-Piqueras, J.7
Malhotra, V.8
Egea, G.9
-
51
-
-
0036702196
-
Regulating the actin cytoskeleton during vesicular transport
-
Stamnes M. Regulating the actin cytoskeleton during vesicular transport. Curr. Opin. Cell Biol. 14:2002;428-433.
-
(2002)
Curr. Opin. Cell Biol.
, vol.14
, pp. 428-433
-
-
Stamnes, M.1
-
52
-
-
0036843024
-
The overexpression of GMAP-210 blocks anterograde and retrograde transport between the ER and the Golgi apparatus
-
Pernet-Gallay K., Antony C., Johannes L., Bornens M., Goud B., Rios R.M. The overexpression of GMAP-210 blocks anterograde and retrograde transport between the ER and the Golgi apparatus. Traffic. 3:2002;822-832.
-
(2002)
Traffic
, vol.3
, pp. 822-832
-
-
Pernet-Gallay, K.1
Antony, C.2
Johannes, L.3
Bornens, M.4
Goud, B.5
Rios, R.M.6
-
53
-
-
0037128212
-
CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family
-
Cytoplasmic linker proteins (CLIPs) are non-motor microtubule-binding proteins. The authors have characterised a novel CLIP protein, CLIPR-59, that is localised to trans-Golgi network (TGN) membranes. CLIP-59 could be involved in early/recycling endosome-TGN dynamics
-
Perez F., Pernet-Gallay K., Nizak C., Goodson H.V., Kreis T.E., Goud B. CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family. J. Cell Biol. 156:2002;631-642 Cytoplasmic linker proteins (CLIPs) are non-motor microtubule-binding proteins. The authors have characterised a novel CLIP protein, CLIPR-59, that is localised to trans-Golgi network (TGN) membranes. CLIP-59 could be involved in early/recycling endosome-TGN dynamics.
-
(2002)
J. Cell Biol.
, vol.156
, pp. 631-642
-
-
Perez, F.1
Pernet-Gallay, K.2
Nizak, C.3
Goodson, H.V.4
Kreis, T.E.5
Goud, B.6
-
54
-
-
0035203528
-
The GM130 and GRASP65 Golgi proteins cycle through a define a subdomain of the intermediate compartment
-
Marra P., Maffucci T., Daniele T., Di Tullio G., Ikehara Y., Chan E.K.L., Luini A., Beznoussenko G., Mironov A., De Matteis M.A. The GM130 and GRASP65 Golgi proteins cycle through a define a subdomain of the intermediate compartment. Nat. Cell Biol. 3:2001;1101-1113.
-
(2001)
Nat. Cell Biol.
, vol.3
, pp. 1101-1113
-
-
Marra, P.1
Maffucci, T.2
Daniele, T.3
Di Tullio, G.4
Ikehara, Y.5
Chan, E.K.L.6
Luini, A.7
Beznoussenko, G.8
Mironov, A.9
De Matteis, M.A.10
-
55
-
-
0036629335
-
Vesicle tethering complexes in membrane traffic
-
Whyte J.R.C., Munro S. Vesicle tethering complexes in membrane traffic. J. Cell Sci. 115:2002;2627-2637.
-
(2002)
J. Cell Sci.
, vol.115
, pp. 2627-2637
-
-
Whyte, J.R.C.1
Munro, S.2
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