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Volumn 31, Issue , 2014, Pages 40-47

Membrane-associated cargo recycling by tubule-based endosomal sorting

Author keywords

Amphipathic helix; BAR; Retromer; Sorting nexin

Indexed keywords

ACAP PROTEIN; BAR PROTEIN; BINDING PROTEIN; CARRIER PROTEIN; CELL PROTEIN; EHD PROTEIN; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITIDE; SNX BAR PROTEIN; SORTING NEXIN; UNCLASSIFIED DRUG;

EID: 84901988137     PISSN: 10849521     EISSN: 10963634     Source Type: Journal    
DOI: 10.1016/j.semcdb.2014.03.015     Document Type: Review
Times cited : (71)

References (93)
  • 2
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink J., Ghigo E., Kalaidzidis Y., Zerial M. Rab conversion as a mechanism of progression from early to late endosomes. Cell 2005, 122:735-749.
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 3
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • Huotari J., Helenius A. Endosome maturation. EMBO J 2011, 30:3481-3500.
    • (2011) EMBO J , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 4
    • 0021033757 scopus 로고
    • Intracellular routing of transferrin and transferrin receptors in epidermoid carcinoma A431 cells
    • Hopkins C.R. Intracellular routing of transferrin and transferrin receptors in epidermoid carcinoma A431 cells. Cell 1983, 35:321-330.
    • (1983) Cell , vol.35 , pp. 321-330
    • Hopkins, C.R.1
  • 5
    • 0024241414 scopus 로고
    • Sorting of mannose 6-phosphate receptors and lysosomal membrane proteins in endocytic vesicles
    • Geuze H.J., Stoorvogel W., Strous G.J., Slot J.W., Bleekemolen J.E., Mellman I. Sorting of mannose 6-phosphate receptors and lysosomal membrane proteins in endocytic vesicles. J Cell Biol 1988, 107:2491-2501.
    • (1988) J Cell Biol , vol.107 , pp. 2491-2501
    • Geuze, H.J.1    Stoorvogel, W.2    Strous, G.J.3    Slot, J.W.4    Bleekemolen, J.E.5    Mellman, I.6
  • 6
    • 0023839303 scopus 로고
    • The mannose 6-phosphate receptor and the biogenesis of lysosomes
    • Griffiths G., Hoflack B., Simons K., Mellman I., Kornfeld S. The mannose 6-phosphate receptor and the biogenesis of lysosomes. Cell 1988, 52:329-341.
    • (1988) Cell , vol.52 , pp. 329-341
    • Griffiths, G.1    Hoflack, B.2    Simons, K.3    Mellman, I.4    Kornfeld, S.5
  • 9
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon H.T., Gallop J. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 2005, 438:590-596.
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.2
  • 10
    • 84885063096 scopus 로고    scopus 로고
    • Bending on the rocks - a cocktail of biophysical modules to build endocytic pathways
    • Johannes L., Wunder C., Bassereau P. Bending on the rocks - a cocktail of biophysical modules to build endocytic pathways. Cold Spring Harb Perspect Biol 2014, 6. 10.1101/cshperspect.a016741.
    • (2014) Cold Spring Harb Perspect Biol , vol.6
    • Johannes, L.1    Wunder, C.2    Bassereau, P.3
  • 11
    • 1442317538 scopus 로고    scopus 로고
    • BAR domains as sensors of membrane curvature: the amphiphysin BAR structure
    • Peter B.J., Kent H.M., Mills I.G., Vallis Y., Butler P.J.G., Evans P.R., et al. BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science 2004, 303:495-499.
    • (2004) Science , vol.303 , pp. 495-499
    • Peter, B.J.1    Kent, H.M.2    Mills, I.G.3    Vallis, Y.4    Butler, P.J.G.5    Evans, P.R.6
  • 12
    • 1842483252 scopus 로고    scopus 로고
    • Membrane curvature: how BAR domains bend bilayers
    • Zimmerberg J., McLaughlin S. Membrane curvature: how BAR domains bend bilayers. Curr Biol 2004, 14:R250-R252.
    • (2004) Curr Biol , vol.14
    • Zimmerberg, J.1    McLaughlin, S.2
  • 13
    • 40049086567 scopus 로고    scopus 로고
    • Structural basis of membrane invagination by F-BAR domains
    • Frost A., Perera R., Roux A., Spasov K., Destaing O., Egelman E.H., et al. Structural basis of membrane invagination by F-BAR domains. Cell 2008, 132:807-817.
    • (2008) Cell , vol.132 , pp. 807-817
    • Frost, A.1    Perera, R.2    Roux, A.3    Spasov, K.4    Destaing, O.5    Egelman, E.H.6
  • 14
    • 70449133786 scopus 로고    scopus 로고
    • Phosphoinositides: Navigation through the endosomal maze
    • Rutherford A.C., Cullen P.J. Phosphoinositides: Navigation through the endosomal maze. Biochem Soc 2009, 20-25.
    • (2009) Biochem Soc , pp. 20-25
    • Rutherford, A.C.1    Cullen, P.J.2
  • 15
    • 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., et al. Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides. Curr Biol 2004, 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
  • 16
    • 45849124923 scopus 로고    scopus 로고
    • Endosomal sorting and signalling: an emerging role for sorting nexins
    • Cullen P.J. Endosomal sorting and signalling: an emerging role for sorting nexins. Nat Rev Mol Cell Biol 2008, 9:574-582.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 574-582
    • Cullen, P.J.1
  • 17
    • 79955548766 scopus 로고    scopus 로고
    • Evolutionary reconstruction of the retromer complex and its function in Trypanosoma brucei
    • Koumandou V.L., Klute M.J., Herman E.K., Nunez-Miguel R., Dacks J.B., Field M.C. Evolutionary reconstruction of the retromer complex and its function in Trypanosoma brucei. J Cell Sci 2011, 124:1496-1509.
    • (2011) J Cell Sci , vol.124 , pp. 1496-1509
    • Koumandou, V.L.1    Klute, M.J.2    Herman, E.K.3    Nunez-Miguel, R.4    Dacks, J.B.5    Field, M.C.6
  • 18
    • 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 2004, 165:111-122.
    • (2004) J Cell Biol , vol.165 , pp. 111-122
    • Seaman, M.N.1
  • 20
    • 84255208762 scopus 로고    scopus 로고
    • Sorting nexins provide diversity for retromer-dependent trafficking events
    • Cullen P.J., Korswagen H.C. Sorting nexins provide diversity for retromer-dependent trafficking events. Nat Cell Biol 2012, 14:29-37.
    • (2012) Nat Cell Biol , vol.14 , pp. 29-37
    • Cullen, P.J.1    Korswagen, H.C.2
  • 21
    • 67650218762 scopus 로고    scopus 로고
    • The retromer coat complex coordinates endosomal sorting and dynein-mediated transport, with carrier recognition by the trans-Golgi network
    • Wassmer T., Attar N., Harterink M., van Weering J.R.T., Traer C.J., Oakley J., et al. The retromer coat complex coordinates endosomal sorting and dynein-mediated transport, with carrier recognition by the trans-Golgi network. Dev Cell 2009, 17:110-122.
    • (2009) Dev Cell , vol.17 , pp. 110-122
    • Wassmer, T.1    Attar, N.2    Harterink, M.3    van Weering, J.R.T.4    Traer, C.J.5    Oakley, J.6
  • 22
    • 57049128177 scopus 로고    scopus 로고
    • Evolution of specificity in the eukaryotic endomembrane system
    • Dacks J.B., Peden A.A., Field M.C. Evolution of specificity in the eukaryotic endomembrane system. Int J Biochem Cell Biol 2009, 41:330-340.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 330-340
    • Dacks, J.B.1    Peden, A.A.2    Field, M.C.3
  • 23
    • 35548969906 scopus 로고    scopus 로고
    • Functional architecture of the retromer cargo-recognition complex
    • Hierro A., Rojas A.L., Rojas R., Murthy V.N., Effantin G., Kajava A.V., et al. Functional architecture of the retromer cargo-recognition complex. Nature 2007, 449:1063-1067.
    • (2007) Nature , vol.449 , pp. 1063-1067
    • Hierro, A.1    Rojas, A.L.2    Rojas, R.3    Murthy, V.N.4    Effantin, G.5    Kajava, A.V.6
  • 25
    • 45849110080 scopus 로고    scopus 로고
    • SNX18 is an SNX9 paralog that acts as a membrane tubulator in AP-1-positive endosomal trafficking
    • Haberg K., Lundmark R., Carlsson S.R. SNX18 is an SNX9 paralog that acts as a membrane tubulator in AP-1-positive endosomal trafficking. J Cell Sci 2008, 121:1495-1505.
    • (2008) J Cell Sci , vol.121 , pp. 1495-1505
    • Haberg, K.1    Lundmark, R.2    Carlsson, S.R.3
  • 26
    • 83255187127 scopus 로고    scopus 로고
    • SNX-BAR-mediated endosome tubulation is co-ordinated with endosome maturation
    • van Weering J.R.T., Verkade P., Cullen P.J. SNX-BAR-mediated endosome tubulation is co-ordinated with endosome maturation. Traffic 2012, 13:94-107.
    • (2012) Traffic , vol.13 , pp. 94-107
    • van Weering, J.R.T.1    Verkade, P.2    Cullen, P.J.3
  • 27
    • 84870541192 scopus 로고    scopus 로고
    • Molecular basis for SNX-BAR-mediated assembly of distinct endosomal sorting tubules
    • van Weering J.R.T., Sessions R.B., Traer C.J., Kloer D.P., Bhatia V.K., Stamou D., et al. Molecular basis for SNX-BAR-mediated assembly of distinct endosomal sorting tubules. EMBO J 2012, 31:4466-4480.
    • (2012) EMBO J , vol.31 , pp. 4466-4480
    • van Weering, J.R.T.1    Sessions, R.B.2    Traer, C.J.3    Kloer, D.P.4    Bhatia, V.K.5    Stamou, D.6
  • 28
    • 79551470818 scopus 로고    scopus 로고
    • Specific amino acids in the BAR domain allow homodimerization and prevent heterodimerization of sorting nexin 33
    • Dislich B., Than M.E., Lichtenthaler S.F. Specific amino acids in the BAR domain allow homodimerization and prevent heterodimerization of sorting nexin 33. Biochem J 2010, 433:75-83.
    • (2010) Biochem J , vol.433 , pp. 75-83
    • Dislich, B.1    Than, M.E.2    Lichtenthaler, S.F.3
  • 29
    • 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., Cullen P.J. A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer. J Cell Sci 2007, 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
  • 30
    • 36749009581 scopus 로고    scopus 로고
    • SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport into the endocytic recycling compartment
    • Traer C.J., Rutherford A.C., Palmer K.J., Wassmer T., Oakley J., Attar N., et al. SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport into the endocytic recycling compartment. Nat Cell Biol 2007, 9:1370-1380.
    • (2007) Nat Cell Biol , vol.9 , pp. 1370-1380
    • Traer, C.J.1    Rutherford, A.C.2    Palmer, K.J.3    Wassmer, T.4    Oakley, J.5    Attar, N.6
  • 32
    • 77952393464 scopus 로고    scopus 로고
    • SNX18 shares a redundant role with SNX9 and modulates endocytic trafficking at the plasma membrane
    • Park J., Kim Y., Lee S., Park J.J., Park Z.Y., Sun W., et al. SNX18 shares a redundant role with SNX9 and modulates endocytic trafficking at the plasma membrane. J Cell Sci 2010, 123:1742-1750.
    • (2010) J Cell Sci , vol.123 , pp. 1742-1750
    • Park, J.1    Kim, Y.2    Lee, S.3    Park, J.J.4    Park, Z.Y.5    Sun, W.6
  • 33
    • 69249156036 scopus 로고    scopus 로고
    • Sorting nexin 33 induces mammalian cell micronucleated phenotype and actin polymerization by interacting with Wiskott-Aldrich syndrome protein
    • Zhang J., Zhang X., Guo Y., Xu L., Pei D. Sorting nexin 33 induces mammalian cell micronucleated phenotype and actin polymerization by interacting with Wiskott-Aldrich syndrome protein. J Biol Chem 2009, 284:21659-21669.
    • (2009) J Biol Chem , vol.284 , pp. 21659-21669
    • Zhang, J.1    Zhang, X.2    Guo, Y.3    Xu, L.4    Pei, D.5
  • 34
    • 33745523031 scopus 로고    scopus 로고
    • Mechanism of endophilin N-BAR domain-mediated membrane curvature
    • Gallop J.L., Jao C.C., Kent H.M., Butler P.J., Evans P.R., Langen R., et al. Mechanism of endophilin N-BAR domain-mediated membrane curvature. EMBO J 2006, 25:2898-2910.
    • (2006) EMBO J , vol.25 , pp. 2898-2910
    • Gallop, J.L.1    Jao, C.C.2    Kent, H.M.3    Butler, P.J.4    Evans, P.R.5    Langen, R.6
  • 35
    • 70350783743 scopus 로고    scopus 로고
    • Amphipathic motifs in BAR domains are essential for membrane curvature sensing
    • Bhatia V.K., Madsen K.L., Bolinger P-Y., Kunding A., Hedegård P., Gether U., et al. Amphipathic motifs in BAR domains are essential for membrane curvature sensing. EMBO J 2009, 28:3303-3314.
    • (2009) EMBO J , vol.28 , pp. 3303-3314
    • Bhatia, V.K.1    Madsen, K.L.2    Bolinger, P.-Y.3    Kunding, A.4    Hedegård, P.5    Gether, U.6
  • 36
    • 17944367436 scopus 로고    scopus 로고
    • The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate
    • Bravo J., Karathanassis D., Pacold C.M., Pacold M.E., Ellson C.D., Anderson K.E., et al. The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate. Mol Cell 2001, 8:829-839.
    • (2001) Mol Cell , vol.8 , pp. 829-839
    • Bravo, J.1    Karathanassis, D.2    Pacold, C.M.3    Pacold, M.E.4    Ellson, C.D.5    Anderson, K.E.6
  • 37
    • 84859175662 scopus 로고    scopus 로고
    • Membrane fission is promoted by insertion of amphipathic helices and is restricted by crescent BAR domains
    • Boucrot E., Pick A., Camdere G., Liska N., Evergren E., McMahon H.T., et al. Membrane fission is promoted by insertion of amphipathic helices and is restricted by crescent BAR domains. Cell 2012, 149:124-136.
    • (2012) Cell , vol.149 , pp. 124-136
    • Boucrot, E.1    Pick, A.2    Camdere, G.3    Liska, N.4    Evergren, E.5    McMahon, H.T.6
  • 38
    • 53049089051 scopus 로고    scopus 로고
    • Structure and plasticity of endophilin and sorting nexin 9
    • Wang Q., Kaan H.Y.K., Hooda R.N., Goh S.L., Sondermann H. Structure and plasticity of endophilin and sorting nexin 9. Structure 2008, 16:1574-1587.
    • (2008) Structure , vol.16 , pp. 1574-1587
    • Wang, Q.1    Kaan, H.Y.K.2    Hooda, R.N.3    Goh, S.L.4    Sondermann, H.5
  • 39
    • 33749505651 scopus 로고    scopus 로고
    • Cooperation of phosphoinositides and BAR domain proteins in endosomal tubulation
    • Shinozaki-Narikawa N., Kodama T., Shibasaki Y. Cooperation of phosphoinositides and BAR domain proteins in endosomal tubulation. Traffic 2006, 7:1539-1550.
    • (2006) Traffic , vol.7 , pp. 1539-1550
    • Shinozaki-Narikawa, N.1    Kodama, T.2    Shibasaki, Y.3
  • 41
    • 0035837426 scopus 로고    scopus 로고
    • The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways
    • Tarricone C., Xiao B., Justin N., Walker P.A., Rittinger K., Gamblin S.J., et al. The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Nature 2001, 411:215-219.
    • (2001) Nature , vol.411 , pp. 215-219
    • Tarricone, C.1    Xiao, B.2    Justin, N.3    Walker, P.A.4    Rittinger, K.5    Gamblin, S.J.6
  • 42
    • 3543025954 scopus 로고    scopus 로고
    • The BAR-domain family of proteins: a case of bending and binding?
    • Habermann B. The BAR-domain family of proteins: a case of bending and binding?. EMBO Rep 2004, 5:250-255.
    • (2004) EMBO Rep , vol.5 , pp. 250-255
    • Habermann, B.1
  • 43
    • 33745559393 scopus 로고    scopus 로고
    • Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms
    • Masuda M., Takeda S., Sone M., Ohki T., Mori H., Kamioka Y., et al. Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms. EMBO J 2006, 25:2889-2897.
    • (2006) EMBO J , vol.25 , pp. 2889-2897
    • Masuda, M.1    Takeda, S.2    Sone, M.3    Ohki, T.4    Mori, H.5    Kamioka, Y.6
  • 44
    • 34447256592 scopus 로고    scopus 로고
    • Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature
    • Henne W.M., Kent H.M., Ford M.G., Hegde B.G., Daumke O., Butler P.J., et al. Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature. Structure 2007, 15:839-852.
    • (2007) Structure , vol.15 , pp. 839-852
    • Henne, W.M.1    Kent, H.M.2    Ford, M.G.3    Hegde, B.G.4    Daumke, O.5    Butler, P.J.6
  • 45
    • 69149089020 scopus 로고    scopus 로고
    • Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin
    • Wang Q., Navarro M.V.A.S., Peng G., Molinelli E., Goh S.L., Judson B.L., et al. Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin. Proc Natl Acad Sci U S A 2009, 106:12700-12705.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 12700-12705
    • Wang, Q.1    Navarro, M.V.A.S.2    Peng, G.3    Molinelli, E.4    Goh, S.L.5    Judson, B.L.6
  • 46
    • 77953810901 scopus 로고    scopus 로고
    • A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to membrane-curvature sensing
    • Plomann M., Wittmann J.G., Rudolph M.G. A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to membrane-curvature sensing. J Mol Biol 2010, 400:129-136.
    • (2010) J Mol Biol , vol.400 , pp. 129-136
    • Plomann, M.1    Wittmann, J.G.2    Rudolph, M.G.3
  • 47
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: universal membrane tubulation and fission molecules?
    • Praefcke G.J., McMahon H.T. The dynamin superfamily: universal membrane tubulation and fission molecules?. Nat Rev Mol Cell Biol 2004, 5:133-147.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 48
    • 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., et al. A tubular EHD1-containing compartment involved in the recycling of major histocompatibility complex class I molecules to the plasma membrane. EMBO J 2002, 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
  • 49
    • 23144467137 scopus 로고    scopus 로고
    • EHD proteins associate with syndapin I and II and such interactions play a crucial role in endosomal recycling
    • Braun A., Pinyol R., Dahlhaus R., Koch D., Fonarev P., Grant B.D., et al. EHD proteins associate with syndapin I and II and such interactions play a crucial role in endosomal recycling. Mol Biol Cell 2005, 16:3642-3658.
    • (2005) Mol Biol Cell , vol.16 , pp. 3642-3658
    • Braun, A.1    Pinyol, R.2    Dahlhaus, R.3    Koch, D.4    Fonarev, P.5    Grant, B.D.6
  • 50
    • 35349007899 scopus 로고    scopus 로고
    • Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling
    • Daumke O., Lundmark R., Vallis Y., Martens S., Butler P.J., McMahon H.T. Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling. Nature 2007, 449:923-927.
    • (2007) Nature , vol.449 , pp. 923-927
    • Daumke, O.1    Lundmark, R.2    Vallis, Y.3    Martens, S.4    Butler, P.J.5    McMahon, H.T.6
  • 51
    • 79151477797 scopus 로고    scopus 로고
    • EHD proteins: key conductors of endocytic transport
    • Naslavsky N., Caplan S. EHD proteins: key conductors of endocytic transport. Trends Cell Biol 2011, 21:122-131.
    • (2011) Trends Cell Biol , vol.21 , pp. 122-131
    • Naslavsky, N.1    Caplan, S.2
  • 52
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • Sweitzer S.M., Hinshaw J.E. Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell 1998, 93:1021-1029.
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 53
    • 73349097586 scopus 로고    scopus 로고
    • AMPH-1/amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling
    • Pant S., Sharma M., Patel K., Caplan S., Carr C.M., Grant B.D. AMPH-1/amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling. Nat Cell Biol 2009, 11:1399-1410.
    • (2009) Nat Cell Biol , vol.11 , pp. 1399-1410
    • Pant, S.1    Sharma, M.2    Patel, K.3    Caplan, S.4    Carr, C.M.5    Grant, B.D.6
  • 54
    • 84878686056 scopus 로고    scopus 로고
    • Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular recycling endosome biogenesis
    • S1-S15
    • Giridharan S.S., Cai B., Vitale N., Naslavsky N., Caplan S. Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular recycling endosome biogenesis. Mol Biol Cell 2013, 24:1776-1790. S1-S15.
    • (2013) Mol Biol Cell , vol.24 , pp. 1776-1790
    • Giridharan, S.S.1    Cai, B.2    Vitale, N.3    Naslavsky, N.4    Caplan, S.5
  • 55
    • 35948968787 scopus 로고    scopus 로고
    • EHD1 interacts with retromer to stabilize SNX1 tubules and facilitate endosome-to-Golgi retrieval
    • Gokool S., Tattersall D., Seaman M.N. EHD1 interacts with retromer to stabilize SNX1 tubules and facilitate endosome-to-Golgi retrieval. Traffic 2007, 8:1873-1886.
    • (2007) Traffic , vol.8 , pp. 1873-1886
    • Gokool, S.1    Tattersall, D.2    Seaman, M.N.3
  • 56
    • 0029563632 scopus 로고
    • Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued
    • Vaughan K.T., Vallee R.B. Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued. J Cell Biol 1995, 131:1507-1516.
    • (1995) J Cell Biol , vol.131 , pp. 1507-1516
    • Vaughan, K.T.1    Vallee, R.B.2
  • 57
    • 84880018609 scopus 로고    scopus 로고
    • Microtubule motors mediate endosomal sorting by maintaining functional domain organization
    • Hunt S.D., Townley A.K., Danson C.M., Cullen P.J., Stephens D.J. Microtubule motors mediate endosomal sorting by maintaining functional domain organization. J Cell Sci 2013, 126:2493-2501.
    • (2013) J Cell Sci , vol.126 , pp. 2493-2501
    • Hunt, S.D.1    Townley, A.K.2    Danson, C.M.3    Cullen, P.J.4    Stephens, D.J.5
  • 58
    • 71549167371 scopus 로고    scopus 로고
    • A FAM21-containing WASH complex regulates retromer-dependent sorting
    • Gomez T.S., Billadeau D.D. A FAM21-containing WASH complex regulates retromer-dependent sorting. Dev Cell 2009, 17:699-711.
    • (2009) Dev Cell , vol.17 , pp. 699-711
    • Gomez, T.S.1    Billadeau, D.D.2
  • 59
    • 78149347707 scopus 로고    scopus 로고
    • The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics
    • Harbour M.E., Breusegem S.Y.A., Antrobus R., Freeman C., Reid E., Seaman M.N.J. The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics. J Cell Sci 2010, 123:3703-3717.
    • (2010) J Cell Sci , vol.123 , pp. 3703-3717
    • Harbour, M.E.1    Breusegem, S.Y.A.2    Antrobus, R.3    Freeman, C.4    Reid, E.5    Seaman, M.N.J.6
  • 60
    • 84877293857 scopus 로고    scopus 로고
    • A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport
    • Steinberg F., Gallon M., Winfield M., Thomas E.C., Bell A.J., Heesom K.J., et al. A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport. Nat Cell Biol 2013, 15:461-471.
    • (2013) Nat Cell Biol , vol.15 , pp. 461-471
    • Steinberg, F.1    Gallon, M.2    Winfield, M.3    Thomas, E.C.4    Bell, A.J.5    Heesom, K.J.6
  • 61
    • 0024842857 scopus 로고
    • Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome
    • Dunn K.W., McGraw T.E., Maxfield F.R. Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome. J Cell Biol 1989, 109:3303-3314.
    • (1989) J Cell Biol , vol.109 , pp. 3303-3314
    • Dunn, K.W.1    McGraw, T.E.2    Maxfield, F.R.3
  • 62
    • 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., Maxfield F.R. Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process. J Cell Biol 1993, 121:1257-1269.
    • (1993) J Cell Biol , vol.121 , pp. 1257-1269
    • Mayor, S.1    Presley, J.F.2    Maxfield, F.R.3
  • 63
    • 79961002971 scopus 로고    scopus 로고
    • A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless and is required for Wnt secretion
    • Harterink M., Port F., Lorenowicz M.J., McGough I.J., Silhankova M., Betist M.C., et al. A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless and is required for Wnt secretion. Nat Cell Biol 2011, 13:914-923.
    • (2011) Nat Cell Biol , vol.13 , pp. 914-923
    • Harterink, M.1    Port, F.2    Lorenowicz, M.J.3    McGough, I.J.4    Silhankova, M.5    Betist, M.C.6
  • 64
    • 69649083104 scopus 로고    scopus 로고
    • Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5
    • Seaman M.N.J., Harbour M.E., Tattersall D., Read E., Bright N. Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5. J Cell Sci 2009, 122:2371-2382.
    • (2009) J Cell Sci , vol.122 , pp. 2371-2382
    • Seaman, M.N.J.1    Harbour, M.E.2    Tattersall, D.3    Read, E.4    Bright, N.5
  • 65
    • 33744943284 scopus 로고    scopus 로고
    • The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain
    • Shi H., Rojas R., Bonifacino J.S., Hurley J.H. The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain. Nat Struct Mol Biol 2006, 13:540-548.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 540-548
    • Shi, H.1    Rojas, R.2    Bonifacino, J.S.3    Hurley, J.H.4
  • 66
    • 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.J., Owen D.J. Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly. Nat Struct Mol Biol 2005, 12:594-602.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 594-602
    • Collins, B.M.1    Skinner, C.F.2    Watson, P.J.3    Seaman, M.N.J.4    Owen, D.J.5
  • 67
    • 79956366497 scopus 로고    scopus 로고
    • VPS29 is not an active metallo-phosphatase but is a rigid scaffold required for retromer interaction with accessory proteins
    • Swarbrick J.D., Shaw D.J., Chhabra S., Ghai R., Valkov E., Norwood S.J., et al. VPS29 is not an active metallo-phosphatase but is a rigid scaffold required for retromer interaction with accessory proteins. PLoS ONE 2011, 6:e20420.
    • (2011) PLoS ONE , vol.6
    • Swarbrick, J.D.1    Shaw, D.J.2    Chhabra, S.3    Ghai, R.4    Valkov, E.5    Norwood, S.J.6
  • 68
    • 34547796509 scopus 로고    scopus 로고
    • Identification of a novel conserved sorting motif required for retromer-mediated endosome-to-TGN retrieval
    • Seaman M.N.J. Identification of a novel conserved sorting motif required for retromer-mediated endosome-to-TGN retrieval. J Cell Sci 2007, 120:2378-2389.
    • (2007) J Cell Sci , vol.120 , pp. 2378-2389
    • Seaman, M.N.J.1
  • 69
    • 77149155327 scopus 로고    scopus 로고
    • Retromer-mediated direct sorting is required for proper endosomal recycling of the mammalian iron transporter DMT1
    • Tabuchi M., Yanatori I., Kawai Y., Kishi F. Retromer-mediated direct sorting is required for proper endosomal recycling of the mammalian iron transporter DMT1. J Cell Sci 2010, 123:756-766.
    • (2010) J Cell Sci , vol.123 , pp. 756-766
    • Tabuchi, M.1    Yanatori, I.2    Kawai, Y.3    Kishi, F.4
  • 70
    • 84863011338 scopus 로고    scopus 로고
    • Retromer binds the FANSHY sorting motif in SorLA to regulate amyloid precursor protein sorting and processing
    • Fjorback A.W., Seaman M., Gustafsen C., Mehmedbasic A., Gokool S., Wu C., et al. Retromer binds the FANSHY sorting motif in SorLA to regulate amyloid precursor protein sorting and processing. J Neurosci 2012, 32:1467-1480.
    • (2012) J Neurosci , vol.32 , pp. 1467-1480
    • Fjorback, A.W.1    Seaman, M.2    Gustafsen, C.3    Mehmedbasic, A.4    Gokool, S.5    Wu, C.6
  • 72
    • 0035985175 scopus 로고    scopus 로고
    • Down-regulation of protease-activated receptor-1 is regulated by sorting nexin 1
    • Wang Y., Zhou Y., Szabo K., Haft C.R., Trejo J. Down-regulation of protease-activated receptor-1 is regulated by sorting nexin 1. Mol Biol Cell 2002, 13:1965-1976.
    • (2002) Mol Biol Cell , vol.13 , pp. 1965-1976
    • Wang, Y.1    Zhou, Y.2    Szabo, K.3    Haft, C.R.4    Trejo, J.5
  • 73
    • 77951718320 scopus 로고    scopus 로고
    • Regulation of P2Y(1) receptor traffic by sorting nexin 1 is retromer-independent
    • Nisar S., Kelly E., Cullen P.J., Mundell S.J. Regulation of P2Y(1) receptor traffic by sorting nexin 1 is retromer-independent. Traffic 2010, 11:508-519.
    • (2010) Traffic , vol.11 , pp. 508-519
    • Nisar, S.1    Kelly, E.2    Cullen, P.J.3    Mundell, S.J.4
  • 74
    • 11144229682 scopus 로고    scopus 로고
    • A library of 7TM receptor C-terminal tails. Interactions with the proposed post-endocytic sorting proteins ERM-binding phosphoprotein 50 (EBP50), N-ethylmaleimide-sensitive factor (NSF), sorting nexin 1 (SNX1), and G protein-coupled receptor-associated sorting protein (GASP)
    • Heydorn A., Sondergaard B.P., Ersboll B., Holst B., Nielsen F.C., Haft C.R., et al. A library of 7TM receptor C-terminal tails. Interactions with the proposed post-endocytic sorting proteins ERM-binding phosphoprotein 50 (EBP50), N-ethylmaleimide-sensitive factor (NSF), sorting nexin 1 (SNX1), and G protein-coupled receptor-associated sorting protein (GASP). J Biol Chem 2004, 279:54291-54303.
    • (2004) J Biol Chem , vol.279 , pp. 54291-54303
    • Heydorn, A.1    Sondergaard, B.P.2    Ersboll, B.3    Holst, B.4    Nielsen, F.C.5    Haft, C.R.6
  • 75
    • 34247143246 scopus 로고    scopus 로고
    • Grd19/Snx3p functions as a cargo-specific adapter for retromer-dependent endocytic recycling
    • Strochlic T.I., Setty T.G., Sitaram A., Burd C.G. Grd19/Snx3p functions as a cargo-specific adapter for retromer-dependent endocytic recycling. J Cell Biol 2007, 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
  • 76
    • 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 1998, 140:577-590.
    • (1998) J Cell Biol , vol.140 , pp. 577-590
    • Voos, W.1    Stevens, T.H.2
  • 77
    • 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.B. Retromer and the sorting nexins Snx4/41/42 mediate distinct retrieval pathways from yeast endosomes. EMBO J 2003, 22:548-557.
    • (2003) EMBO J , vol.22 , pp. 548-557
    • Hettema, E.H.1    Lewis, M.J.2    Black, M.W.3    Pelham, H.R.B.4
  • 79
    • 79957914861 scopus 로고    scopus 로고
    • SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors
    • Temkin P., Lauffer B., Jäger S., Cimermancic P., Krogan N.J., von Zastrow M. SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors. Nat Cell Biol 2011, 13:715-721.
    • (2011) Nat Cell Biol , vol.13 , pp. 715-721
    • Temkin, P.1    Lauffer, B.2    Jäger, S.3    Cimermancic, P.4    Krogan, N.J.5    von Zastrow, M.6
  • 80
    • 0038025375 scopus 로고    scopus 로고
    • A developmentally regulated and psychostimulant-inducible novel rat gene mrt1 encoding PDZ-PX proteins isolated in the neocortex
    • Kajii Y., Muraoka S., Hiraoka S., Fujiyama K., Umino A., Nishikawa T. A developmentally regulated and psychostimulant-inducible novel rat gene mrt1 encoding PDZ-PX proteins isolated in the neocortex. Mol Psychiatry 2003, 8:434-444.
    • (2003) Mol Psychiatry , vol.8 , pp. 434-444
    • Kajii, Y.1    Muraoka, S.2    Hiraoka, S.3    Fujiyama, K.4    Umino, A.5    Nishikawa, T.6
  • 81
    • 79956337233 scopus 로고    scopus 로고
    • Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases
    • Ghai R., Mobli M., Norwood S.J., Bugarcic A., Teasdale R.D., King G.F., et al. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Proc Natl Acad Sci U S A 2011, 108:7763-7768.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 7763-7768
    • Ghai, R.1    Mobli, M.2    Norwood, S.J.3    Bugarcic, A.4    Teasdale, R.D.5    King, G.F.6
  • 82
    • 79954992086 scopus 로고    scopus 로고
    • Mechanism underlying selective regulation of G protein-gated inwardly rectifying potassium channels by the psychostimulant-sensitive sorting nexin 27
    • Balana B., Maslennikov I., Kwiatkowski W., Stern K.M., Bahima L., Choe S., et al. Mechanism underlying selective regulation of G protein-gated inwardly rectifying potassium channels by the psychostimulant-sensitive sorting nexin 27. Proc Natl Acad Sci U S A 2011, 108:5831-5836.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 5831-5836
    • Balana, B.1    Maslennikov, I.2    Kwiatkowski, W.3    Stern, K.M.4    Bahima, L.5    Choe, S.6
  • 84
    • 9444267090 scopus 로고    scopus 로고
    • New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a receptor splice variant: roles in receptor targeting
    • Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W., et al. New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a receptor splice variant: roles in receptor targeting. J Cell Sci 2004, 117:5367-5379.
    • (2004) J Cell Sci , vol.117 , pp. 5367-5379
    • Joubert, L.1    Hanson, B.2    Barthet, G.3    Sebben, M.4    Claeysen, S.5    Hong, W.6
  • 85
    • 77955866103 scopus 로고    scopus 로고
    • SNX27 mediates PDZ-directed sorting from endosomes to the plasma membrane
    • Lauffer B.E.L., Melero C., Temkin P., Lei C., Hong W., Kortemme T., et al. SNX27 mediates PDZ-directed sorting from endosomes to the plasma membrane. J Cell Biol 2010, 190:565-574.
    • (2010) J Cell Biol , vol.190 , pp. 565-574
    • Lauffer, B.E.L.1    Melero, C.2    Temkin, P.3    Lei, C.4    Hong, W.5    Kortemme, T.6
  • 87
    • 34250665428 scopus 로고    scopus 로고
    • Proteomics identification of sorting nexin 27 as a diacylglycerol kinase zeta-associated protein: new diacylglycerol kinase roles in endocytic recycling
    • Rincón E., Santos T., Avila-Flores A., Albar J.P., Lalioti V., Lei C., et al. Proteomics identification of sorting nexin 27 as a diacylglycerol kinase zeta-associated protein: new diacylglycerol kinase roles in endocytic recycling. Mol Cell Proteomics 2007, 6:1073-1087.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1073-1087
    • Rincón, E.1    Santos, T.2    Avila-Flores, A.3    Albar, J.P.4    Lalioti, V.5    Lei, C.6
  • 89
    • 84861949426 scopus 로고    scopus 로고
    • SNX17 protects integrins from degradation by sorting between lysosomal and recycling pathways
    • Steinberg F., Heesom K.J., Bass M.D., Cullen P.J. SNX17 protects integrins from degradation by sorting between lysosomal and recycling pathways. J Cell Biol 2012, 197:219-230.
    • (2012) J Cell Biol , vol.197 , pp. 219-230
    • Steinberg, F.1    Heesom, K.J.2    Bass, M.D.3    Cullen, P.J.4
  • 90
    • 84861622962 scopus 로고    scopus 로고
    • Sorting nexin 17 prevents lysosomal degradation of beta1 integrins by binding to the beta1-integrin tail
    • Bottcher R.T., Stremmel C., Meves A., Meyer H., Widmaier M., Tseng H.Y., et al. Sorting nexin 17 prevents lysosomal degradation of beta1 integrins by binding to the beta1-integrin tail. Nat Cell Biol 2012, 14:584-592.
    • (2012) Nat Cell Biol , vol.14 , pp. 584-592
    • Bottcher, R.T.1    Stremmel, C.2    Meves, A.3    Meyer, H.4    Widmaier, M.5    Tseng, H.Y.6
  • 91
    • 38849154635 scopus 로고    scopus 로고
    • SNX1 defines an early endosomal recycling exit for sortilin and mannose 6-phosphate receptors
    • Mari M., Bujny M.V., Zeuschner D., Geerts W.J., Griffith J., Petersen C.M., et al. SNX1 defines an early endosomal recycling exit for sortilin and mannose 6-phosphate receptors. Traffic 2008, 9:380-393.
    • (2008) Traffic , vol.9 , pp. 380-393
    • Mari, M.1    Bujny, M.V.2    Zeuschner, D.3    Geerts, W.J.4    Griffith, J.5    Petersen, C.M.6
  • 92
    • 7744230736 scopus 로고    scopus 로고
    • ACAP1 promotes endocytic recycling by recognizing recycling sorting signals
    • Dai J., Li J., Bos E., Porcionatto M., Premont R.T., Bourgoin S., et al. ACAP1 promotes endocytic recycling by recognizing recycling sorting signals. Dev Cell 2004, 7:771-776.
    • (2004) Dev Cell , vol.7 , pp. 771-776
    • Dai, J.1    Li, J.2    Bos, E.3    Porcionatto, M.4    Premont, R.T.5    Bourgoin, S.6
  • 93
    • 34547567210 scopus 로고    scopus 로고
    • An ACAP1-containing clathrin coat complex for endocytic recycling
    • Li J., Peters P.J., Bai M., Dai J., Bos E., Kirchhausen T., et al. An ACAP1-containing clathrin coat complex for endocytic recycling. J Cell Biol 2007, 178:453-464.
    • (2007) J Cell Biol , vol.178 , pp. 453-464
    • Li, J.1    Peters, P.J.2    Bai, M.3    Dai, J.4    Bos, E.5    Kirchhausen, T.6


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