메뉴 건너뛰기




Volumn 72, Issue 18, 2015, Pages 3441-3455

Biogenesis of endosome-derived transport carriers

Author keywords

Endosome; Fission; Recycling; Retrograde; Retromer; SNX BAR; Sorting

Indexed keywords

BINDING PROTEIN; CARRIER PROTEIN; COAT PROTEIN; ENDOSOME DERIVED TRANSPORT CARRIER; PROTEIN BIN AMPHIPHYSIN RVS; SORTING NEXIN; UNCLASSIFIED DRUG; VESICULAR TRANSPORT PROTEIN;

EID: 84940467342     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-015-1935-x     Document Type: Review
Times cited : (40)

References (147)
  • 1
    • 84903745685 scopus 로고    scopus 로고
    • The complex ultrastructure of the endolysosomal system
    • 10.1101/cshperspect.a016857 24851870
    • Klumperman J, Raposo G (2014) The complex ultrastructure of the endolysosomal system. Cold Spring Harb Perspect Biol 6(10):a016857. doi: 10.1101/cshperspect.a016857
    • (2014) Cold Spring Harb Perspect Biol , vol.6 , Issue.10 , pp. a016857
    • Klumperman, J.1    Raposo, G.2
  • 2
    • 79960225411 scopus 로고    scopus 로고
    • The ESCRT pathway
    • 10.1016/j.devcel.2011.05.015 1:CAS:528:DC%2BC3MXptVSqsr8%3D 21763610
    • Henne WM, Buchkovich NJ, Emr SD (2011) The ESCRT pathway. Dev Cell 21(1):77-91. doi: 10.1016/j.devcel.2011.05.015
    • (2011) Dev Cell , vol.21 , Issue.1 , pp. 77-91
    • Henne, W.M.1    Buchkovich, N.J.2    Emr, S.D.3
  • 3
    • 0035881462 scopus 로고    scopus 로고
    • A large family of endosome-localized proteins related to sorting nexin 1
    • 1222026 1:CAS:528:DC%2BD3MXmsFSht7c%3D 11485546
    • Teasdale RD, Loci D, Houghton F, Karlsson L, Gleeson PA (2001) A large family of endosome-localized proteins related to sorting nexin 1. Biochem J 358(Pt 1):7-16
    • (2001) Biochem J , vol.358 , pp. 7-16
    • Teasdale, R.D.1    Loci, D.2    Houghton, F.3    Karlsson, L.4    Gleeson, P.A.5
  • 4
    • 84921628946 scopus 로고    scopus 로고
    • Retromer and sorting nexins in endosomal sorting
    • 10.1042/BST20140290 1:CAS:528:DC%2BC2MXhsV2ms7s%3D 25619244
    • Gallon M, Cullen PJ (2015) Retromer and sorting nexins in endosomal sorting. Biochem Soc Trans 43(1):33-47. doi: 10.1042/BST20140290
    • (2015) Biochem Soc Trans , vol.43 , Issue.1 , pp. 33-47
    • Gallon, M.1    Cullen, P.J.2
  • 6
    • 84895765280 scopus 로고    scopus 로고
    • Fission of SNX-BAR-coated endosomal retrograde transport carriers is promoted by the dynamin-related protein Vps1
    • 10.1083/jcb.201309084 3941054 1:CAS:528:DC%2BC2cXkt1eitL0%3D 24567361
    • Chi RJ, Liu J, West M, Wang J, Odorizzi G, Burd CG (2014) Fission of SNX-BAR-coated endosomal retrograde transport carriers is promoted by the dynamin-related protein Vps1. J Cell Biol 204(5):793-806. doi: 10.1083/jcb.201309084
    • (2014) J Cell Biol , vol.204 , Issue.5 , pp. 793-806
    • Chi, R.J.1    Liu, J.2    West, M.3    Wang, J.4    Odorizzi, G.5    Burd, C.G.6
  • 7
    • 84890850009 scopus 로고    scopus 로고
    • Linear aggregation of proteins on the membrane as a prelude to membrane remodeling
    • 10.1073/pnas.1309819110 3870675 1:CAS:528:DC%2BC2cXnsVKksg%3D%3D 24284177
    • Simunovic M, Srivastava A, Voth GA (2013) Linear aggregation of proteins on the membrane as a prelude to membrane remodeling. Proc Natl Acad Sci USA 110(51):20396-20401. doi: 10.1073/pnas.1309819110
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.51 , pp. 20396-20401
    • Simunovic, M.1    Srivastava, A.2    Voth, G.A.3
  • 8
    • 83255187127 scopus 로고    scopus 로고
    • SNX-BAR-mediated endosome tubulation is co-ordinated with endosome maturation
    • 10.1111/j.1600-0854.2011.01297.x 21973056
    • van Weering JR, Verkade P, Cullen PJ (2012) SNX-BAR-mediated endosome tubulation is co-ordinated with endosome maturation. Traffic 13(1):94-107. doi: 10.1111/j.1600-0854.2011.01297.x
    • (2012) Traffic , vol.13 , Issue.1 , pp. 94-107
    • Van Weering, J.R.1    Verkade, P.2    Cullen, P.J.3
  • 10
    • 84891658400 scopus 로고    scopus 로고
    • Retromer: A master conductor of endosome sorting
    • perspectives in biology 6
    • Burd C, Cullen PJ (2014) Retromer: a master conductor of endosome sorting. Cold Spring Harbor perspectives in biology 6(2). doi: 10.1101/cshperspect.a016774
    • (2014) Cold Spring Harbor , Issue.2
    • Burd, C.1    Cullen, P.J.2
  • 11
    • 84255208762 scopus 로고    scopus 로고
    • Sorting nexins provide diversity for retromer-dependent trafficking events
    • 10.1038/ncb2374 1:CAS:528:DC%2BC3MXhs1Gks7rJ
    • Cullen PJ, Korswagen HC (2012) Sorting nexins provide diversity for retromer-dependent trafficking events. Nat Cell Biol 14(1):29-37. doi: 10.1038/ncb2374
    • (2012) Nat Cell Biol , vol.14 , Issue.1 , pp. 29-37
    • Cullen, P.J.1    Korswagen, H.C.2
  • 12
    • 84872183810 scopus 로고    scopus 로고
    • The retromer complex - Endosomal protein recycling and beyond
    • 10.1242/jcs.103440 3517092 1:CAS:528:DC%2BC3sXhs1Ohtrg%3D 23148298
    • Seaman MN (2012) The retromer complex - endosomal protein recycling and beyond. J Cell Sci 125(Pt 20):4693-4702. doi: 10.1242/jcs.103440
    • (2012) J Cell Sci , vol.125 , pp. 4693-4702
    • Seaman, M.N.1
  • 13
    • 0035172729 scopus 로고    scopus 로고
    • Vps26p, a component of retromer, directs the interactions of Vps35p in endosome-to-Golgi retrieval
    • 60170 1:CAS:528:DC%2BD3MXns1Cht7g%3D 11598206
    • Reddy JV, Seaman MN (2001) Vps26p, a component of retromer, directs the interactions of Vps35p in endosome-to-Golgi retrieval. Mol Biol Cell 12(10):3242-3256
    • (2001) Mol Biol Cell , vol.12 , Issue.10 , pp. 3242-3256
    • Reddy, J.V.1    Seaman, M.N.2
  • 14
    • 0031823307 scopus 로고    scopus 로고
    • A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast
    • 2148169 1:CAS:528:DyaK1cXlsVWlt78%3D 9700157
    • Seaman MN, McCaffery JM, Emr SD (1998) A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. J Cell Biol 142(3):665-681
    • (1998) J Cell Biol , vol.142 , Issue.3 , pp. 665-681
    • Seaman, M.N.1    McCaffery, J.M.2    Emr, S.D.3
  • 15
    • 22144490854 scopus 로고    scopus 로고
    • Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly
    • 1:CAS:528:DC%2BD2MXlsl2iu7w%3D 15965486
    • Collins BM, Skinner CF, Watson PJ, Seaman MN, Owen DJ (2005) Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly. Nat Struct Mol Biol 12(7):594-602
    • (2005) Nat Struct Mol Biol , vol.12 , Issue.7 , pp. 594-602
    • Collins, B.M.1    Skinner, C.F.2    Watson, P.J.3    Seaman, M.N.4    Owen, D.J.5
  • 16
    • 38849094724 scopus 로고    scopus 로고
    • Structure of Vps26B and mapping of its interaction with the retromer protein complex
    • 1:CAS:528:DC%2BD1cXisVakurw%3D 18088321
    • Collins BM, Norwood SJ, Kerr MC, Mahony D, Seaman MN, Teasdale RD, Owen DJ (2008) Structure of Vps26B and mapping of its interaction with the retromer protein complex. Traffic 9(3):366-379
    • (2008) Traffic , vol.9 , Issue.3 , pp. 366-379
    • Collins, B.M.1    Norwood, S.J.2    Kerr, M.C.3    Mahony, D.4    Seaman, M.N.5    Teasdale, R.D.6    Owen, D.J.7
  • 18
    • 36549042931 scopus 로고    scopus 로고
    • A SNARE-adaptor interaction is a new mode of cargo recognition in clathrin-coated vesicles
    • 10.1038/nature06353 1:CAS:528:DC%2BD2sXhtlCrtb7J 18033301
    • Miller SE, Collins BM, McCoy AJ, Robinson MS, Owen DJ (2007) A SNARE-adaptor interaction is a new mode of cargo recognition in clathrin-coated vesicles. Nature 450(7169):570-574. doi: 10.1038/nature06353
    • (2007) Nature , vol.450 , Issue.7169 , pp. 570-574
    • Miller, S.E.1    Collins, B.M.2    McCoy, A.J.3    Robinson, M.S.4    Owen, D.J.5
  • 19
    • 78650030472 scopus 로고    scopus 로고
    • Assembly and solution structure of the core retromer protein complex
    • 10.1111/j.1600-0854.2010.01124.x 20875039
    • Norwood SJ, Shaw DJ, Cowieson NP, Owen DJ, Teasdale RD, Collins BM (2010) Assembly and solution structure of the core retromer protein complex. Traffic. doi: 10.1111/j.1600-0854.2010.01124.x
    • (2010) Traffic
    • Norwood, S.J.1    Shaw, D.J.2    Cowieson, N.P.3    Owen, D.J.4    Teasdale, R.D.5    Collins, B.M.6
  • 20
    • 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
    • 276174 1:CAS:528:DyaK2sXlvVWgs7s%3D 9285823
    • Horazdovsky BF, Davies BA, Seaman MN, McLaughlin SA, Yoon S, Emr SD (1997) A sorting nexin-1 homologue, Vps5p, forms a complex with Vps17p and is required for recycling the vacuolar protein-sorting receptor. Mol Biol Cell 8(8):1529-1541
    • (1997) Mol Biol Cell , vol.8 , Issue.8 , pp. 1529-1541
    • Horazdovsky, B.F.1    Davies, B.A.2    Seaman, M.N.3    McLaughlin, S.A.4    Yoon, S.5    Emr, S.D.6
  • 21
    • 84863535520 scopus 로고    scopus 로고
    • Rab GTPase regulation of retromer-mediated cargo export during endosome maturation
    • 10.1091/mbc.E11-11-0915 1:CAS:528:DC%2BC38XhtVOrsLrO 22593205
    • Liu TT, Gomez TS, Sackey BK, Billadeau DD, Burd CG (2012) Rab GTPase regulation of retromer-mediated cargo export during endosome maturation. Mol Biol Cell 23(13):2505-2515. doi: 10.1091/mbc.E11-11-0915
    • (2012) Mol Biol Cell , vol.23 , Issue.13 , pp. 2505-2515
    • Liu, T.T.1    Gomez, T.S.2    Sackey, B.K.3    Billadeau, D.D.4    Burd, C.G.5
  • 22
    • 33846587097 scopus 로고    scopus 로고
    • Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors
    • 1800681 1:CAS:528:DC%2BD2sXhtFGhur4%3D 17101778
    • Rojas R, Kametaka S, Haft CR, Bonifacino JS (2007) Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors. Mol Cell Biol 27(3):1112-1124
    • (2007) Mol Cell Biol , vol.27 , Issue.3 , pp. 1112-1124
    • Rojas, R.1    Kametaka, S.2    Haft, C.R.3    Bonifacino, J.S.4
  • 23
    • 33846811334 scopus 로고    scopus 로고
    • A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer
    • 1:CAS:528:DC%2BD2sXht1Gms7s%3D 17148574
    • Wassmer T, Attar N, Bujny MV, Oakley J, Traer CJ, Cullen PJ (2007) A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer. J Cell Sci 120(Pt 1):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
  • 24
    • 79955548766 scopus 로고    scopus 로고
    • Evolutionary reconstruction of the retromer complex and its function in Trypanosoma brucei
    • 10.1242/jcs.081596 3078816 1:CAS:528:DC%2BC3MXnt1Cjsrk%3D 21502137
    • Koumandou VL, Klute MJ, Herman EK, Nunez-Miguel R, Dacks JB, Field MC (2011) Evolutionary reconstruction of the retromer complex and its function in Trypanosoma brucei. J Cell Sci 124(Pt 9):1496-1509. doi: 10.1242/jcs.081596
    • (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
  • 25
    • 0030897485 scopus 로고    scopus 로고
    • Endosome to Golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the VPS29, VPS30, and VPS35 gene products (in process citation)
    • 2139870 1:CAS:528:DyaK2sXisVKitrw%3D 9105038
    • Seaman MN, Marcusson EG, Cereghino JL, Emr SD (1997) Endosome to Golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the VPS29, VPS30, and VPS35 gene products (in process citation). J Cell Biol 137(1):79-92
    • (1997) J Cell Biol , vol.137 , Issue.1 , pp. 79-92
    • Seaman, M.N.1    Marcusson, E.G.2    Cereghino, J.L.3    Emr, S.D.4
  • 26
    • 67650218762 scopus 로고    scopus 로고
    • The retromer coat complex coordinates endosomal sorting and dynein-mediated transport, with carrier recognition by the trans-Golgi network
    • 10.1016/j.devcel.2009.04.016 2714578 1:CAS:528:DC%2BD1MXpsV2msbc%3D 19619496
    • Wassmer T, Attar N, Harterink M, van Weering JR, Traer CJ, Oakley J, Goud B, Stephens DJ, Verkade P, Korswagen HC, Cullen PJ (2009) The retromer coat complex coordinates endosomal sorting and dynein-mediated transport, with carrier recognition by the trans-Golgi network. Dev Cell 17(1):110-122. doi: 10.1016/j.devcel.2009.04.016
    • (2009) Dev Cell , vol.17 , Issue.1 , pp. 110-122
    • Wassmer, T.1    Attar, N.2    Harterink, M.3    Van Weering, J.R.4    Traer, C.J.5    Oakley, J.6    Goud, B.7    Stephens, D.J.8    Verkade, P.9    Korswagen, H.C.10    Cullen, P.J.11
  • 28
    • 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
    • 10.1242/jcs.048686 2704877 1:CAS:528:DC%2BD1MXpvFGmurk%3D 19531583
    • Seaman MN, Harbour ME, Tattersall D, Read E, Bright N (2009) 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 122(Pt 14):2371-2382. doi: 10.1242/jcs.048686
    • (2009) J Cell Sci , vol.122 , pp. 2371-2382
    • Seaman, M.N.1    Harbour, M.E.2    Tattersall, D.3    Read, E.4    Bright, N.5
  • 29
    • 84891919318 scopus 로고    scopus 로고
    • A mechanism for retromer endosomal coat complex assembly with cargo
    • 10.1073/pnas.1316482111 3890810 1:CAS:528:DC%2BC2cXps1Gksw%3D%3D 24344282
    • Harrison MS, Hung CS, Liu TT, Christiano R, Walther TC, Burd CG (2014) A mechanism for retromer endosomal coat complex assembly with cargo. Proc Natl Acad Sci USA 111(1):267-272. doi: 10.1073/pnas.1316482111
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.1 , pp. 267-272
    • Harrison, M.S.1    Hung, C.S.2    Liu, T.T.3    Christiano, R.4    Walther, T.C.5    Burd, C.G.6
  • 30
    • 37749037456 scopus 로고    scopus 로고
    • Human subtelomeric WASH genes encode a new subclass of the WASP family
    • 10.1371/journal.pgen.0030237 2151093 18159949
    • Linardopoulou EV, Parghi SS, Friedman C, Osborn GE, Parkhurst SM, Trask BJ (2007) Human subtelomeric WASH genes encode a new subclass of the WASP family. PLoS Genet 3(12):e237. doi: 10.1371/journal.pgen.0030237
    • (2007) PLoS Genet , vol.3 , Issue.12 , pp. e237
    • Linardopoulou, E.V.1    Parghi, S.S.2    Friedman, C.3    Osborn, G.E.4    Parkhurst, S.M.5    Trask, B.J.6
  • 31
    • 71549167371 scopus 로고    scopus 로고
    • A FAM21-containing WASH complex regulates retromer-dependent sorting
    • 10.1016/j.devcel.2009.09.009 2803077 1:CAS:528:DC%2BD1MXhsFKltb7O 19922874
    • Gomez TS, Billadeau DD (2009) A FAM21-containing WASH complex regulates retromer-dependent sorting. Dev Cell 17(5):699-711. doi: 10.1016/j.devcel.2009.09.009
    • (2009) Dev Cell , vol.17 , Issue.5 , pp. 699-711
    • Gomez, T.S.1    Billadeau, D.D.2
  • 32
    • 71549146571 scopus 로고    scopus 로고
    • The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex
    • 10.1016/j.devcel.2009.09.010 1:CAS:528:DC%2BD1MXhsFKltb7P 19922875
    • Derivery E, Sousa C, Gautier JJ, Lombard B, Loew D, Gautreau A (2009) The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex. Dev Cell 17(5):712-723. doi: 10.1016/j.devcel.2009.09.010
    • (2009) Dev Cell , vol.17 , Issue.5 , pp. 712-723
    • Derivery, E.1    Sousa, C.2    Gautier, J.J.3    Lombard, B.4    Loew, D.5    Gautreau, A.6
  • 33
    • 79959427994 scopus 로고    scopus 로고
    • Actin polymerization driven by WASH causes V-ATPase retrieval and vesicle neutralization before exocytosis
    • 10.1083/jcb.201009119 3105540 1:CAS:528:DC%2BC3MXnt1Knt7w%3D 21606208
    • Carnell M, Zech T, Calaminus SD, Ura S, Hagedorn M, Johnston SA, May RC, Soldati T, Machesky LM, Insall RH (2011) Actin polymerization driven by WASH causes V-ATPase retrieval and vesicle neutralization before exocytosis. J Cell Biol 193(5):831-839. doi: 10.1083/jcb.201009119
    • (2011) J Cell Biol , vol.193 , Issue.5 , pp. 831-839
    • Carnell, M.1    Zech, T.2    Calaminus, S.D.3    Ura, S.4    Hagedorn, M.5    Johnston, S.A.6    May, R.C.7    Soldati, T.8    Machesky, L.M.9    Insall, R.H.10
  • 34
    • 84886749671 scopus 로고    scopus 로고
    • Retromer-mediated endosomal protein sorting: All WASHed up!
    • 10.1016/j.tcb.2013.04.010 3924425 1:CAS:528:DC%2BC3sXoslWmsbo%3D 23721880
    • Seaman MN, Gautreau A, Billadeau DD (2013) Retromer-mediated endosomal protein sorting: all WASHed up! Trends Cell Biol 23(11):522-528. doi: 10.1016/j.tcb.2013.04.010
    • (2013) Trends Cell Biol , vol.23 , Issue.11 , pp. 522-528
    • Seaman, M.N.1    Gautreau, A.2    Billadeau, D.D.3
  • 35
    • 84862637856 scopus 로고    scopus 로고
    • Actin polymerization controls the organization of WASH domains at the surface of endosomes
    • 10.1371/journal.pone.0039774 3380866 1:CAS:528:DC%2BC38XpsVWmtbw%3D 22737254
    • Derivery E, Helfer E, Henriot V, Gautreau A (2012) Actin polymerization controls the organization of WASH domains at the surface of endosomes. PLoS ONE 7(6):e39774. doi: 10.1371/journal.pone.0039774
    • (2012) PLoS ONE , vol.7 , Issue.6 , pp. e39774
    • Derivery, E.1    Helfer, E.2    Henriot, V.3    Gautreau, A.4
  • 36
    • 77949801905 scopus 로고    scopus 로고
    • WASH and the Arp2/3 complex regulate endosome shape and trafficking
    • 10.1002/cm.20437 2887680 1:CAS:528:DC%2BC3cXkvFOntrg%3D 20175130
    • Duleh SN, Welch MD (2010) WASH and the Arp2/3 complex regulate endosome shape and trafficking. Cytoskeleton 67(3):193-206. doi: 10.1002/cm.20437
    • (2010) Cytoskeleton , vol.67 , Issue.3 , pp. 193-206
    • Duleh, S.N.1    Welch, M.D.2
  • 37
    • 84870520072 scopus 로고    scopus 로고
    • Trafficking defects in WASH-knockout fibroblasts originate from collapsed endosomal and lysosomal networks
    • 10.1091/mbc.E12-02-0101 3418315 1:CAS:528:DC%2BC38Xht1arur%2FK 22718907
    • Gomez TS, Gorman JA, de Narvajas AA, Koenig AO, Billadeau DD (2012) Trafficking defects in WASH-knockout fibroblasts originate from collapsed endosomal and lysosomal networks. Mol Biol Cell 23(16):3215-3228. doi: 10.1091/mbc.E12-02-0101
    • (2012) Mol Biol Cell , vol.23 , Issue.16 , pp. 3215-3228
    • Gomez, T.S.1    Gorman, J.A.2    De Narvajas, A.A.3    Koenig, A.O.4    Billadeau, D.D.5
  • 38
    • 79251527516 scopus 로고    scopus 로고
    • Sequence-dependent sorting of recycling proteins by actin-stabilized endosomal microdomains
    • 10.1016/j.cell.2010.10.003 3058345 1:CAS:528:DC%2BC3cXhsVygsLfN 21111236
    • Puthenveedu MA, Lauffer B, Temkin P, Vistein R, Carlton P, Thorn K, Taunton J, Weiner OD, Parton RG, von Zastrow M (2010) Sequence-dependent sorting of recycling proteins by actin-stabilized endosomal microdomains. Cell 143(5):761-773. doi: 10.1016/j.cell.2010.10.003
    • (2010) Cell , vol.143 , Issue.5 , pp. 761-773
    • Puthenveedu, M.A.1    Lauffer, B.2    Temkin, P.3    Vistein, R.4    Carlton, P.5    Thorn, K.6    Taunton, J.7    Weiner, O.D.8    Parton, R.G.9    Von Zastrow, M.10
  • 39
    • 84862573732 scopus 로고    scopus 로고
    • Multiple repeat elements within the FAM21 tail link the WASH actin regulatory complex to the retromer
    • 10.1091/mbc.E11-12-1059 3374753 1:CAS:528:DC%2BC38XhtVOku77P 22513087
    • Jia D, Gomez TS, Billadeau DD, Rosen MK (2012) Multiple repeat elements within the FAM21 tail link the WASH actin regulatory complex to the retromer. Mol Biol Cell 23(12):2352-2361. doi: 10.1091/mbc.E11-12-1059
    • (2012) Mol Biol Cell , vol.23 , Issue.12 , pp. 2352-2361
    • Jia, D.1    Gomez, T.S.2    Billadeau, D.D.3    Rosen, M.K.4
  • 40
    • 84903376048 scopus 로고    scopus 로고
    • Active organization of membrane constituents in living cells
    • 10.1016/j.ceb.2014.05.007 1:CAS:528:DC%2BC2cXhtlGmt7rN 24975942
    • Rao M, Mayor S (2014) Active organization of membrane constituents in living cells. Curr Opin Cell Biol 29:126-132. doi: 10.1016/j.ceb.2014.05.007
    • (2014) Curr Opin Cell Biol , vol.29 , pp. 126-132
    • Rao, M.1    Mayor, S.2
  • 41
    • 0037415752 scopus 로고    scopus 로고
    • Retromer and the sorting nexins Snx4/41/42 mediate distinct retrieval pathways from yeast endosomes
    • 140746 1:CAS:528:DC%2BD3sXitlKksrc%3D 12554655
    • Hettema EH, Lewis MJ, Black MW, Pelham HR (2003) Retromer and the sorting nexins Snx4/41/42 mediate distinct retrieval pathways from yeast endosomes. EMBO J 22(3):548-557
    • (2003) EMBO J , vol.22 , Issue.3 , pp. 548-557
    • Hettema, E.H.1    Lewis, M.J.2    Black, M.W.3    Pelham, H.R.4
  • 43
    • 80655144724 scopus 로고    scopus 로고
    • Two novel WD40 domain-containing proteins, Ere1 and Ere2, function in the retromer-mediated endosomal recycling pathway
    • 10.1091/mbc.E11-05-0440 3204071 1:CAS:528:DC%2BC3MXhsV2qu7bN 21880895
    • Shi Y, Stefan CJ, Rue SM, Teis D, Emr SD (2011) Two novel WD40 domain-containing proteins, Ere1 and Ere2, function in the retromer-mediated endosomal recycling pathway. Mol Biol Cell 22(21):4093-4107. doi: 10.1091/mbc.E11-05-0440
    • (2011) Mol Biol Cell , vol.22 , Issue.21 , pp. 4093-4107
    • Shi, Y.1    Stefan, C.J.2    Rue, S.M.3    Teis, D.4    Emr, S.D.5
  • 44
    • 84880018609 scopus 로고    scopus 로고
    • Microtubule motors mediate endosomal sorting by maintaining functional domain organization
    • 10.1242/jcs.122317 3679488 23549789
    • Hunt SD, Townley AK, Danson CM, Cullen PJ, Stephens DJ (2013) Microtubule motors mediate endosomal sorting by maintaining functional domain organization. J Cell Sci. doi: 10.1242/jcs.122317
    • (2013) J Cell Sci
    • Hunt, S.D.1    Townley, A.K.2    Danson, C.M.3    Cullen, P.J.4    Stephens, D.J.5
  • 45
    • 84883332951 scopus 로고    scopus 로고
    • Reggies/flotillins interact with Rab11a and SNX4 at the tubulovesicular recycling compartment and function in transferrin receptor and E-cadherin trafficking
    • 10.1091/mbc.E12-12-0854 3756921 1:CAS:528:DC%2BC3sXhsVSgtr3I 23825023
    • Solis GP, Hulsbusch N, Radon Y, Katanaev VL, Plattner H, Stuermer CA (2013) Reggies/flotillins interact with Rab11a and SNX4 at the tubulovesicular recycling compartment and function in transferrin receptor and E-cadherin trafficking. Mol Biol Cell 24(17):2689-2702. doi: 10.1091/mbc.E12-12-0854
    • (2013) Mol Biol Cell , vol.24 , Issue.17 , pp. 2689-2702
    • Solis, G.P.1    Hulsbusch, N.2    Radon, Y.3    Katanaev, V.L.4    Plattner, H.5    Stuermer, C.A.6
  • 46
    • 84885660381 scopus 로고    scopus 로고
    • SNX18 tubulates recycling endosomes for autophagosome biogenesis
    • 10.4161/auto.26124 24113029
    • Knaevelsrud H, Carlsson SR, Simonsen A (2013) SNX18 tubulates recycling endosomes for autophagosome biogenesis. Autophagy 9(10):1639-1641. doi: 10.4161/auto.26124
    • (2013) Autophagy , vol.9 , Issue.10 , pp. 1639-1641
    • Knaevelsrud, H.1    Carlsson, S.R.2    Simonsen, A.3
  • 47
    • 45849110080 scopus 로고    scopus 로고
    • SNX18 is an SNX9 paralog that acts as a membrane tubulator in AP-1-positive endosomal trafficking
    • 10.1242/jcs.028530 18411244
    • Haberg K, Lundmark R, Carlsson SR (2008) SNX18 is an SNX9 paralog that acts as a membrane tubulator in AP-1-positive endosomal trafficking. J Cell Sci 121(Pt 9):1495-1505. doi: 10.1242/jcs.028530
    • (2008) J Cell Sci , vol.121 , pp. 1495-1505
    • Haberg, K.1    Lundmark, R.2    Carlsson, S.R.3
  • 48
    • 77952393464 scopus 로고    scopus 로고
    • SNX18 shares a redundant role with SNX9 and modulates endocytic trafficking at the plasma membrane
    • 10.1242/jcs.064170 1:CAS:528:DC%2BC3cXotFGrsbo%3D 20427313
    • Park J, Kim Y, Lee S, Park JJ, Park ZY, Sun W, Kim H, Chang S (2010) SNX18 shares a redundant role with SNX9 and modulates endocytic trafficking at the plasma membrane. J Cell Sci 123(Pt 10):1742-1750. doi: 10.1242/jcs.064170
    • (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    Kim, H.7    Chang, S.8
  • 50
    • 79953158981 scopus 로고    scopus 로고
    • Mitophagy in yeast is independent of mitochondrial fission and requires the stress response gene WHI2
    • 10.1242/jcs.076406 1:CAS:528:DC%2BC3MXnsVelsLY%3D 21429936
    • Mendl N, Occhipinti A, Muller M, Wild P, Dikic I, Reichert AS (2011) Mitophagy in yeast is independent of mitochondrial fission and requires the stress response gene WHI2. J Cell Sci 124(Pt 8):1339-1350. doi: 10.1242/jcs.076406
    • (2011) J Cell Sci , vol.124 , pp. 1339-1350
    • Mendl, N.1    Occhipinti, A.2    Muller, M.3    Wild, P.4    Dikic, I.5    Reichert, A.S.6
  • 51
    • 0037119448 scopus 로고    scopus 로고
    • Cooperative binding of the cytoplasm to vacuole targeting pathway proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre-autophagosomal structure is required for selective autophagy
    • 10.1074/jbc.M204736200 2754692 1:CAS:528:DC%2BD38XmsVKhsbk%3D 12048214
    • Nice DC, Sato TK, Stromhaug PE, Emr SD, Klionsky DJ (2002) Cooperative binding of the cytoplasm to vacuole targeting pathway proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre-autophagosomal structure is required for selective autophagy. J Biol Chem 277(33):30198-30207. doi: 10.1074/jbc.M204736200
    • (2002) J Biol Chem , vol.277 , Issue.33 , pp. 30198-30207
    • Nice, D.C.1    Sato, T.K.2    Stromhaug, P.E.3    Emr, S.D.4    Klionsky, D.J.5
  • 52
    • 67650246357 scopus 로고    scopus 로고
    • Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy
    • 10.1016/j.devcel.2009.06.013 1:CAS:528:DC%2BD1MXpsV2msbk%3D 19619494
    • Okamoto K, Kondo-Okamoto N, Ohsumi Y (2009) Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy. Dev Cell 17(1):87-97. doi: 10.1016/j.devcel.2009.06.013
    • (2009) Dev Cell , vol.17 , Issue.1 , pp. 87-97
    • Okamoto, K.1    Kondo-Okamoto, N.2    Ohsumi, Y.3
  • 53
    • 77957198526 scopus 로고    scopus 로고
    • An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis
    • 10.1083/jcb.200912089 3101592 1:CAS:528:DC%2BC3cXht1ahsbjJ 20855505
    • Mari M, Griffith J, Rieter E, Krishnappa L, Klionsky DJ, Reggiori F (2010) An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis. J Cell Biol 190(6):1005-1022. doi: 10.1083/jcb.200912089
    • (2010) J Cell Biol , vol.190 , Issue.6 , pp. 1005-1022
    • Mari, M.1    Griffith, J.2    Rieter, E.3    Krishnappa, L.4    Klionsky, D.J.5    Reggiori, F.6
  • 54
    • 77950491704 scopus 로고    scopus 로고
    • New insights into the function of Atg9
    • 10.1016/j.febslet.2010.01.020 1:CAS:528:DC%2BC3cXjs12nu7o%3D 20083107
    • Webber JL, Tooze SA (2010) New insights into the function of Atg9. FEBS Lett 584(7):1319-1326. doi: 10.1016/j.febslet.2010.01.020
    • (2010) FEBS Lett , vol.584 , Issue.7 , pp. 1319-1326
    • Webber, J.L.1    Tooze, S.A.2
  • 55
    • 84864991509 scopus 로고    scopus 로고
    • Atg9 vesicles are an important membrane source during early steps of autophagosome formation
    • 10.1083/jcb.201202061 3410421 1:CAS:528:DC%2BC38XhtFaisLbO 22826123
    • Yamamoto H, Kakuta S, Watanabe TM, Kitamura A, Sekito T, Kondo-Kakuta C, Ichikawa R, Kinjo M, Ohsumi Y (2012) Atg9 vesicles are an important membrane source during early steps of autophagosome formation. J Cell Biol 198(2):219-233. doi: 10.1083/jcb.201202061
    • (2012) J Cell Biol , vol.198 , Issue.2 , pp. 219-233
    • Yamamoto, H.1    Kakuta, S.2    Watanabe, T.M.3    Kitamura, A.4    Sekito, T.5    Kondo-Kakuta, C.6    Ichikawa, R.7    Kinjo, M.8    Ohsumi, Y.9
  • 56
    • 84887581571 scopus 로고    scopus 로고
    • TRAPPIII is responsible for vesicular transport from early endosomes to Golgi, facilitating Atg9 cycling in autophagy
    • 10.1242/jcs.131318 1:CAS:528:DC%2BC3sXhvVygsL3M 23986483
    • Shirahama-Noda K, Kira S, Yoshimori T, Noda T (2013) TRAPPIII is responsible for vesicular transport from early endosomes to Golgi, facilitating Atg9 cycling in autophagy. J Cell Sci 126(Pt 21):4963-4973. doi: 10.1242/jcs.131318
    • (2013) J Cell Sci , vol.126 , pp. 4963-4973
    • Shirahama-Noda, K.1    Kira, S.2    Yoshimori, T.3    Noda, T.4
  • 57
    • 78649682788 scopus 로고    scopus 로고
    • Membrane delivery to the yeast autophagosome from the Golgi-endosomal system
    • 10.1091/mbc.E10-05-0457 2982105 1:CAS:528:DC%2BC3cXhsFagsrfO 20861302
    • Ohashi Y, Munro S (2010) Membrane delivery to the yeast autophagosome from the Golgi-endosomal system. Mol Biol Cell 21(22):3998-4008. doi: 10.1091/mbc.E10-05-0457
    • (2010) Mol Biol Cell , vol.21 , Issue.22 , pp. 3998-4008
    • Ohashi, Y.1    Munro, S.2
  • 58
    • 33748461590 scopus 로고    scopus 로고
    • The Phox (PX) domain proteins and membrane traffic
    • 1:CAS:528:DC%2BD28XpsVajsbs%3D 16782399
    • Seet LF, Hong W (2006) The Phox (PX) domain proteins and membrane traffic. Biochim Biophys Acta 1761(8):878-896
    • (2006) Biochim Biophys Acta , vol.1761 , Issue.8 , pp. 878-896
    • Seet, L.F.1    Hong, W.2
  • 59
    • 84055185227 scopus 로고    scopus 로고
    • Insights into the PX (phox-homology) domain and SNX (sorting nexin) protein families: Structures, functions and roles in disease
    • 10.1042/BJ20111226 1:CAS:528:DC%2BC3MXhs1Cgs7jE 22168438
    • Teasdale RD, Collins BM (2012) Insights into the PX (phox-homology) domain and SNX (sorting nexin) protein families: structures, functions and roles in disease. Biochem J 441(1):39-59. doi: 10.1042/BJ20111226
    • (2012) Biochem J , vol.441 , Issue.1 , pp. 39-59
    • Teasdale, R.D.1    Collins, B.M.2
  • 60
    • 34247143246 scopus 로고    scopus 로고
    • Grd19/Snx3p functions as a cargo-specific adapter for retromer-dependent endocytic recycling
    • 2064116 1:CAS:528:DC%2BD2sXktlKltrs%3D 17420293
    • Strochlic TI, Setty TG, Sitaram A, Burd CG (2007) Grd19/Snx3p functions as a cargo-specific adapter for retromer-dependent endocytic recycling. J Cell Biol 177(1):115-125
    • (2007) J Cell Biol , vol.177 , Issue.1 , pp. 115-125
    • Strochlic, T.I.1    Setty, T.G.2    Sitaram, A.3    Burd, C.G.4
  • 61
    • 54749138888 scopus 로고    scopus 로고
    • Hrs and SNX3 functions in sorting and membrane invagination within multivesicular bodies
    • 10.1371/journal.pbio.0060214 2528051 18767904
    • Pons V, Luyet PP, Morel E, Abrami L, van der Goot FG, Parton RG, Gruenberg J (2008) Hrs and SNX3 functions in sorting and membrane invagination within multivesicular bodies. PLoS Biol 6(9):e214. doi: 10.1371/journal.pbio.0060214
    • (2008) PLoS Biol , vol.6 , Issue.9 , pp. e214
    • Pons, V.1    Luyet, P.P.2    Morel, E.3    Abrami, L.4    Van Der Goot, F.G.5    Parton, R.G.6    Gruenberg, J.7
  • 62
    • 84862254447 scopus 로고    scopus 로고
    • Sorting nexin 12 interacts with BACE1 and regulates BACE1-mediated APP processing
    • 10.1186/1750-1326-7-30 3439308 1:CAS:528:DC%2BC38XhvVSiurjJ 22709416
    • Zhao Y, Wang Y, Yang J, Wang X, Zhao Y, Zhang X, Zhang YW (2012) Sorting nexin 12 interacts with BACE1 and regulates BACE1-mediated APP processing. Mol Neurodegener 7:30. doi: 10.1186/1750-1326-7-30
    • (2012) Mol Neurodegener , vol.7 , pp. 30
    • Zhao, Y.1    Wang, Y.2    Yang, J.3    Wang, X.4    Zhao, Y.5    Zhang, X.6    Zhang, Y.W.7
  • 64
    • 82655178026 scopus 로고    scopus 로고
    • SNX3 controls Wingless/Wnt secretion through regulating retromer-dependent recycling of Wntless
    • 10.1038/cr.2011.167 3357989 1:CAS:528:DC%2BC3MXhsFKms7fJ 22041890
    • Zhang P, Wu Y, Belenkaya TY, Lin X (2011) SNX3 controls Wingless/Wnt secretion through regulating retromer-dependent recycling of Wntless. Cell Res 21(12):1677-1690. doi: 10.1038/cr.2011.167
    • (2011) Cell Res , vol.21 , Issue.12 , pp. 1677-1690
    • Zhang, P.1    Wu, Y.2    Belenkaya, T.Y.3    Lin, X.4
  • 65
    • 35948987177 scopus 로고    scopus 로고
    • Structural features of vps35p involved in interaction with other subunits of the retromer complex
    • 2504507 1:CAS:528:DC%2BD2sXhsVeit73N 17892535
    • Restrepo R, Zhao X, Peter H, Zhang BY, Arvan P, Nothwehr SF (2007) Structural features of vps35p involved in interaction with other subunits of the retromer complex. Traffic 8(12):1841-1853
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1841-1853
    • Restrepo, R.1    Zhao, X.2    Peter, H.3    Zhang, B.Y.4    Arvan, P.5    Nothwehr, S.F.6
  • 66
    • 58149311474 scopus 로고    scopus 로고
    • Opposing activities of the Snx3-retromer complex and ESCRT proteins mediate regulated cargo sorting at a common endosome
    • 10.1091/mbc.E08-03-0296 2575174 1:CAS:528:DC%2BD1cXhtlKqsbbF 18768754
    • Strochlic TI, Schmiedekamp BC, Lee J, Katzmann DJ, Burd CG (2008) Opposing activities of the Snx3-retromer complex and ESCRT proteins mediate regulated cargo sorting at a common endosome. Mol Biol Cell 19(11):4694-4706. doi: 10.1091/mbc.E08-03-0296
    • (2008) Mol Biol Cell , vol.19 , Issue.11 , pp. 4694-4706
    • Strochlic, T.I.1    Schmiedekamp, B.C.2    Lee, J.3    Katzmann, D.J.4    Burd, C.G.5
  • 68
    • 0037073673 scopus 로고    scopus 로고
    • The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation
    • 1:CAS:528:DC%2BD38Xptlegu74%3D 12198132
    • Cozier GE, Carlton J, McGregor AH, Gleeson PA, Teasdale RD, Mellor H, Cullen PJ (2002) The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation. J Biol Chem 277(50):48730-48736
    • (2002) J Biol Chem , vol.277 , Issue.50 , pp. 48730-48736
    • Cozier, G.E.1    Carlton, J.2    McGregor, A.H.3    Gleeson, P.A.4    Teasdale, R.D.5    Mellor, H.6    Cullen, P.J.7
  • 69
    • 0035941208 scopus 로고    scopus 로고
    • All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate
    • 1:STN:280:DC%2BD3MnmslKmsQ%3D%3D 11557775
    • Yu JW, Lemmon MA (2001) All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate. J Biol Chem 276(47):44179-44184
    • (2001) J Biol Chem , vol.276 , Issue.47 , pp. 44179-44184
    • Yu, J.W.1    Lemmon, M.A.2
  • 70
    • 84856281728 scopus 로고    scopus 로고
    • Recruitment of the endosomal WASH complex is mediated by the extended 'tail' of Fam21 binding to the retromer protein Vps35
    • 1:CAS:528:DC%2BC38XhsVOms7Y%3D 22070227
    • Harbour ME, Breusegem SY, Seaman MN (2012) Recruitment of the endosomal WASH complex is mediated by the extended 'tail' of Fam21 binding to the retromer protein Vps35. Biochem J 442(1):209-220. doi: 10.1042/BJ20111761
    • (2012) Biochem J , vol.442 , Issue.1 , pp. 209-220
    • Harbour, M.E.1    Breusegem, S.Y.2    Seaman, M.N.3
  • 71
    • 84863469061 scopus 로고    scopus 로고
    • Identification of Alzheimer disease-associated variants in genes that regulate retromer function
    • 33 2231.e2215-2231.e2230
    • Vardarajan BN, Bruesegem SY, Harbour ME, St George-Hyslop P, Seaman MN, Farrer LA (2012) Identification of Alzheimer disease-associated variants in genes that regulate retromer function. Neurobiol Aging 33(9):2231.e2215-2231.e2230. doi: 10.1016/j.neurobiolaging.2012.04.020
    • (2012) Neurobiol Aging , Issue.9
    • Vardarajan, B.N.1    Bruesegem, S.Y.2    Harbour, M.E.3    St George-Hyslop, P.4    Seaman, M.N.5    Farrer, L.A.6
  • 72
    • 84874231112 scopus 로고    scopus 로고
    • Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins
    • 10.1073/pnas.1216229110 3581954 1:CAS:528:DC%2BC3sXjvV2rsbY%3D 23382219
    • Ghai R, Bugarcic A, Liu H, Norwood SJ, Skeldal S, Coulson EJ, Li SS, Teasdale RD, Collins BM (2013) Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins. Proc Natl Acad Sci USA 110(8):E643-E652. doi: 10.1073/pnas.1216229110
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.8 , pp. E643-E652
    • Ghai, R.1    Bugarcic, A.2    Liu, H.3    Norwood, S.J.4    Skeldal, S.5    Coulson, E.J.6    Li, S.S.7    Teasdale, R.D.8    Collins, B.M.9
  • 73
    • 14844338868 scopus 로고    scopus 로고
    • Functions of sorting nexin 17 domains and recognition motif for P-selectin trafficking
    • 10.1016/j.jmb.2005.02.004 1:CAS:528:DC%2BD2MXitlCgurY%3D 15769472
    • Knauth P, Schluter T, Czubayko M, Kirsch C, Florian V, Schreckenberger S, Hahn H, Bohnensack R (2005) Functions of sorting nexin 17 domains and recognition motif for P-selectin trafficking. J Mol Biol 347(4):813-825. doi: 10.1016/j.jmb.2005.02.004
    • (2005) J Mol Biol , vol.347 , Issue.4 , pp. 813-825
    • Knauth, P.1    Schluter, T.2    Czubayko, M.3    Kirsch, C.4    Florian, V.5    Schreckenberger, S.6    Hahn, H.7    Bohnensack, R.8
  • 74
    • 84861622962 scopus 로고    scopus 로고
    • Sorting nexin 17 prevents lysosomal degradation of beta1 integrins by binding to the beta1-integrin tail
    • 10.1038/ncb2501 22561348
    • Bottcher RT, Stremmel C, Meves A, Meyer H, Widmaier M, Tseng HY, Fassler R (2012) Sorting nexin 17 prevents lysosomal degradation of beta1 integrins by binding to the beta1-integrin tail. Nat Cell Biol 14(6):584-592. doi: 10.1038/ncb2501
    • (2012) Nat Cell Biol , vol.14 , Issue.6 , pp. 584-592
    • Bottcher, R.T.1    Stremmel, C.2    Meves, A.3    Meyer, H.4    Widmaier, M.5    Tseng, H.Y.6    Fassler, R.7
  • 75
    • 84878976235 scopus 로고    scopus 로고
    • A sorting nexin 17-binding domain within the LRP1 cytoplasmic tail mediates receptor recycling through the basolateral sorting endosome
    • 10.1111/tra.12076 3679278 1:CAS:528:DC%2BC3sXhtVKnsrzE 23593972
    • Farfan P, Lee J, Larios J, Sotelo P, Bu G, Marzolo MP (2013) A sorting nexin 17-binding domain within the LRP1 cytoplasmic tail mediates receptor recycling through the basolateral sorting endosome. Traffic 14(7):823-838. doi: 10.1111/tra.12076
    • (2013) Traffic , vol.14 , Issue.7 , pp. 823-838
    • Farfan, P.1    Lee, J.2    Larios, J.3    Sotelo, P.4    Bu, G.5    Marzolo, M.P.6
  • 76
    • 84899110602 scopus 로고    scopus 로고
    • Sorting nexin 17 regulates ApoER2 recycling and reelin signaling
    • 10.1371/journal.pone.0093672 3976305 24705369
    • Sotelo P, Farfan P, Benitez ML, Bu G, Marzolo MP (2014) Sorting nexin 17 regulates ApoER2 recycling and reelin signaling. PLoS ONE 9(4):e93672. doi: 10.1371/journal.pone.0093672
    • (2014) PLoS ONE , vol.9 , Issue.4 , pp. e93672
    • Sotelo, P.1    Farfan, P.2    Benitez, M.L.3    Bu, G.4    Marzolo, M.P.5
  • 77
    • 84861949426 scopus 로고    scopus 로고
    • SNX17 protects integrins from degradation by sorting between lysosomal and recycling pathways
    • 10.1083/jcb.201111121 3328392 1:CAS:528:DC%2BC38XmtFGksrs%3D 22492727
    • Steinberg F, Heesom KJ, Bass MD, Cullen PJ (2012) SNX17 protects integrins from degradation by sorting between lysosomal and recycling pathways. J Cell Biol 197(2):219-230. doi: 10.1083/jcb.201111121
    • (2012) J Cell Biol , vol.197 , Issue.2 , pp. 219-230
    • Steinberg, F.1    Heesom, K.J.2    Bass, M.D.3    Cullen, P.J.4
  • 79
    • 63049103433 scopus 로고    scopus 로고
    • Polarized traffic of LRP1 involves AP1B and SNX17 operating on Y-dependent sorting motifs in different pathways
    • 10.1091/mbc.E08-08-0805 2613102 1:CAS:528:DC%2BD1MXht1Srs7o%3D 19005208
    • Donoso M, Cancino J, Lee J, van Kerkhof P, Retamal C, Bu G, Gonzalez A, Caceres A, Marzolo MP (2009) Polarized traffic of LRP1 involves AP1B and SNX17 operating on Y-dependent sorting motifs in different pathways. Mol Biol Cell 20(1):481-497. doi: 10.1091/mbc.E08-08-0805
    • (2009) Mol Biol Cell , vol.20 , Issue.1 , pp. 481-497
    • Donoso, M.1    Cancino, J.2    Lee, J.3    Van Kerkhof, P.4    Retamal, C.5    Bu, G.6    Gonzalez, A.7    Caceres, A.8    Marzolo, M.P.9
  • 80
    • 1942469413 scopus 로고    scopus 로고
    • Sorting motifs in the intracellular domain of the low density lipoprotein receptor interact with a novel domain of sorting nexin-17
    • 10.1074/jbc.M313689200 1:CAS:528:DC%2BD2cXivF2qsbg%3D 14739284
    • Burden JJ, Sun XM, Garcia AB, Soutar AK (2004) Sorting motifs in the intracellular domain of the low density lipoprotein receptor interact with a novel domain of sorting nexin-17. J Biol Chem 279(16):16237-16245. doi: 10.1074/jbc.M313689200
    • (2004) J Biol Chem , vol.279 , Issue.16 , pp. 16237-16245
    • Burden, J.J.1    Sun, X.M.2    Garcia, A.B.3    Soutar, A.K.4
  • 81
    • 45549102847 scopus 로고    scopus 로고
    • Adaptor protein sorting nexin 17 regulates amyloid precursor protein trafficking and processing in the early endosomes
    • 10.1074/jbc.M800642200 2431074 1:CAS:528:DC%2BD1cXkvVSgt7c%3D 18276590
    • Lee J, Retamal C, Cuitino L, Caruano-Yzermans A, Shin JE, van Kerkhof P, Marzolo MP, Bu G (2008) Adaptor protein sorting nexin 17 regulates amyloid precursor protein trafficking and processing in the early endosomes. J Biol Chem 283(17):11501-11508. doi: 10.1074/jbc.M800642200
    • (2008) J Biol Chem , vol.283 , Issue.17 , pp. 11501-11508
    • Lee, J.1    Retamal, C.2    Cuitino, L.3    Caruano-Yzermans, A.4    Shin, J.E.5    Van Kerkhof, P.6    Marzolo, M.P.7    Bu, G.8
  • 82
    • 0037102292 scopus 로고    scopus 로고
    • The PX-domain protein SNX17 interacts with members of the LDL receptor family and modulates endocytosis of the LDL receptor
    • 126172 1:CAS:528:DC%2BD38Xms1Kntbc%3D 12169628
    • Stockinger W, Sailler B, Strasser V, Recheis B, Fasching D, Kahr L, Schneider WJ, Nimpf J (2002) The PX-domain protein SNX17 interacts with members of the LDL receptor family and modulates endocytosis of the LDL receptor. EMBO J 21(16):4259-4267
    • (2002) EMBO J , vol.21 , Issue.16 , pp. 4259-4267
    • Stockinger, W.1    Sailler, B.2    Strasser, V.3    Recheis, B.4    Fasching, D.5    Kahr, L.6    Schneider, W.J.7    Nimpf, J.8
  • 83
    • 3042721744 scopus 로고    scopus 로고
    • Sorting nexin 17 accelerates internalization yet retards degradation of P-selectin
    • 10.1091/mbc.E04-02-0143 452567 1:CAS:528:DC%2BD2cXlslWns7w%3D 15121882
    • Williams R, Schluter T, Roberts MS, Knauth P, Bohnensack R, Cutler DF (2004) Sorting nexin 17 accelerates internalization yet retards degradation of P-selectin. Mol Biol Cell 15(7):3095-3105. doi: 10.1091/mbc.E04-02-0143
    • (2004) Mol Biol Cell , vol.15 , Issue.7 , pp. 3095-3105
    • Williams, R.1    Schluter, T.2    Roberts, M.S.3    Knauth, P.4    Bohnensack, R.5    Cutler, D.F.6
  • 84
    • 84877293857 scopus 로고    scopus 로고
    • A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport
    • 10.1038/ncb2721 4052425 23563491
    • Steinberg F, Gallon M, Winfield M, Thomas EC, Bell AJ, Heesom KJ, Tavare JM, Cullen PJ (2013) A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport. Nat Cell Biol. doi: 10.1038/ncb2721
    • (2013) Nat Cell Biol
    • Steinberg, F.1    Gallon, M.2    Winfield, M.3    Thomas, E.C.4    Bell, A.J.5    Heesom, K.J.6    Tavare, J.M.7    Cullen, P.J.8
  • 85
    • 84886888066 scopus 로고    scopus 로고
    • Differential roles of C-terminal Eps15 homology domain proteins as vesiculators and tubulators of recycling endosomes
    • 10.1074/jbc.M113.488627 3798485 1:CAS:528:DC%2BC3sXhs1Crtb3M 24019528
    • Cai B, Giridharan SS, Zhang J, Saxena S, Bahl K, Schmidt JA, Sorgen PL, Guo W, Naslavsky N, Caplan S (2013) Differential roles of C-terminal Eps15 homology domain proteins as vesiculators and tubulators of recycling endosomes. J Biol Chem 288(42):30172-30180. doi: 10.1074/jbc.M113.488627
    • (2013) J Biol Chem , vol.288 , Issue.42 , pp. 30172-30180
    • Cai, B.1    Giridharan, S.S.2    Zhang, J.3    Saxena, S.4    Bahl, K.5    Schmidt, J.A.6    Sorgen, P.L.7    Guo, W.8    Naslavsky, N.9    Caplan, S.10
  • 86
    • 84883441205 scopus 로고    scopus 로고
    • Alphavbeta3-integrin-mediated adhesion is regulated through an AAK1L- and EHD3-dependent rapid-recycling pathway
    • 10.1242/jcs.122465 3744025 1:CAS:528:DC%2BC3sXhsFeksr7F 23781025
    • Waxmonsky NC, Conner SD (2013) Alphavbeta3-integrin-mediated adhesion is regulated through an AAK1L- and EHD3-dependent rapid-recycling pathway. J Cell Sci 126(Pt 16):3593-3601. doi: 10.1242/jcs.122465
    • (2013) J Cell Sci , vol.126 , pp. 3593-3601
    • Waxmonsky, N.C.1    Conner, S.D.2
  • 87
    • 84906217775 scopus 로고    scopus 로고
    • Sorting nexin 31 binds multiple beta integrin cytoplasmic domains and regulates beta1 integrin surface levels and stability
    • 10.1016/j.jmb.2014.07.003 1:CAS:528:DC%2BC2cXht1KmurrP 25020227
    • Tseng HY, Thorausch N, Ziegler T, Meves A, Fassler R, Bottcher RT (2014) Sorting nexin 31 binds multiple beta integrin cytoplasmic domains and regulates beta1 integrin surface levels and stability. J Mol Biol 426(18):3180-3194. doi: 10.1016/j.jmb.2014.07.003
    • (2014) J Mol Biol , vol.426 , Issue.18 , pp. 3180-3194
    • Tseng, H.Y.1    Thorausch, N.2    Ziegler, T.3    Meves, A.4    Fassler, R.5    Bottcher, R.T.6
  • 88
    • 84902668546 scopus 로고    scopus 로고
    • SNX31: A novel sorting nexin associated with the uroplakin-degrading multivesicular bodies in terminally differentiated urothelial cells
    • 10.1371/journal.pone.0099644 4051706 24914955
    • Vieira N, Deng FM, Liang FX, Liao Y, Chang J, Zhou G, Zheng W, Simon JP, Ding M, Wu XR, Romih R, Kreibich G, Sun TT (2014) SNX31: a novel sorting nexin associated with the uroplakin-degrading multivesicular bodies in terminally differentiated urothelial cells. PLoS ONE 9(6):e99644. doi: 10.1371/journal.pone.0099644
    • (2014) PLoS ONE , vol.9 , Issue.6 , pp. e99644
    • Vieira, N.1    Deng, F.M.2    Liang, F.X.3    Liao, Y.4    Chang, J.5    Zhou, G.6    Zheng, W.7    Simon, J.P.8    Ding, M.9    Wu, X.R.10    Romih, R.11    Kreibich, G.12    Sun, T.T.13
  • 89
    • 79957914861 scopus 로고    scopus 로고
    • SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors
    • 10.1038/ncb2252 3113693 21602791
    • Temkin P, Lauffer B, Jager S, Cimermancic P, Krogan NJ, von Zastrow M (2011) SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors. Nat Cell Biol 13(6):715-721. doi: 10.1038/ncb2252
    • (2011) Nat Cell Biol , vol.13 , Issue.6 , pp. 715-721
    • Temkin, P.1    Lauffer, B.2    Jager, S.3    Cimermancic, P.4    Krogan, N.J.5    Von Zastrow, M.6
  • 90
    • 0742305880 scopus 로고    scopus 로고
    • Endocytic recycling
    • 1:CAS:528:DC%2BD2cXnsFOjtg%3D%3D 15040445
    • Maxfield FR, McGraw TE (2004) Endocytic recycling. Nat Rev Mol Cell Biol 5(2):121-132
    • (2004) Nat Rev Mol Cell Biol , vol.5 , Issue.2 , pp. 121-132
    • Maxfield, F.R.1    McGraw, T.E.2
  • 92
    • 34547796509 scopus 로고    scopus 로고
    • Identification of a novel conserved sorting motif required for retromer-mediated endosome-to-TGN retrieval
    • 1:CAS:528:DC%2BD2sXpslChsLY%3D 17606993
    • Seaman MN (2007) Identification of a novel conserved sorting motif required for retromer-mediated endosome-to-TGN retrieval. J Cell Sci 120(Pt 14):2378-2389
    • (2007) J Cell Sci , vol.120 , pp. 2378-2389
    • Seaman, M.N.1
  • 93
    • 77149155327 scopus 로고    scopus 로고
    • Retromer-mediated direct sorting is required for proper endosomal recycling of the mammalian iron transporter DMT1
    • 10.1242/jcs.060574 1:CAS:528:DC%2BC3cXksVChtL4%3D 20164305
    • Tabuchi M, Yanatori I, Kawai Y, Kishi F (2010) Retromer-mediated direct sorting is required for proper endosomal recycling of the mammalian iron transporter DMT1. J Cell Sci 123(Pt 5):756-766. doi: 10.1242/jcs.060574
    • (2010) J Cell Sci , vol.123 , pp. 756-766
    • Tabuchi, M.1    Yanatori, I.2    Kawai, Y.3    Kishi, F.4
  • 94
    • 0032910357 scopus 로고    scopus 로고
    • Distinct domains within Vps35p mediate the retrieval of two different cargo proteins from the yeast prevacuolar/endosomal compartment
    • 25208 1:CAS:528:DyaK1MXisVGksrY%3D 10198044
    • Nothwehr SF, Bruinsma P, Strawn LA (1999) Distinct domains within Vps35p mediate the retrieval of two different cargo proteins from the yeast prevacuolar/endosomal compartment. Mol Biol Cell 10(4):875-890
    • (1999) Mol Biol Cell , vol.10 , Issue.4 , pp. 875-890
    • Nothwehr, S.F.1    Bruinsma, P.2    Strawn, L.A.3
  • 95
    • 2442530398 scopus 로고    scopus 로고
    • Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor
    • 1:CAS:528:DC%2BD2cXjtFKjsr0%3D 15078903
    • Arighi CN, Hartnell LM, Aguilar RC, Haft CR, Bonifacino JS (2004) Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor. J Cell Biol 165(1):123-133
    • (2004) J Cell Biol , vol.165 , Issue.1 , pp. 123-133
    • Arighi, C.N.1    Hartnell, L.M.2    Aguilar, R.C.3    Haft, C.R.4    Bonifacino, J.S.5
  • 96
    • 33748746143 scopus 로고    scopus 로고
    • The human Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide
    • 1:CAS:528:DC%2BD28XoslGluro%3D 16737443
    • Damen E, Krieger E, Nielsen JE, Eygensteyn J, van Leeuwen JE (2006) The human Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide. Biochem J 398(3):399-409
    • (2006) Biochem J , vol.398 , Issue.3 , pp. 399-409
    • Damen, E.1    Krieger, E.2    Nielsen, J.E.3    Eygensteyn, J.4    Van Leeuwen, J.E.5
  • 97
    • 81055140198 scopus 로고    scopus 로고
    • Vps26A and Vps26B subunits define distinct retromer complexes
    • 10.1111/j.1600-0854.2011.01284.x 1:CAS:528:DC%2BC3MXhs1Sqt77O 21920005
    • Bugarcic A, Zhe Y, Kerr MC, Griffin J, Collins BM, Teasdale RD (2011) Vps26A and Vps26B subunits define distinct retromer complexes. Traffic 12(12):1759-1773. doi: 10.1111/j.1600-0854.2011.01284.x
    • (2011) Traffic , vol.12 , Issue.12 , pp. 1759-1773
    • Bugarcic, A.1    Zhe, Y.2    Kerr, M.C.3    Griffin, J.4    Collins, B.M.5    Teasdale, R.D.6
  • 98
    • 2442509574 scopus 로고    scopus 로고
    • Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer
    • 2172078 1:CAS:528:DC%2BD2cXjtFKjsrw%3D 15078902
    • Seaman MN (2004) Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J Cell Biol 165(1):111-122
    • (2004) J Cell Biol , vol.165 , Issue.1 , pp. 111-122
    • Seaman, M.N.1
  • 99
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • 1:CAS:528:DC%2BD2MXhtVaqu73J 16143105
    • Rink J, Ghigo E, Kalaidzidis Y, Zerial M (2005) Rab conversion as a mechanism of progression from early to late endosomes. Cell 122(5):735-749
    • (2005) Cell , vol.122 , Issue.5 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 100
    • 0037117524 scopus 로고    scopus 로고
    • A minimal system allowing tubulation with molecular motors pulling on giant liposomes
    • 10.1073/pnas.082107299 122780 1:CAS:528:DC%2BD38XjtFKlsLs%3D 11959994
    • Roux A, Cappello G, Cartaud J, Prost J, Goud B, Bassereau P (2002) A minimal system allowing tubulation with molecular motors pulling on giant liposomes. Proc Natl Acad Sci USA 99(8):5394-5399. doi: 10.1073/pnas.082107299
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.8 , pp. 5394-5399
    • Roux, A.1    Cappello, G.2    Cartaud, J.3    Prost, J.4    Goud, B.5    Bassereau, P.6
  • 102
    • 18844384403 scopus 로고    scopus 로고
    • Modulation of receptor recycling and degradation by the endosomal kinesin KIF16B
    • 10.1016/j.cell.2005.02.017 1:CAS:528:DC%2BD2MXktlShsr4%3D 15882625
    • Hoepfner S, Severin F, Cabezas A, Habermann B, Runge A, Gillooly D, Stenmark H, Zerial M (2005) Modulation of receptor recycling and degradation by the endosomal kinesin KIF16B. Cell 121(3):437-450. doi: 10.1016/j.cell.2005.02.017
    • (2005) Cell , vol.121 , Issue.3 , pp. 437-450
    • Hoepfner, S.1    Severin, F.2    Cabezas, A.3    Habermann, B.4    Runge, A.5    Gillooly, D.6    Stenmark, H.7    Zerial, M.8
  • 104
    • 59549101542 scopus 로고    scopus 로고
    • The Rip11/Rab11-FIP5 and kinesin II complex regulates endocytic protein recycling
    • 10.1242/jcs.032441 4365997 1:CAS:528:DC%2BD1cXhsFaktLjJ 18957512
    • Schonteich E, Wilson GM, Burden J, Hopkins CR, Anderson K, Goldenring JR, Prekeris R (2008) The Rip11/Rab11-FIP5 and kinesin II complex regulates endocytic protein recycling. J Cell Sci 121(Pt 22):3824-3833. doi: 10.1242/jcs.032441
    • (2008) J Cell Sci , vol.121 , pp. 3824-3833
    • Schonteich, E.1    Wilson, G.M.2    Burden, J.3    Hopkins, C.R.4    Anderson, K.5    Goldenring, J.R.6    Prekeris, R.7
  • 105
    • 0026061507 scopus 로고
    • Tubular early endosomal networks in AtT20 and other cells
    • 1:STN:280:DyaK38%2FhtF2jtw%3D%3D 1918157
    • Tooze J, Hollinshead M (1991) Tubular early endosomal networks in AtT20 and other cells. J Cell Biol 115(3):635-653
    • (1991) J Cell Biol , vol.115 , Issue.3 , pp. 635-653
    • Tooze, J.1    Hollinshead, M.2
  • 106
    • 71749090787 scopus 로고    scopus 로고
    • The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport
    • 10.1038/cr.2009.130 1:CAS:528:DC%2BD1MXhsFSgsrjF 19935774
    • Hong Z, Yang Y, Zhang C, Niu Y, Li K, Zhao X, Liu JJ (2009) The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport. Cell Res 19(12):1334-1349. doi: 10.1038/cr.2009.130
    • (2009) Cell Res , vol.19 , Issue.12 , pp. 1334-1349
    • Hong, Z.1    Yang, Y.2    Zhang, C.3    Niu, Y.4    Li, K.5    Zhao, X.6    Liu, J.J.7
  • 107
    • 67650110003 scopus 로고    scopus 로고
    • SNX4 in complex with clathrin and dynein: Implications for endosome movement
    • 10.1371/journal.pone.0005935 2691479 19529763
    • Skanland SS, Walchli S, Brech A, Sandvig K (2009) SNX4 in complex with clathrin and dynein: implications for endosome movement. PLoS ONE 4(6):e5935. doi: 10.1371/journal.pone.0005935
    • (2009) PLoS ONE , vol.4 , Issue.6 , pp. e5935
    • Skanland, S.S.1    Walchli, S.2    Brech, A.3    Sandvig, K.4
  • 108
    • 77749246128 scopus 로고    scopus 로고
    • Membrane curvature controls dynamin polymerization
    • 10.1073/pnas.0913734107 2840091 1:CAS:528:DC%2BC3cXjsFWitLg%3D 20160074
    • Roux A, Koster G, Lenz M, Sorre B, Manneville JB, Nassoy P, Bassereau P (2010) Membrane curvature controls dynamin polymerization. Proc Natl Acad Sci USA 107(9):4141-4146. doi: 10.1073/pnas.0913734107
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.9 , pp. 4141-4146
    • Roux, A.1    Koster, G.2    Lenz, M.3    Sorre, B.4    Manneville, J.B.5    Nassoy, P.6    Bassereau, P.7
  • 110
    • 84883389095 scopus 로고    scopus 로고
    • Dual role of BAR domain-containing proteins in regulating vesicle release catalyzed by the GTPase, dynamin-2
    • 10.1074/jbc.M113.490474 3757176 1:CAS:528:DC%2BC3sXhtlyisbrF 23861397
    • Neumann S, Schmid SL (2013) Dual role of BAR domain-containing proteins in regulating vesicle release catalyzed by the GTPase, dynamin-2. J Biol Chem 288(35):25119-25128. doi: 10.1074/jbc.M113.490474
    • (2013) J Biol Chem , vol.288 , Issue.35 , pp. 25119-25128
    • Neumann, S.1    Schmid, S.L.2
  • 112
    • 35349007899 scopus 로고    scopus 로고
    • Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling
    • 10.1038/nature06173 1:CAS:528:DC%2BD2sXhtFOjt7bI 17914359
    • Daumke O, Lundmark R, Vallis Y, Martens S, Butler PJ, McMahon HT (2007) Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling. Nature 449(7164):923-927. doi: 10.1038/nature06173
    • (2007) Nature , vol.449 , Issue.7164 , pp. 923-927
    • Daumke, O.1    Lundmark, R.2    Vallis, Y.3    Martens, S.4    Butler, P.J.5    McMahon, H.T.6
  • 113
    • 73349097586 scopus 로고    scopus 로고
    • AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling
    • 10.1038/ncb1986 2788952 1:CAS:528:DC%2BD1MXhsV2gsLbN 19915558
    • Pant S, Sharma M, Patel K, Caplan S, Carr CM, Grant BD (2009) AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling. Nat Cell Biol 11(12):1399-1410. doi: 10.1038/ncb1986
    • (2009) Nat Cell Biol , vol.11 , Issue.12 , pp. 1399-1410
    • Pant, S.1    Sharma, M.2    Patel, K.3    Caplan, S.4    Carr, C.M.5    Grant, B.D.6
  • 114
    • 84939550403 scopus 로고    scopus 로고
    • GRAF1 forms a complex with MICAL-L1 and EHD1 to cooperate in tubular recycling endosome vesiculation
    • 10.3389/fcell.2014.00022 4214196 25364729
    • Cai B, Xie S, Caplan S, Naslavsky N (2014) GRAF1 forms a complex with MICAL-L1 and EHD1 to cooperate in tubular recycling endosome vesiculation. Front Cell Dev Biol 2:22. doi: 10.3389/fcell.2014.00022
    • (2014) Front Cell Dev Biol , vol.2 , pp. 22
    • Cai, B.1    Xie, S.2    Caplan, S.3    Naslavsky, N.4
  • 117
    • 79151477797 scopus 로고    scopus 로고
    • EHD proteins: Key conductors of endocytic transport
    • CAS:528:DC%2BC3MXhtlSmu70%3D 21067929
    • Naslavsky N, Caplan S (2011) EHD proteins: key conductors of endocytic transport. Trends Cell Biol 21(2):122-131. doi: 10.1016/j.tcb.2010.10.003
    • (2011) Trends Cell Biol , vol.21 , Issue.2 , pp. 122-131
    • Naslavsky, N.1    Caplan, S.2
  • 118
    • 84861150709 scopus 로고    scopus 로고
    • CPLA2alpha and EHD1 interact and regulate the vesiculation of cholesterol-rich, GPI-anchored, protein-containing endosomes
    • 10.1091/mbc.E11-10-0881 3350552 1:CAS:528:DC%2BC38XotlWmu7w%3D 22456504
    • Cai B, Caplan S, Naslavsky N (2012) cPLA2alpha and EHD1 interact and regulate the vesiculation of cholesterol-rich, GPI-anchored, protein-containing endosomes. Mol Biol Cell 23(10):1874-1888. doi: 10.1091/mbc.E11-10-0881
    • (2012) Mol Biol Cell , vol.23 , Issue.10 , pp. 1874-1888
    • Cai, B.1    Caplan, S.2    Naslavsky, N.3
  • 119
    • 84878686056 scopus 로고    scopus 로고
    • Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular recycling endosome biogenesis 24-rf- S1771-S1715
    • Giridharan SS, Cai B, Vitale N, Naslavsky N, Caplan S (2013) Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular recycling endosome biogenesis. Mol Biol Cell 24(11):1776-1790, S1771-S1715. doi: 10.1091/mbc.E13-01-0026
    • (2013) Mol Biol Cell , Issue.11 , pp. 1776-1790
    • Giridharan, S.S.1    Cai, B.2    Vitale, N.3    Naslavsky, N.4    Caplan, S.5
  • 120
    • 80053250463 scopus 로고    scopus 로고
    • Regulation of synaptic vesicle budding and dynamin function by an EHD ATPase
    • 10.1523/JNEUROSCI.1289-11.2011 1:CAS:528:DC%2BC3MXht1ylu7nJ 21957258
    • Jakobsson J, Ackermann F, Andersson F, Larhammar D, Low P, Brodin L (2011) Regulation of synaptic vesicle budding and dynamin function by an EHD ATPase. J Neurosci 31(39):13972-13980. doi: 10.1523/JNEUROSCI.1289-11.2011
    • (2011) J Neurosci , vol.31 , Issue.39 , pp. 13972-13980
    • Jakobsson, J.1    Ackermann, F.2    Andersson, F.3    Larhammar, D.4    Low, P.5    Brodin, L.6
  • 121
    • 84879899805 scopus 로고    scopus 로고
    • Local cytoskeletal and organelle interactions impact molecular-motor- driven early endosomal trafficking
    • 10.1016/j.cub.2013.05.015 3738301 1:CAS:528:DC%2BC3sXpsV2qurc%3D 23770188
    • Zajac AL, Goldman YE, Holzbaur EL, Ostap EM (2013) Local cytoskeletal and organelle interactions impact molecular-motor- driven early endosomal trafficking. Curr Biol 23(13):1173-1180. doi: 10.1016/j.cub.2013.05.015
    • (2013) Curr Biol , vol.23 , Issue.13 , pp. 1173-1180
    • Zajac, A.L.1    Goldman, Y.E.2    Holzbaur, E.L.3    Ostap, E.M.4
  • 123
    • 12344250580 scopus 로고    scopus 로고
    • The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B
    • 10.1093/hmg/ddi003 1:CAS:528:DC%2BD2MXitFGmsA%3D%3D 15537668
    • Reid E, Connell J, Edwards TL, Duley S, Brown SE, Sanderson CM (2005) The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B. Hum Mol Genet 14(1):19-38. doi: 10.1093/hmg/ddi003
    • (2005) Hum Mol Genet , vol.14 , Issue.1 , pp. 19-38
    • Reid, E.1    Connell, J.2    Edwards, T.L.3    Duley, S.4    Brown, S.E.5    Sanderson, C.M.6
  • 124
    • 77958064894 scopus 로고    scopus 로고
    • SPG20 protein spartin is recruited to midbodies by ESCRT-III protein Ist1 and participates in cytokinesis
    • 10.1091/mbc.E09-10-0879 2947466 1:CAS:528:DC%2BC3cXhtlGlt7zN 20719964
    • Renvoise B, Parker RL, Yang D, Bakowska JC, Hurley JH, Blackstone C (2010) SPG20 protein spartin is recruited to midbodies by ESCRT-III protein Ist1 and participates in cytokinesis. Mol Biol Cell 21(19):3293-3303. doi: 10.1091/mbc.E09-10-0879
    • (2010) Mol Biol Cell , vol.21 , Issue.19 , pp. 3293-3303
    • Renvoise, B.1    Parker, R.L.2    Yang, D.3    Bakowska, J.C.4    Hurley, J.H.5    Blackstone, C.6
  • 125
    • 70349761410 scopus 로고    scopus 로고
    • The mechanochemistry of endocytosis
    • 10.1371/journal.pbio.1000204 2742711 19787029
    • Liu J, Sun Y, Drubin DG, Oster GF (2009) The mechanochemistry of endocytosis. PLoS Biol 7(9):e1000204. doi: 10.1371/journal.pbio.1000204
    • (2009) PLoS Biol , vol.7 , Issue.9 , pp. e1000204
    • Liu, J.1    Sun, Y.2    Drubin, D.G.3    Oster, G.F.4
  • 126
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • 1:CAS:528:DC%2BD3sXpt1Oqsrw%3D 14622601
    • Kaksonen M, Sun Y, Drubin DG (2003) A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell 115(4):475-487
    • (2003) Cell , vol.115 , Issue.4 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 127
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrin-mediated endocytosis
    • 1:CAS:528:DC%2BD28XkvVylsbw%3D 16723976
    • Kaksonen M, Toret CP, Drubin DG (2006) Harnessing actin dynamics for clathrin-mediated endocytosis. Nat Rev Mol Cell Biol 7(6):404-414
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.6 , pp. 404-414
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 128
    • 84911472010 scopus 로고    scopus 로고
    • ER contact sites define the position and timing of endosome fission
    • 10.1016/j.cell.2014.10.023 1:CAS:528:DC%2BC2cXhvFOgsrvF 25416943
    • Rowland AA, Chitwood PJ, Phillips MJ, Voeltz GK (2014) ER contact sites define the position and timing of endosome fission. Cell 159(5):1027-1041. doi: 10.1016/j.cell.2014.10.023
    • (2014) Cell , vol.159 , Issue.5 , pp. 1027-1041
    • Rowland, A.A.1    Chitwood, P.J.2    Phillips, M.J.3    Voeltz, G.K.4
  • 129
    • 80054844842 scopus 로고    scopus 로고
    • ER tubules mark sites of mitochondrial division
    • 10.1126/science.1207385 3366560 1:CAS:528:DC%2BC3MXhtlahsrzM 21885730
    • Friedman JR, Lackner LL, West M, DiBenedetto JR, Nunnari J, Voeltz GK (2011) ER tubules mark sites of mitochondrial division. Science 334(6054):358-362. doi: 10.1126/science.1207385
    • (2011) Science , vol.334 , Issue.6054 , pp. 358-362
    • Friedman, J.R.1    Lackner, L.L.2    West, M.3    DiBenedetto, J.R.4    Nunnari, J.5    Voeltz, G.K.6
  • 130
    • 77749254726 scopus 로고    scopus 로고
    • Retromer is required for apoptotic cell clearance by phagocytic receptor recycling
    • 10.1126/science.1184840 1:CAS:528:DC%2BC3cXis1Cmurs%3D 20133524
    • Chen D, Xiao H, Zhang K, Wang B, Gao Z, Jian Y, Qi X, Sun J, Miao L, Yang C (2010) Retromer is required for apoptotic cell clearance by phagocytic receptor recycling. Science 327(5970):1261-1264. doi: 10.1126/science.1184840
    • (2010) Science , vol.327 , Issue.5970 , pp. 1261-1264
    • Chen, D.1    Xiao, H.2    Zhang, K.3    Wang, B.4    Gao, Z.5    Jian, Y.6    Qi, X.7    Sun, J.8    Miao, L.9    Yang, C.10
  • 131
    • 77049112709 scopus 로고    scopus 로고
    • Identification of different itineraries and retromer components for endosome-to-Golgi transport of TGN38 and Shiga toxin
    • 10.1016/j.ejcb.2009.10.021 1:CAS:528:DC%2BC3cXltVCrsrs%3D 20138391
    • Lieu ZZ, Gleeson PA (2010) Identification of different itineraries and retromer components for endosome-to-Golgi transport of TGN38 and Shiga toxin. Eur J Cell Biol 89(5):379-393. doi: 10.1016/j.ejcb.2009.10.021
    • (2010) Eur J Cell Biol , vol.89 , Issue.5 , pp. 379-393
    • Lieu, Z.Z.1    Gleeson, P.A.2
  • 132
    • 72749126343 scopus 로고    scopus 로고
    • Retromer recycles vacuolar sorting receptors from the trans-Golgi network
    • 10.1111/j.1365-313X.2009.04034.x 1:CAS:528:DC%2BC3cXovF2ksg%3D%3D 19796370
    • Niemes S, Langhans M, Viotti C, Scheuring D, San Wan Yan M, Jiang L, Hillmer S, Robinson DG, Pimpl P (2010) Retromer recycles vacuolar sorting receptors from the trans-Golgi network. Plant J 61(1):107-121. doi: 10.1111/j.1365-313X.2009.04034.x
    • (2010) Plant J , vol.61 , Issue.1 , pp. 107-121
    • Niemes, S.1    Langhans, M.2    Viotti, C.3    Scheuring, D.4    San Wan Yan, M.5    Jiang, L.6    Hillmer, S.7    Robinson, D.G.8    Pimpl, P.9
  • 133
    • 33745453426 scopus 로고    scopus 로고
    • Plant retromer, localized to the prevacuolar compartment and microvesicles in Arabidopsis, may interact with vacuolar sorting receptors
    • 1456867 1:CAS:528:DC%2BD28XkslCmu7s%3D 16582012
    • Oliviusson P, Heinzerling O, Hillmer S, Hinz G, Tse YC, Jiang L, Robinson DG (2006) Plant retromer, localized to the prevacuolar compartment and microvesicles in Arabidopsis, may interact with vacuolar sorting receptors. Plant Cell 18(5):1239-1252
    • (2006) Plant Cell , vol.18 , Issue.5 , pp. 1239-1252
    • Oliviusson, P.1    Heinzerling, O.2    Hillmer, S.3    Hinz, G.4    Tse, Y.C.5    Jiang, L.6    Robinson, D.G.7
  • 134
    • 77955817279 scopus 로고    scopus 로고
    • Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing
    • 10.1096/fj.09-146357 2909280 1:CAS:528:DC%2BC3cXhtVeisbfJ 20354142
    • Okada H, Zhang W, Peterhoff C, Hwang JC, Nixon RA, Ryu SH, Kim TW (2010) Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing. FASEB J 24(8):2783-2794. doi: 10.1096/fj.09-146357
    • (2010) FASEB J , vol.24 , Issue.8 , pp. 2783-2794
    • Okada, H.1    Zhang, W.2    Peterhoff, C.3    Hwang, J.C.4    Nixon, R.A.5    Ryu, S.H.6    Kim, T.W.7
  • 135
    • 34548704766 scopus 로고    scopus 로고
    • The retromer protein VPS29 links cell polarity and organ initiation in plants
    • 1:CAS:528:DC%2BD2sXhtFKnurvL 17889650
    • Jaillais Y, Santambrogio M, Rozier F, Fobis-Loisy I, Miege C, Gaude T (2007) The retromer protein VPS29 links cell polarity and organ initiation in plants. Cell 130(6):1057-1070
    • (2007) Cell , vol.130 , Issue.6 , pp. 1057-1070
    • Jaillais, Y.1    Santambrogio, M.2    Rozier, F.3    Fobis-Loisy, I.4    Miege, C.5    Gaude, T.6
  • 136
    • 56649100703 scopus 로고    scopus 로고
    • Differential degradation of PIN2 auxin efflux carrier by retromer-dependent vacuolar targeting
    • 10.1073/pnas.0808073105 2584678 1:CAS:528:DC%2BD1cXhsVCmurzF 19004783
    • Kleine-Vehn J, Leitner J, Zwiewka M, Sauer M, Abas L, Luschnig C, Friml J (2008) Differential degradation of PIN2 auxin efflux carrier by retromer-dependent vacuolar targeting. Proc Natl Acad Sci USA 105(46):17812-17817. doi: 10.1073/pnas.0808073105
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.46 , pp. 17812-17817
    • Kleine-Vehn, J.1    Leitner, J.2    Zwiewka, M.3    Sauer, M.4    Abas, L.5    Luschnig, C.6    Friml, J.7
  • 137
    • 84894290116 scopus 로고    scopus 로고
    • BMP signaling requires retromer-dependent recycling of the type i receptor
    • 10.1073/pnas.1319947111 3932876 1:CAS:528:DC%2BC2cXivFamsrs%3D 24550286
    • Gleason RJ, Akintobi AM, Grant BD, Padgett RW (2014) BMP signaling requires retromer-dependent recycling of the type I receptor. Proc Natl Acad Sci USA 111(7):2578-2583. doi: 10.1073/pnas.1319947111
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.7 , pp. 2578-2583
    • Gleason, R.J.1    Akintobi, A.M.2    Grant, B.D.3    Padgett, R.W.4
  • 139
    • 0034805704 scopus 로고    scopus 로고
    • A new member of the sorting nexin family interacts with the C-terminus of P-selectin
    • 10.1006/bbrc.2001.4467 1:CAS:528:DC%2BD3MXhs1Cgsrc%3D 11237770
    • Florian V, Schluter T, Bohnensack R (2001) A new member of the sorting nexin family interacts with the C-terminus of P-selectin. Biochem Biophys Res Commun 281(4):1045-1050. doi: 10.1006/bbrc.2001.4467
    • (2001) Biochem Biophys Res Commun , vol.281 , Issue.4 , pp. 1045-1050
    • Florian, V.1    Schluter, T.2    Bohnensack, R.3
  • 140
    • 84911975794 scopus 로고    scopus 로고
    • Identification of molecular heterogeneity in SNX27-retromer-mediated endosome-to-plasma-membrane recycling
    • 10.1242/jcs.156299 4231307 25278552
    • McGough IJ, Steinberg F, Gallon M, Yatsu A, Ohbayashi N, Heesom KJ, Fukuda M, Cullen PJ (2014) Identification of molecular heterogeneity in SNX27-retromer-mediated endosome-to-plasma-membrane recycling. J Cell Sci 127(22):4940-4953. doi: 10.1242/jcs.156299
    • (2014) J Cell Sci , vol.127 , Issue.22 , pp. 4940-4953
    • McGough, I.J.1    Steinberg, F.2    Gallon, M.3    Yatsu, A.4    Ohbayashi, N.5    Heesom, K.J.6    Fukuda, M.7    Cullen, P.J.8
  • 141
    • 37549057671 scopus 로고    scopus 로고
    • AP-1 and retromer play opposite roles in the trafficking of sortilin between the Golgi apparatus and the lysosomes
    • 1:CAS:528:DC%2BD1cXivVemtg%3D%3D 18078806
    • Canuel M, Lefrancois S, Zeng J, Morales CR (2008) AP-1 and retromer play opposite roles in the trafficking of sortilin between the Golgi apparatus and the lysosomes. Biochem Biophys Res Commun 366(3):724-730
    • (2008) Biochem Biophys Res Commun , vol.366 , Issue.3 , pp. 724-730
    • Canuel, M.1    Lefrancois, S.2    Zeng, J.3    Morales, C.R.4
  • 143
    • 79960200667 scopus 로고    scopus 로고
    • Retromer controls epithelial cell polarity by trafficking the apical determinant Crumbs
    • 10.1016/j.cub.2011.05.007 1:CAS:528:DC%2BC3MXoslaktLc%3D 21700461
    • Pocha SM, Wassmer T, Niehage C, Hoflack B, Knust E (2011) Retromer controls epithelial cell polarity by trafficking the apical determinant Crumbs. Curr Biol 21(13):1111-1117. doi: 10.1016/j.cub.2011.05.007
    • (2011) Curr Biol , vol.21 , Issue.13 , pp. 1111-1117
    • Pocha, S.M.1    Wassmer, T.2    Niehage, C.3    Hoflack, B.4    Knust, E.5
  • 144
    • 0030908449 scopus 로고    scopus 로고
    • The yeast VPS5/GRD2 gene encodes a sorting nexin-1-like protein required for localizing membrane proteins to the late Golgi
    • 1:CAS:528:DyaK2sXjsVGksLY%3D 9175702
    • Nothwehr SF, Hindes AE (1997) The yeast VPS5/GRD2 gene encodes a sorting nexin-1-like protein required for localizing membrane proteins to the late Golgi. J Cell Sci 110(Pt 9):1063-1072
    • (1997) J Cell Sci , vol.110 , pp. 1063-1072
    • Nothwehr, S.F.1    Hindes, A.E.2
  • 145
    • 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
    • 2140161 1:CAS:528:DyaK1cXhtVamsrk%3D 9456318
    • Voos W, Stevens TH (1998) Retrieval of resident late-Golgi membrane proteins from the prevacuolar compartment of Saccharomyces cerevisiae is dependent on the function of Grd19p. J Cell Biol 140(3):577-590
    • (1998) J Cell Biol , vol.140 , Issue.3 , pp. 577-590
    • Voos, W.1    Stevens, T.H.2
  • 146
    • 0029088909 scopus 로고
    • The cytoplasmic tail domain of the vacuolar protein sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function, and localization
    • 301269 1:STN:280:DyaK28%2FnvFamug%3D%3D 8534908
    • Cereghino JL, Marcusson EG, Emr SD (1995) The cytoplasmic tail domain of the vacuolar protein sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function, and localization. Mol Biol Cell 6(9):1089-1102
    • (1995) Mol Biol Cell , vol.6 , Issue.9 , pp. 1089-1102
    • Cereghino, J.L.1    Marcusson, E.G.2    Emr, S.D.3
  • 147
    • 84892444172 scopus 로고    scopus 로고
    • V-ATPase-dependent luminal acidification is required for endocytic recycling of a yeast cell wall stress sensor, Wsc1p
    • 10.1016/j.bbrc.2013.12.008 1:CAS:528:DC%2BC3sXhvFOhsr7P 24326069
    • Ueno K, Saito M, Nagashima M, Kojima A, Nishinoaki S, Toshima JY, Toshima J (2014) V-ATPase-dependent luminal acidification is required for endocytic recycling of a yeast cell wall stress sensor, Wsc1p. Biochem Biophys Res Commun 443-g(2):549-555. doi: 10.1016/j.bbrc.2013.12.008
    • (2014) Biochem Biophys Res Commun , vol.443 , Issue.2 , pp. 549-555
    • Ueno, K.1    Saito, M.2    Nagashima, M.3    Kojima, A.4    Nishinoaki, S.5    Toshima, J.Y.6    Toshima, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.