메뉴 건너뛰기




Volumn 72, Issue 19, 2015, Pages 3709-3720

Mechanisms for exporting large-sized cargoes from the endoplasmic reticulum

Author keywords

Chylomicron; Collagen; COPII; cTAGE5; TANGO1

Indexed keywords

CHYLOMICRON; COAT PROTEIN COMPLEX II; COLLAGEN; GUANOSINE TRIPHOSPHATASE; ARNT PROTEIN, HUMAN; CARRIER PROTEIN; CTAGE5 PROTEIN, HUMAN; HYPOXIA INDUCIBLE FACTOR 1BETA; TUMOR ANTIGEN; TUMOR PROTEIN;

EID: 84941413076     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-015-1952-9     Document Type: Review
Times cited : (39)

References (138)
  • 2
    • 0027500969 scopus 로고
    • SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER
    • 10.1038/365347a0 1:CAS:528:DyaK3sXlvFOrtb8%3D
    • Barlowe C, Schekman R (1993) SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER. Nature 365(6444):347-349. doi: 10.1038/365347a0
    • (1993) Nature , vol.365 , Issue.6444 , pp. 347-349
    • Barlowe, C.1    Schekman, R.2
  • 3
    • 0024807217 scopus 로고
    • A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus
    • 1:CAS:528:DyaK3cXhtFehuro%3D
    • Nakano A, Muramatsu M (1989) A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus. J Cell Biol 109(6 Pt 1):2677-2691
    • (1989) J Cell Biol , vol.109 , Issue.6 , pp. 2677-2691
    • Nakano, A.1    Muramatsu, M.2
  • 4
    • 0027459023 scopus 로고
    • Purification and characterization of SAR1p, a small GTP-binding protein required for transport vesicle formation from the endoplasmic reticulum
    • 1:CAS:528:DyaK3sXlsVGmuw%3D%3D
    • Barlowe C, d'Enfert C, Schekman R (1993) Purification and characterization of SAR1p, a small GTP-binding protein required for transport vesicle formation from the endoplasmic reticulum. J Biol Chem 268(2):873-879
    • (1993) J Biol Chem , vol.268 , Issue.2 , pp. 873-879
    • Barlowe, C.1    D'Enfert, C.2    Schekman, R.3
  • 5
    • 0034946168 scopus 로고    scopus 로고
    • The mammalian guanine nucleotide exchange factor mSec12 is essential for activation of the Sar1 GTPase directing endoplasmic reticulum export
    • 1:CAS:528:DC%2BD3MXlt1arurk%3D
    • Weissman JT, Plutner H, Balch WE (2001) The mammalian guanine nucleotide exchange factor mSec12 is essential for activation of the Sar1 GTPase directing endoplasmic reticulum export. Traffic 2(7):465-475
    • (2001) Traffic , vol.2 , Issue.7 , pp. 465-475
    • Weissman, J.T.1    Plutner, H.2    Balch, W.E.3
  • 6
    • 0035842886 scopus 로고    scopus 로고
    • Crystal structure of Sar1-GDP at 1.7 A resolution and the role of the NH2 terminus in ER export
    • 10.1083/jcb.200106039 2150902 1:CAS:528:DC%2BD3MXptVejsLc%3D
    • Huang M, Weissman JT, Beraud-Dufour S, Luan P, Wang C, Chen W, Aridor M, Wilson IA, Balch WE (2001) Crystal structure of Sar1-GDP at 1.7 A resolution and the role of the NH2 terminus in ER export. J Cell Biol 155(6):937-948. doi: 10.1083/jcb.200106039
    • (2001) J Cell Biol , vol.155 , Issue.6 , pp. 937-948
    • Huang, M.1    Weissman, J.T.2    Beraud-Dufour, S.3    Luan, P.4    Wang, C.5    Chen, W.6    Aridor, M.7    Wilson, I.A.8    Balch, W.E.9
  • 7
    • 29144454715 scopus 로고    scopus 로고
    • Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission
    • 10.1083/jcb.200509095 2171319 1:CAS:528:DC%2BD2MXhtlequ7fM
    • Bielli A, Haney CJ, Gabreski G, Watkins SC, Bannykh SI, Aridor M (2005) Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission. J Cell Biol 171(6):919-924. doi: 10.1083/jcb.200509095
    • (2005) J Cell Biol , vol.171 , Issue.6 , pp. 919-924
    • Bielli, A.1    Haney, C.J.2    Gabreski, G.3    Watkins, S.C.4    Bannykh, S.I.5    Aridor, M.6
  • 8
    • 23944488301 scopus 로고    scopus 로고
    • Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle
    • 10.1016/j.cell.2005.07.025 1:CAS:528:DC%2BD2MXpvVKntbg%3D
    • Lee MC, Orci L, Hamamoto S, Futai E, Ravazzola M, Schekman R (2005) Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 122(4):605-617. doi: 10.1016/j.cell.2005.07.025
    • (2005) Cell , vol.122 , Issue.4 , pp. 605-617
    • Lee, M.C.1    Orci, L.2    Hamamoto, S.3    Futai, E.4    Ravazzola, M.5    Schekman, R.6
  • 9
    • 70350763840 scopus 로고    scopus 로고
    • Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane
    • 10.1038/emboj.2009.269 2776102 1:CAS:528:DC%2BD1MXhtFWhu73O
    • Tabata KV, Sato K, Ide T, Nishizaka T, Nakano A, Noji H (2009) Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane. EMBO J 28(21):3279-3289. doi: 10.1038/emboj.2009.269
    • (2009) EMBO J , vol.28 , Issue.21 , pp. 3279-3289
    • Tabata, K.V.1    Sato, K.2    Ide, T.3    Nishizaka, T.4    Nakano, A.5    Noji, H.6
  • 10
    • 0037136560 scopus 로고    scopus 로고
    • Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat
    • 10.1038/nature01040 1:CAS:528:DC%2BD38XntFSgs7c%3D
    • Bi X, Corpina RA, Goldberg J (2002) Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature 419(6904):271-277. doi: 10.1038/nature01040
    • (2002) Nature , vol.419 , Issue.6904 , pp. 271-277
    • Bi, X.1    Corpina, R.A.2    Goldberg, J.3
  • 11
    • 0032495477 scopus 로고    scopus 로고
    • COPII-cargo interactions direct protein sorting into ER-derived transport vesicles
    • 10.1038/34438 1:CAS:528:DyaK1cXmt1KjtA%3D%3D
    • Kuehn MJ, Herrmann JM, Schekman R (1998) COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature 391(6663):187-190. doi: 10.1038/34438
    • (1998) Nature , vol.391 , Issue.6663 , pp. 187-190
    • Kuehn, M.J.1    Herrmann, J.M.2    Schekman, R.3
  • 12
    • 0032489878 scopus 로고    scopus 로고
    • Cargo selection by the COPII budding machinery during export from the ER
    • 2132735 1:CAS:528:DyaK1cXis1ejsr0%3D
    • Aridor M, Weissman J, Bannykh S, Nuoffer C, Balch WE (1998) Cargo selection by the COPII budding machinery during export from the ER. J Cell Biol 141(1):61-70
    • (1998) J Cell Biol , vol.141 , Issue.1 , pp. 61-70
    • Aridor, M.1    Weissman, J.2    Bannykh, S.3    Nuoffer, C.4    Balch, W.E.5
  • 13
    • 0037112755 scopus 로고    scopus 로고
    • Cargo selection into COPII vesicles is driven by the Sec24p subunit
    • 137197 1:CAS:528:DC%2BD38XptFOrtrs%3D
    • Miller E, Antonny B, Hamamoto S, Schekman R (2002) Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J 21(22):6105-6113
    • (2002) EMBO J , vol.21 , Issue.22 , pp. 6105-6113
    • Miller, E.1    Antonny, B.2    Hamamoto, S.3    Schekman, R.4
  • 14
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
    • 1:CAS:528:DC%2BD3sXmvFahtbc%3D
    • Miller EA, Beilharz TH, Malkus PN, Lee MC, Hamamoto S, Orci L, Schekman R (2003) Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114(4):497-509
    • (2003) Cell , vol.114 , Issue.4 , pp. 497-509
    • Miller, E.A.1    Beilharz, T.H.2    Malkus, P.N.3    Lee, M.C.4    Hamamoto, S.5    Orci, L.6    Schekman, R.7
  • 15
    • 84922877368 scopus 로고    scopus 로고
    • Sec24 is a coincidence detector that simultaneously binds two signals to drive ER export
    • 10.1016/j.cub.2014.11.070 1:CAS:528:DC%2BC2MXhsVarsr8%3D
    • Pagant S, Wu A, Edwards S, Diehl F, Miller EA (2015) Sec24 is a coincidence detector that simultaneously binds two signals to drive ER export. Curr Biol 25(4):403-412. doi: 10.1016/j.cub.2014.11.070
    • (2015) Curr Biol , vol.25 , Issue.4 , pp. 403-412
    • Pagant, S.1    Wu, A.2    Edwards, S.3    Diehl, F.4    Miller, E.A.5
  • 16
    • 0027467609 scopus 로고
    • Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum
    • 1:CAS:528:DyaK3sXhs1Cqu7g%3D
    • Yoshihisa T, Barlowe C, Schekman R (1993) Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science 259(5100):1466-1468
    • (1993) Science , vol.259 , Issue.5100 , pp. 1466-1468
    • Yoshihisa, T.1    Barlowe, C.2    Schekman, R.3
  • 17
    • 0034965355 scopus 로고    scopus 로고
    • Dynamics of the COPII coat with GTP and stable analogues
    • 10.1038/35078500 1:CAS:528:DC%2BD3MXksFeltbc%3D
    • Antonny B, Madden D, Hamamoto S, Orci L, Schekman R (2001) Dynamics of the COPII coat with GTP and stable analogues. Nat Cell Biol 3(6):531-537. doi: 10.1038/35078500
    • (2001) Nat Cell Biol , vol.3 , Issue.6 , pp. 531-537
    • Antonny, B.1    Madden, D.2    Hamamoto, S.3    Orci, L.4    Schekman, R.5
  • 18
    • 35549004893 scopus 로고    scopus 로고
    • Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31
    • 10.1016/j.devcel.2007.10.006 2686382 1:CAS:528:DC%2BD2sXhtlWitrfP
    • Bi X, Mancias JD, Goldberg J (2007) Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31. Dev Cell 13(5):635-645. doi: 10.1016/j.devcel.2007.10.006
    • (2007) Dev Cell , vol.13 , Issue.5 , pp. 635-645
    • Bi, X.1    Mancias, J.D.2    Goldberg, J.3
  • 19
    • 18344405156 scopus 로고    scopus 로고
    • COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes
    • 1:CAS:528:DyaK1cXivVynsr0%3D
    • Matsuoka K, Orci L, Amherdt M, Bednarek SY, Hamamoto S, Schekman R, Yeung T (1998) COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 93(2):263-275
    • (1998) Cell , vol.93 , Issue.2 , pp. 263-275
    • Matsuoka, K.1    Orci, L.2    Amherdt, M.3    Bednarek, S.Y.4    Hamamoto, S.5    Schekman, R.6    Yeung, T.7
  • 20
    • 23944445863 scopus 로고    scopus 로고
    • Sec16 is a determinant of transitional ER organization
    • 10.1016/j.cub.2005.06.065 1:CAS:528:DC%2BD2MXos1ajtr4%3D
    • Connerly PL, Esaki M, Montegna EA, Strongin DE, Levi S, Soderholm J, Glick BS (2005) Sec16 is a determinant of transitional ER organization. Curr Biol 15(16):1439-1447. doi: 10.1016/j.cub.2005.06.065
    • (2005) Curr Biol , vol.15 , Issue.16 , pp. 1439-1447
    • Connerly, P.L.1    Esaki, M.2    Montegna, E.A.3    Strongin, D.E.4    Levi, S.5    Soderholm, J.6    Glick, B.S.7
  • 21
    • 34547138159 scopus 로고    scopus 로고
    • Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic reticulum
    • 10.1074/jbc.M611237200 1:CAS:528:DC%2BD2sXmt1eku78%3D
    • Iinuma T, Shiga A, Nakamoto K, O'Brien MB, Aridor M, Arimitsu N, Tagaya M, Tani K (2007) Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic reticulum. J Biol Chem 282(24):17632-17639. doi: 10.1074/jbc.M611237200
    • (2007) J Biol Chem , vol.282 , Issue.24 , pp. 17632-17639
    • Iinuma, T.1    Shiga, A.2    Nakamoto, K.3    O'Brien, M.B.4    Aridor, M.5    Arimitsu, N.6    Tagaya, M.7    Tani, K.8
  • 22
    • 57349165449 scopus 로고    scopus 로고
    • Drosophila Sec16 mediates the biogenesis of ter sites upstream of Sar1 through an arginine-rich motif
    • 10.1091/mbc.E08-03-0246 2555954 1:CAS:528:DC%2BD1cXht1ygsb7J
    • Ivan V, de Voer G, Xanthakis D, Spoorendonk KM, Kondylis V, Rabouille C (2008) Drosophila Sec16 mediates the biogenesis of tER sites upstream of Sar1 through an arginine-rich motif. Mol Biol Cell 19(10):4352-4365. doi: 10.1091/mbc.E08-03-0246
    • (2008) Mol Biol Cell , vol.19 , Issue.10 , pp. 4352-4365
    • Ivan, V.1    De Voer, G.2    Xanthakis, D.3    Spoorendonk, K.M.4    Kondylis, V.5    Rabouille, C.6
  • 23
    • 84863035842 scopus 로고    scopus 로고
    • Sec12 binds to Sec16 at transitional ER sites
    • 10.1371/journal.pone.0031156 3275590 1:CAS:528:DC%2BC38XivVWiu78%3D
    • Montegna EA, Bhave M, Liu Y, Bhattacharyya D, Glick BS (2012) Sec12 binds to Sec16 at transitional ER sites. PLoS One 7(2):e31156. doi: 10.1371/journal.pone.0031156
    • (2012) PLoS One , vol.7 , Issue.2 , pp. e31156
    • Montegna, E.A.1    Bhave, M.2    Liu, Y.3    Bhattacharyya, D.4    Glick, B.S.5
  • 24
    • 33750969692 scopus 로고    scopus 로고
    • Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells
    • 10.1111/j.1600-0854.2006.00493.x 1761133 1:CAS:528:DC%2BD28XhtlSitrvI
    • Watson P, Townley AK, Koka P, Palmer KJ, Stephens DJ (2006) Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells. Traffic 7(12):1678-1687. doi: 10.1111/j.1600-0854.2006.00493.x
    • (2006) Traffic , vol.7 , Issue.12 , pp. 1678-1687
    • Watson, P.1    Townley, A.K.2    Koka, P.3    Palmer, K.J.4    Stephens, D.J.5
  • 25
    • 77955453495 scopus 로고    scopus 로고
    • Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat
    • 10.1083/jcb.201003092 2922654 1:CAS:528:DC%2BC3cXhtVCrs7zO
    • Whittle JR, Schwartz TU (2010) Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat. J Cell Biol 190(3):347-361. doi: 10.1083/jcb.201003092
    • (2010) J Cell Biol , vol.190 , Issue.3 , pp. 347-361
    • Whittle, J.R.1    Schwartz, T.U.2
  • 26
    • 84887118903 scopus 로고    scopus 로고
    • Sec16 influences transitional ER sites by regulating rather than organizing COPII
    • 10.1091/mbc.E13-04-0185 3814151 1:CAS:528:DC%2BC3sXhvVyitLrO
    • Bharucha N, Liu Y, Papanikou E, McMahon C, Esaki M, Jeffrey PD, Hughson FM, Glick BS (2013) Sec16 influences transitional ER sites by regulating rather than organizing COPII. Mol Biol Cell 24(21):3406-3419. doi: 10.1091/mbc.E13-04-0185
    • (2013) Mol Biol Cell , vol.24 , Issue.21 , pp. 3406-3419
    • Bharucha, N.1    Liu, Y.2    Papanikou, E.3    McMahon, C.4    Esaki, M.5    Jeffrey, P.D.6    Hughson, F.M.7    Glick, B.S.8
  • 28
    • 84863830464 scopus 로고    scopus 로고
    • Insights into structural and regulatory roles of Sec16 in COPII vesicle formation at ER exit sites
    • 10.1091/mbc.E12-05-0356 3408419 1:CAS:528:DC%2BC38XhtF2hsrnM
    • Yorimitsu T, Sato K (2012) Insights into structural and regulatory roles of Sec16 in COPII vesicle formation at ER exit sites. Mol Biol Cell 23(15):2930-2942. doi: 10.1091/mbc.E12-05-0356
    • (2012) Mol Biol Cell , vol.23 , Issue.15 , pp. 2930-2942
    • Yorimitsu, T.1    Sato, K.2
  • 29
    • 84906544287 scopus 로고    scopus 로고
    • Apoptosis-linked gene-2 (ALG-2)/Sec31 interactions regulate endoplasmic reticulum (ER)-to-Golgi transport: A potential effector pathway for luminal calcium
    • 10.1074/jbc.M114.561829 4156086 1:CAS:528:DC%2BC2cXhsVSms73N
    • Helm JR, Bentley M, Thorsen KD, Wang T, Foltz L, Oorschot V, Klumperman J, Hay JC (2014) Apoptosis-linked gene-2 (ALG-2)/Sec31 interactions regulate endoplasmic reticulum (ER)-to-Golgi transport: a potential effector pathway for luminal calcium. J Biol Chem 289(34):23609-23628. doi: 10.1074/jbc.M114.561829
    • (2014) J Biol Chem , vol.289 , Issue.34 , pp. 23609-23628
    • Helm, J.R.1    Bentley, M.2    Thorsen, K.D.3    Wang, T.4    Foltz, L.5    Oorschot, V.6    Klumperman, J.7    Hay, J.C.8
  • 30
    • 84884378448 scopus 로고    scopus 로고
    • ALG-2 attenuates COPII budding in vitro and stabilizes the Sec23/Sec31A complex
    • 10.1371/journal.pone.0075309 3777911
    • la Cour JM, Schindler AJ, Berchtold MW, Schekman R (2013) ALG-2 attenuates COPII budding in vitro and stabilizes the Sec23/Sec31A complex. PLoS One 8(9):e75309. doi: 10.1371/journal.pone.0075309
    • (2013) PLoS One , vol.8 , Issue.9 , pp. e75309
    • La Cour, J.M.1    Schindler, A.J.2    Berchtold, M.W.3    Schekman, R.4
  • 31
    • 77957368304 scopus 로고    scopus 로고
    • The ALG-2 binding site in Sec31A influences the retention kinetics of Sec31A at the endoplasmic reticulum exit sites as revealed by live-cell time-lapse imaging
    • 10.1271/bbb.100215 1:CAS:528:DC%2BC3cXht12qs77J
    • Shibata H, Inuzuka T, Yoshida H, Sugiura H, Wada I, Maki M (2010) The ALG-2 binding site in Sec31A influences the retention kinetics of Sec31A at the endoplasmic reticulum exit sites as revealed by live-cell time-lapse imaging. Biosci Biotechnol Biochem 74(9):1819-1826. doi: 10.1271/bbb.100215
    • (2010) Biosci Biotechnol Biochem , vol.74 , Issue.9 , pp. 1819-1826
    • Shibata, H.1    Inuzuka, T.2    Yoshida, H.3    Sugiura, H.4    Wada, I.5    Maki, M.6
  • 33
    • 33750534358 scopus 로고    scopus 로고
    • 2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A
    • 10.1091/mbc.E06-05-0444 1635383 1:CAS:528:DC%2BD28XhtFygtrzF
    • 2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A. Mol Biol Cell 17(11):4876-4887. doi: 10.1091/mbc.E06-05-0444
    • (2006) Mol Biol Cell , vol.17 , Issue.11 , pp. 4876-4887
    • Yamasaki, A.1    Tani, K.2    Yamamoto, A.3    Kitamura, N.4    Komada, M.5
  • 34
    • 84863811537 scopus 로고    scopus 로고
    • 2+-dependent regulation of COPII subunit assembly in Saccharomyces cerevisiae
    • 10.1371/journal.pone.0040765 3394733 1:CAS:528:DC%2BC38XhtVKku7nI
    • 2+-dependent regulation of COPII subunit assembly in Saccharomyces cerevisiae. PLoS One 7(7):e40765. doi: 10.1371/journal.pone.0040765
    • (2012) PLoS One , vol.7 , Issue.7 , pp. e40765
    • Yoshibori, M.1    Yorimitsu, T.2    Sato, K.3
  • 37
    • 77955460168 scopus 로고    scopus 로고
    • P125A exists as part of the mammalian Sec13/Sec31 COPII subcomplex to facilitate ER-Golgi transport
    • 10.1083/jcb.201003005 2922642 1:CAS:528:DC%2BC3cXhtVCrs7zN
    • Ong YS, Tang BL, Loo LS, Hong W (2010) p125A exists as part of the mammalian Sec13/Sec31 COPII subcomplex to facilitate ER-Golgi transport. J Cell Biol 190(3):331-345. doi: 10.1083/jcb.201003005
    • (2010) J Cell Biol , vol.190 , Issue.3 , pp. 331-345
    • Ong, Y.S.1    Tang, B.L.2    Loo, L.S.3    Hong, W.4
  • 38
    • 20144377947 scopus 로고    scopus 로고
    • P125 is localized in endoplasmic reticulum exit sites and involved in their organization
    • 10.1074/jbc.M409673200 1:CAS:528:DC%2BD2MXit1ekur4%3D
    • Shimoi W, Ezawa I, Nakamoto K, Uesaki S, Gabreski G, Aridor M, Yamamoto A, Nagahama M, Tagaya M, Tani K (2005) p125 is localized in endoplasmic reticulum exit sites and involved in their organization. J Biol Chem 280(11):10141-10148. doi: 10.1074/jbc.M409673200
    • (2005) J Biol Chem , vol.280 , Issue.11 , pp. 10141-10148
    • Shimoi, W.1    Ezawa, I.2    Nakamoto, K.3    Uesaki, S.4    Gabreski, G.5    Aridor, M.6    Yamamoto, A.7    Nagahama, M.8    Tagaya, M.9    Tani, K.10
  • 39
    • 84878253184 scopus 로고    scopus 로고
    • Organization of the ER-Golgi interface for membrane traffic control
    • 10.1038/nrm3588 4064004 1:CAS:528:DC%2BC3sXotFSltb0%3D
    • Brandizzi F, Barlowe C (2013) Organization of the ER-Golgi interface for membrane traffic control. Nat Rev Mol Cell Biol 14(6):382-392. doi: 10.1038/nrm3588
    • (2013) Nat Rev Mol Cell Biol , vol.14 , Issue.6 , pp. 382-392
    • Brandizzi, F.1    Barlowe, C.2
  • 40
    • 84880583267 scopus 로고    scopus 로고
    • Vesicle-mediated export from the ER: COPII coat function and regulation
    • 10.1016/j.bbamcr.2013.02.003 3676692
    • D'Arcangelo JG, Stahmer KR, Miller EA (2013) Vesicle-mediated export from the ER: COPII coat function and regulation. Biochim Biophys Acta 1833(11):2464-2472. doi: 10.1016/j.bbamcr.2013.02.003
    • (2013) Biochim Biophys Acta , vol.1833 , Issue.11 , pp. 2464-2472
    • D'Arcangelo, J.G.1    Stahmer, K.R.2    Miller, E.A.3
  • 41
    • 84890881427 scopus 로고    scopus 로고
    • Exiting the ER: What we know and what we don't
    • 10.1016/j.tcb.2013.08.005 1:CAS:528:DC%2BC3sXhsFekt77I
    • Venditti R, Wilson C, De Matteis MA (2014) Exiting the ER: what we know and what we don't. Trends Cell Biol 24(1):9-18. doi: 10.1016/j.tcb.2013.08.005
    • (2014) Trends Cell Biol , vol.24 , Issue.1 , pp. 9-18
    • Venditti, R.1    Wilson, C.2    De Matteis, M.A.3
  • 42
    • 84876387069 scopus 로고    scopus 로고
    • Secretory protein biogenesis and traffic in the early secretory pathway
    • 10.1534/genetics.112.142810 3567731 1:CAS:528:DC%2BC3sXhtVWnu7%2FJ
    • Barlowe CK, Miller EA (2013) Secretory protein biogenesis and traffic in the early secretory pathway. Genetics 193(2):383-410. doi: 10.1534/genetics.112.142810
    • (2013) Genetics , vol.193 , Issue.2 , pp. 383-410
    • Barlowe, C.K.1    Miller, E.A.2
  • 43
    • 84878127508 scopus 로고    scopus 로고
    • Vesicle coats: Structure, function, and general principles of assembly
    • 10.1016/j.tcb.2013.01.005 1:CAS:528:DC%2BC3sXisVyjsLg%3D
    • Faini M, Beck R, Wieland FT, Briggs JA (2013) Vesicle coats: structure, function, and general principles of assembly. Trends Cell Biol 23(6):279-288. doi: 10.1016/j.tcb.2013.01.005
    • (2013) Trends Cell Biol , vol.23 , Issue.6 , pp. 279-288
    • Faini, M.1    Beck, R.2    Wieland, F.T.3    Briggs, J.A.4
  • 44
    • 84870750255 scopus 로고    scopus 로고
    • The highly conserved COPII coat complex sorts cargo from the endoplasmic reticulum and targets it to the golgi
    • 10.1101/cshperspect.a013367 3552504
    • Lord C, Ferro-Novick S, Miller EA (2013) The highly conserved COPII coat complex sorts cargo from the endoplasmic reticulum and targets it to the golgi. Cold Spring Harb Perspect Biol. doi: 10.1101/cshperspect.a013367
    • (2013) Cold Spring Harb Perspect Biol
    • Lord, C.1    Ferro-Novick, S.2    Miller, E.A.3
  • 45
    • 84862192727 scopus 로고    scopus 로고
    • Vesicle-mediated ER export of proteins and lipids
    • 10.1016/j.bbalip.2012.01.005 3337971 1:CAS:528:DC%2BC38XhsFGqu7o%3D
    • Gillon AD, Latham CF, Miller EA (2012) Vesicle-mediated ER export of proteins and lipids. Biochim Biophys Acta 1821(8):1040-1049. doi: 10.1016/j.bbalip.2012.01.005
    • (2012) Biochim Biophys Acta , vol.1821 , Issue.8 , pp. 1040-1049
    • Gillon, A.D.1    Latham, C.F.2    Miller, E.A.3
  • 46
    • 84255188602 scopus 로고    scopus 로고
    • COPII and the regulation of protein sorting in mammals
    • 10.1038/ncb2390 1:CAS:528:DC%2BC3MXhs1GksLrN
    • Zanetti G, Pahuja KB, Studer S, Shim S, Schekman R (2012) COPII and the regulation of protein sorting in mammals. Nat Cell Biol 14(1):20-28. doi: 10.1038/ncb2390
    • (2012) Nat Cell Biol , vol.14 , Issue.1 , pp. 20-28
    • Zanetti, G.1    Pahuja, K.B.2    Studer, S.3    Shim, S.4    Schekman, R.5
  • 47
    • 84940575187 scopus 로고    scopus 로고
    • Ziploc-ing the structure: Triple helix formation is coordinated by rough endoplasmic reticulum resident PPIases
    • 10.1016/j.bbagen.2014.12.024
    • Ishikawa Y, Boudko S, Bachinger HP (2015) Ziploc-ing the structure: triple helix formation is coordinated by rough endoplasmic reticulum resident PPIases. Biochim Biophys Acta. doi: 10.1016/j.bbagen.2014.12.024
    • (2015) Biochim Biophys Acta
    • Ishikawa, Y.1    Boudko, S.2    Bachinger, H.P.3
  • 48
    • 22044441866 scopus 로고    scopus 로고
    • COPII-coated vesicles: Flexible enough for large cargo?
    • 10.1016/j.ceb.2005.06.004 1:CAS:528:DC%2BD2MXmt1SrtbY%3D
    • Fromme JC, Schekman R (2005) COPII-coated vesicles: flexible enough for large cargo? Curr Opin Cell Biol 17(4):345-352. doi: 10.1016/j.ceb.2005.06.004
    • (2005) Curr Opin Cell Biol , vol.17 , Issue.4 , pp. 345-352
    • Fromme, J.C.1    Schekman, R.2
  • 50
    • 0027389056 scopus 로고
    • Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type i collagen
    • 10.1002/ajmg.1320450204 1:STN:280:DyaK3s3gs12jtQ%3D%3D
    • Bachinger HP, Morris NP, Davis JM (1993) Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagen. Am J Med Genet 45(2):152-162. doi: 10.1002/ajmg.1320450204
    • (1993) Am J Med Genet , vol.45 , Issue.2 , pp. 152-162
    • Bachinger, H.P.1    Morris, N.P.2    Davis, J.M.3
  • 51
    • 0037087610 scopus 로고    scopus 로고
    • Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells
    • 1:CAS:528:DC%2BD38XivFGnsbc%3D
    • Stephens DJ, Pepperkok R (2002) Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells. J Cell Sci 115(Pt 6):1149-1160
    • (2002) J Cell Sci , vol.115 , pp. 1149-1160
    • Stephens, D.J.1    Pepperkok, R.2
  • 53
  • 55
    • 35548961813 scopus 로고    scopus 로고
    • The genetic basis of a craniofacial disease provides insight into COPII coat assembly
    • 10.1016/j.devcel.2007.10.005 2262049 1:CAS:528:DC%2BD2sXhtlWitrfO
    • Fromme JC, Ravazzola M, Hamamoto S, Al-Balwi M, Eyaid W, Boyadjiev SA, Cosson P, Schekman R, Orci L (2007) The genetic basis of a craniofacial disease provides insight into COPII coat assembly. Dev Cell 13(5):623-634. doi: 10.1016/j.devcel.2007.10.005
    • (2007) Dev Cell , vol.13 , Issue.5 , pp. 623-634
    • Fromme, J.C.1    Ravazzola, M.2    Hamamoto, S.3    Al-Balwi, M.4    Eyaid, W.5    Boyadjiev, S.A.6    Cosson, P.7    Schekman, R.8    Orci, L.9
  • 56
    • 84858979184 scopus 로고    scopus 로고
    • The [corrected] SEC23-SEC31 [corrected] interface plays critical role for export of procollagen from the endoplasmic reticulum
    • 10.1074/jbc.M111.283382 3323018 1:CAS:528:DC%2BC38XktlKku7k%3D
    • Kim SD, Pahuja KB, Ravazzola M, Yoon J, Boyadjiev SA, Hammamoto S, Schekman R, Orci L, Kim J (2012) The [corrected] SEC23-SEC31 [corrected] interface plays critical role for export of procollagen from the endoplasmic reticulum. J Biol Chem 287(13):10134-10144. doi: 10.1074/jbc.M111.283382
    • (2012) J Biol Chem , vol.287 , Issue.13 , pp. 10134-10144
    • Kim, S.D.1    Pahuja, K.B.2    Ravazzola, M.3    Yoon, J.4    Boyadjiev, S.A.5    Hammamoto, S.6    Schekman, R.7    Orci, L.8    Kim, J.9
  • 58
    • 33749151608 scopus 로고    scopus 로고
    • Secretory COPII coat component Sec23a is essential for craniofacial chondrocyte maturation
    • 10.1038/ng1880 1:CAS:528:DC%2BD28XhtVSns73L
    • Lang MR, Lapierre LA, Frotscher M, Goldenring JR, Knapik EW (2006) Secretory COPII coat component Sec23a is essential for craniofacial chondrocyte maturation. Nat Genet 38(10):1198-1203. doi: 10.1038/ng1880
    • (2006) Nat Genet , vol.38 , Issue.10 , pp. 1198-1203
    • Lang, M.R.1    Lapierre, L.A.2    Frotscher, M.3    Goldenring, J.R.4    Knapik, E.W.5
  • 62
    • 84892371843 scopus 로고    scopus 로고
    • Chondrocyte proliferation regulated by secreted luminal domain of ER stress transducer BBF2H7/CREB3L2
    • 10.1016/j.molcel.2013.11.008 1:CAS:528:DC%2BC3sXhvFOhtrbL
    • Saito A, Kanemoto S, Zhang Y, Asada R, Hino K, Imaizumi K (2014) Chondrocyte proliferation regulated by secreted luminal domain of ER stress transducer BBF2H7/CREB3L2. Mol Cell 53(1):127-139. doi: 10.1016/j.molcel.2013.11.008
    • (2014) Mol Cell , vol.53 , Issue.1 , pp. 127-139
    • Saito, A.1    Kanemoto, S.2    Zhang, Y.3    Asada, R.4    Hino, K.5    Imaizumi, K.6
  • 63
    • 81455136719 scopus 로고    scopus 로고
    • The feelgood mutation in zebrafish dysregulates COPII-dependent secretion of select extracellular matrix proteins in skeletal morphogenesis
    • 10.1242/dmm.007625 1:CAS:528:DC%2BC3MXhs1GqsrfF
    • Melville DB, Montero-Balaguer M, Levic DS, Bradley K, Smith JR, Hatzopoulos AK, Knapik EW (2011) The feelgood mutation in zebrafish dysregulates COPII-dependent secretion of select extracellular matrix proteins in skeletal morphogenesis. Disease models & mechanisms 4(6):763-776. doi: 10.1242/dmm.007625
    • (2011) Disease Models & Mechanisms , vol.4 , Issue.6 , pp. 763-776
    • Melville, D.B.1    Montero-Balaguer, M.2    Levic, D.S.3    Bradley, K.4    Smith, J.R.5    Hatzopoulos, A.K.6    Knapik, E.W.7
  • 64
    • 84863982830 scopus 로고    scopus 로고
    • BBF2H7-mediated Sec23A pathway is required for endoplasmic reticulum-to-Golgi trafficking in dermal fibroblasts to promote collagen synthesis
    • 10.1038/jid.2012.103 1:CAS:528:DC%2BC38Xltl2ruro%3D
    • Ishikura-Kinoshita S, Saeki H, Tsuji-Naito K (2012) BBF2H7-mediated Sec23A pathway is required for endoplasmic reticulum-to-Golgi trafficking in dermal fibroblasts to promote collagen synthesis. J Invest Dermatol 132(8):2010-2018. doi: 10.1038/jid.2012.103
    • (2012) J Invest Dermatol , vol.132 , Issue.8 , pp. 2010-2018
    • Ishikura-Kinoshita, S.1    Saeki, H.2    Tsuji-Naito, K.3
  • 65
    • 33847357796 scopus 로고    scopus 로고
    • Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum
    • 10.1038/sj.embor.7400893 1808030 1:CAS:528:DC%2BD2sXit12rtbk%3D
    • Wendeler MW, Paccaud JP, Hauri HP (2007) Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum. EMBO Rep 8(3):258-264. doi: 10.1038/sj.embor.7400893
    • (2007) EMBO Rep , vol.8 , Issue.3 , pp. 258-264
    • Wendeler, M.W.1    Paccaud, J.P.2    Hauri, H.P.3
  • 66
    • 77956413317 scopus 로고    scopus 로고
    • Sec24D-dependent transport of extracellular matrix proteins is required for zebrafish skeletal morphogenesis
    • 10.1371/journal.pone.0010367 2860987
    • Sarmah S, Barrallo-Gimeno A, Melville DB, Topczewski J, Solnica-Krezel L, Knapik EW (2010) Sec24D-dependent transport of extracellular matrix proteins is required for zebrafish skeletal morphogenesis. PLoS One 5(4):e10367. doi: 10.1371/journal.pone.0010367
    • (2010) PLoS One , vol.5 , Issue.4 , pp. e10367
    • Sarmah, S.1    Barrallo-Gimeno, A.2    Melville, D.B.3    Topczewski, J.4    Solnica-Krezel, L.5    Knapik, E.W.6
  • 67
    • 77952581690 scopus 로고    scopus 로고
    • Sec24d encoding a component of COPII is essential for vertebra formation, revealed by the analysis of the medaka mutant, vbi
    • 10.1016/j.ydbio.2010.03.016 1:CAS:528:DC%2BC3cXlvVegu7c%3D
    • Ohisa S, Inohaya K, Takano Y, Kudo A (2010) sec24d encoding a component of COPII is essential for vertebra formation, revealed by the analysis of the medaka mutant, vbi. Dev Biol 342(1):85-95. doi: 10.1016/j.ydbio.2010.03.016
    • (2010) Dev Biol , vol.342 , Issue.1 , pp. 85-95
    • Ohisa, S.1    Inohaya, K.2    Takano, Y.3    Kudo, A.4
  • 68
    • 1942501149 scopus 로고    scopus 로고
    • Osteogenesis imperfecta
    • 10.1016/S0140-6736(04)16051-0 1:CAS:528:DC%2BD2cXjtl2lsLs%3D
    • Rauch F, Glorieux FH (2004) Osteogenesis imperfecta. Lancet 363(9418):1377-1385. doi: 10.1016/S0140-6736(04)16051-0
    • (2004) Lancet , vol.363 , Issue.9418 , pp. 1377-1385
    • Rauch, F.1    Glorieux, F.H.2
  • 70
    • 84876186687 scopus 로고    scopus 로고
    • Disruption of the Sec24d gene results in early embryonic lethality in the mouse
    • 10.1371/journal.pone.0061114 3626607 1:CAS:528:DC%2BC3sXms12qtbg%3D
    • Baines AC, Adams EJ, Zhang B, Ginsburg D (2013) Disruption of the Sec24d gene results in early embryonic lethality in the mouse. PLoS One 8(4):e61114. doi: 10.1371/journal.pone.0061114
    • (2013) PLoS One , vol.8 , Issue.4 , pp. e61114
    • Baines, A.C.1    Adams, E.J.2    Zhang, B.3    Ginsburg, D.4
  • 71
    • 0030031968 scopus 로고    scopus 로고
    • A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores
    • 1:CAS:528:DyaK28Xnt1egsQ%3D%3D
    • Siniossoglou S, Wimmer C, Rieger M, Doye V, Tekotte H, Weise C, Emig S, Segref A, Hurt EC (1996) A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 84(2):265-275
    • (1996) Cell , vol.84 , Issue.2 , pp. 265-275
    • Siniossoglou, S.1    Wimmer, C.2    Rieger, M.3    Doye, V.4    Tekotte, H.5    Weise, C.6    Emig, S.7    Segref, A.8    Hurt, E.C.9
  • 72
    • 55049134801 scopus 로고    scopus 로고
    • Efficient coupling of Sec23-Sec24 to Sec13-Sec31 drives COPII-dependent collagen secretion and is essential for normal craniofacial development
    • 10.1242/jcs.031070 1:CAS:528:DC%2BD1cXhtlWntLvP
    • Townley AK, Feng Y, Schmidt K, Carter DA, Porter R, Verkade P, Stephens DJ (2008) Efficient coupling of Sec23-Sec24 to Sec13-Sec31 drives COPII-dependent collagen secretion and is essential for normal craniofacial development. J Cell Sci 121(Pt 18):3025-3034. doi: 10.1242/jcs.031070
    • (2008) J Cell Sci , vol.121 , pp. 3025-3034
    • Townley, A.K.1    Feng, Y.2    Schmidt, K.3    Carter, D.A.4    Porter, R.5    Verkade, P.6    Stephens, D.J.7
  • 73
    • 58149390117 scopus 로고    scopus 로고
    • Mypt1-mediated spatial positioning of Bmp2-producing cells is essential for liver organogenesis
    • 10.1242/dev.024406 1:CAS:528:DC%2BD1cXhtlCntbvN
    • Huang H, Ruan H, Aw MY, Hussain A, Guo L, Gao C, Qian F, Leung T, Song H, Kimelman D, Wen Z, Peng J (2008) Mypt1-mediated spatial positioning of Bmp2-producing cells is essential for liver organogenesis. Development 135(19):3209-3218. doi: 10.1242/dev.024406
    • (2008) Development , vol.135 , Issue.19 , pp. 3209-3218
    • Huang, H.1    Ruan, H.2    Aw, M.Y.3    Hussain, A.4    Guo, L.5    Gao, C.6    Qian, F.7    Leung, T.8    Song, H.9    Kimelman, D.10    Wen, Z.11    Peng, J.12
  • 74
    • 84862116924 scopus 로고    scopus 로고
    • Sec13 safeguards the integrity of the endoplasmic reticulum and organogenesis of the digestive system in zebrafish
    • 10.1016/j.ydbio.2012.05.004 1:CAS:528:DC%2BC38XotVartLk%3D
    • Niu X, Gao C, Jan Lo L, Luo Y, Meng C, Hong J, Hong W, Peng J (2012) Sec13 safeguards the integrity of the endoplasmic reticulum and organogenesis of the digestive system in zebrafish. Dev Biol 367(2):197-207. doi: 10.1016/j.ydbio.2012.05.004
    • (2012) Dev Biol , vol.367 , Issue.2 , pp. 197-207
    • Niu, X.1    Gao, C.2    Jan Lo, L.3    Luo, Y.4    Meng, C.5    Hong, J.6    Hong, W.7    Peng, J.8
  • 75
    • 84965076810 scopus 로고    scopus 로고
    • Early stages of retinal development depend on Sec13 function
    • 10.1242/bio.20133251 3603407 1:CAS:528:DC%2BC3sXltVWju70%3D
    • Schmidt K, Cavodeassi F, Feng Y, Stephens DJ (2013) Early stages of retinal development depend on Sec13 function. Biol Open 2(3):256-266. doi: 10.1242/bio.20133251
    • (2013) Biol Open , vol.2 , Issue.3 , pp. 256-266
    • Schmidt, K.1    Cavodeassi, F.2    Feng, Y.3    Stephens, D.J.4
  • 76
    • 84899447342 scopus 로고    scopus 로고
    • The nuclear pore complex function of Sec13 protein is required for cell survival during retinal development
    • 10.1074/jbc.M114.547190 4002104 1:CAS:528:DC%2BC2cXmvVSgtrc%3D
    • Niu X, Hong J, Zheng X, Melville DB, Knapik EW, Meng A, Peng J (2014) The nuclear pore complex function of Sec13 protein is required for cell survival during retinal development. J Biol Chem 289(17):11971-11985. doi: 10.1074/jbc.M114.547190
    • (2014) J Biol Chem , vol.289 , Issue.17 , pp. 11971-11985
    • Niu, X.1    Hong, J.2    Zheng, X.3    Melville, D.B.4    Knapik, E.W.5    Meng, A.6    Peng, J.7
  • 79
    • 0030771853 scopus 로고    scopus 로고
    • COPII subunit interactions in the assembly of the vesicle coat
    • 1:CAS:528:DyaK2sXms1Cru7g%3D
    • Shaywitz DA, Espenshade PJ, Gimeno RE, Kaiser CA (1997) COPII subunit interactions in the assembly of the vesicle coat. J Biol Chem 272(41):25413-25416
    • (1997) J Biol Chem , vol.272 , Issue.41 , pp. 25413-25416
    • Shaywitz, D.A.1    Espenshade, P.J.2    Gimeno, R.E.3    Kaiser, C.A.4
  • 81
    • 61449242669 scopus 로고    scopus 로고
    • TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites
    • 10.1016/j.cell.2008.12.025 1:CAS:528:DC%2BD1MXltFSnsLk%3D
    • Saito K, Chen M, Bard F, Chen S, Zhou H, Woodley D, Polischuk R, Schekman R, Malhotra V (2009) TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites. Cell 136(5):891-902. doi: 10.1016/j.cell.2008.12.025
    • (2009) Cell , vol.136 , Issue.5 , pp. 891-902
    • Saito, K.1    Chen, M.2    Bard, F.3    Chen, S.4    Zhou, H.5    Woodley, D.6    Polischuk, R.7    Schekman, R.8    Malhotra, V.9
  • 83
    • 0020569249 scopus 로고
    • Embryonic lethal mutation in mice induced by retrovirus insertion into the alpha 1(I) collagen gene
    • 1:CAS:528:DyaL3sXkvVehsbk%3D
    • Schnieke A, Harbers K, Jaenisch R (1983) Embryonic lethal mutation in mice induced by retrovirus insertion into the alpha 1(I) collagen gene. Nature 304(5924):315-320
    • (1983) Nature , vol.304 , Issue.5924 , pp. 315-320
    • Schnieke, A.1    Harbers, K.2    Jaenisch, R.3
  • 84
    • 84873813295 scopus 로고    scopus 로고
    • A Rab10-dependent mechanism for polarized basement membrane secretion during organ morphogenesis
    • 10.1016/j.devcel.2012.12.005 3562474 1:CAS:528:DC%2BC3sXhs1emtb0%3D
    • Lerner DW, McCoy D, Isabella AJ, Mahowald AP, Gerlach GF, Chaudhry TA, Horne-Badovinac S (2013) A Rab10-dependent mechanism for polarized basement membrane secretion during organ morphogenesis. Dev Cell 24(2):159-168. doi: 10.1016/j.devcel.2012.12.005
    • (2013) Dev Cell , vol.24 , Issue.2 , pp. 159-168
    • Lerner, D.W.1    McCoy, D.2    Isabella, A.J.3    Mahowald, A.P.4    Gerlach, G.F.5    Chaudhry, T.A.6    Horne-Badovinac, S.7
  • 85
    • 79961238713 scopus 로고    scopus 로고
    • Shaping cells and organs in Drosophila by opposing roles of fat body-secreted collagen IV and perlecan
    • 10.1016/j.devcel.2011.06.026 4153364 1:CAS:528:DC%2BC3MXhtVWqurvN
    • Pastor-Pareja JC, Xu T (2011) Shaping cells and organs in Drosophila by opposing roles of fat body-secreted collagen IV and perlecan. Dev Cell 21(2):245-256. doi: 10.1016/j.devcel.2011.06.026
    • (2011) Dev Cell , vol.21 , Issue.2 , pp. 245-256
    • Pastor-Pareja, J.C.1    Xu, T.2
  • 86
    • 0030714173 scopus 로고    scopus 로고
    • CDNA cloning and chromosomal mapping of a predicted coiled-coil proline-rich protein immunogenic in meningioma patients
    • 1:CAS:528:DyaK2sXntFWrt74%3D
    • Heckel D, Brass N, Fischer U, Blin N, Steudel I, Tureci O, Fackler O, Zang KD, Meese E (1997) cDNA cloning and chromosomal mapping of a predicted coiled-coil proline-rich protein immunogenic in meningioma patients. Hum Mol Genet 6(12):2031-2041
    • (1997) Hum Mol Genet , vol.6 , Issue.12 , pp. 2031-2041
    • Heckel, D.1    Brass, N.2    Fischer, U.3    Blin, N.4    Steudel, I.5    Tureci, O.6    Fackler, O.7    Zang, K.D.8    Meese, E.9
  • 87
    • 0037050211 scopus 로고    scopus 로고
    • MGEA6 is tumor-specific overexpressed and frequently recognized by patient-serum antibodies
    • 10.1038/sj.onc.1205005 1:CAS:528:DC%2BD38XhtVejt7w%3D
    • Comtesse N, Niedermayer I, Glass B, Heckel D, Maldener E, Nastainczyk W, Feiden W, Meese E (2002) MGEA6 is tumor-specific overexpressed and frequently recognized by patient-serum antibodies. Oncogene 21(2):239-247. doi: 10.1038/sj.onc.1205005
    • (2002) Oncogene , vol.21 , Issue.2 , pp. 239-247
    • Comtesse, N.1    Niedermayer, I.2    Glass, B.3    Heckel, D.4    Maldener, E.5    Nastainczyk, W.6    Feiden, W.7    Meese, E.8
  • 88
    • 0041842691 scopus 로고    scopus 로고
    • CTAGE: A cutaneous T cell lymphoma associated antigen family with tumor-specific splicing
    • 10.1046/j.1523-1747.2003.12318.x 1:CAS:528:DC%2BD3sXmtVegt70%3D
    • Usener D, Schadendorf D, Koch J, Dubel S, Eichmuller S (2003) cTAGE: a cutaneous T cell lymphoma associated antigen family with tumor-specific splicing. J Invest Dermatol 121(1):198-206. doi: 10.1046/j.1523-1747.2003.12318.x
    • (2003) J Invest Dermatol , vol.121 , Issue.1 , pp. 198-206
    • Usener, D.1    Schadendorf, D.2    Koch, J.3    Dubel, S.4    Eichmuller, S.5
  • 89
    • 33745119426 scopus 로고    scopus 로고
    • The tumour antigens RAGE-1 and MGEA6 are expressed more frequently in the less lineage restricted subgroups of presentation acute myeloid leukaemia
    • 10.1111/j.1365-2141.2006.06135.x 1:CAS:528:DC%2BD28Xot1ahtbk%3D
    • Guinn BA, Gilkes AF, Mufti GJ, Burnett AK, Mills KI (2006) The tumour antigens RAGE-1 and MGEA6 are expressed more frequently in the less lineage restricted subgroups of presentation acute myeloid leukaemia. Br J Haematol 134(2):238-239. doi: 10.1111/j.1365-2141.2006.06135.x
    • (2006) Br J Haematol , vol.134 , Issue.2 , pp. 238-239
    • Guinn, B.A.1    Gilkes, A.F.2    Mufti, G.J.3    Burnett, A.K.4    Mills, K.I.5
  • 90
    • 79959883614 scopus 로고    scopus 로고
    • CTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites
    • 10.1091/mbc.E11-02-0143 3128532 1:CAS:528:DC%2BC3MXptVaitrc%3D
    • Saito K, Yamashiro K, Ichikawa Y, Erlmann P, Kontani K, Malhotra V, Katada T (2011) cTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites. Mol Biol Cell 22(13):2301-2308. doi: 10.1091/mbc.E11-02-0143
    • (2011) Mol Biol Cell , vol.22 , Issue.13 , pp. 2301-2308
    • Saito, K.1    Yamashiro, K.2    Ichikawa, Y.3    Erlmann, P.4    Kontani, K.5    Malhotra, V.6    Katada, T.7
  • 91
    • 0034972470 scopus 로고    scopus 로고
    • The MGEA6 multigene family has an active locus on 14q and at least nine pseudogenes on different chromosomes
    • 10.1006/geno.2001.6576 1:CAS:528:DC%2BD3MXltlGhsbc%3D
    • Comtesse N, Reus K, Meese E (2001) The MGEA6 multigene family has an active locus on 14q and at least nine pseudogenes on different chromosomes. Genomics 75(1-3):43-48. doi: 10.1006/geno.2001.6576
    • (2001) Genomics , vol.75 , Issue.1-3 , pp. 43-48
    • Comtesse, N.1    Reus, K.2    Meese, E.3
  • 92
    • 80053182614 scopus 로고    scopus 로고
    • Reduced cholesterol and triglycerides in mice with a mutation in Mia2, a liver protein that localizes to ER exit sites
    • 10.1194/jlr.M017277 3173003 1:CAS:528:DC%2BC3MXht1Skt7rP
    • Pitman JL, Bonnet DJ, Curtiss LK, Gekakis N (2011) Reduced cholesterol and triglycerides in mice with a mutation in Mia2, a liver protein that localizes to ER exit sites. J Lipid Res 52(10):1775-1786. doi: 10.1194/jlr.M017277
    • (2011) J Lipid Res , vol.52 , Issue.10 , pp. 1775-1786
    • Pitman, J.L.1    Bonnet, D.J.2    Curtiss, L.K.3    Gekakis, N.4
  • 93
    • 0037674673 scopus 로고    scopus 로고
    • Specific expression and regulation of the new melanoma inhibitory activity-related gene MIA2 in hepatocytes
    • 10.1074/jbc.M212639200 1:CAS:528:DC%2BD3sXjtVClsb8%3D
    • Bosserhoff AK, Moser M, Scholmerich J, Buettner R, Hellerbrand C (2003) Specific expression and regulation of the new melanoma inhibitory activity-related gene MIA2 in hepatocytes. J Biol Chem 278(17):15225-15231. doi: 10.1074/jbc.M212639200
    • (2003) J Biol Chem , vol.278 , Issue.17 , pp. 15225-15231
    • Bosserhoff, A.K.1    Moser, M.2    Scholmerich, J.3    Buettner, R.4    Hellerbrand, C.5
  • 95
    • 38549175151 scopus 로고    scopus 로고
    • The novel gene MIA2 acts as a tumour suppressor in hepatocellular carcinoma
    • 10.1136/gut.2007.129544 1:CAS:528:DC%2BD1cXisVyjsLs%3D
    • Hellerbrand C, Amann T, Schlegel J, Wild P, Bataille F, Spruss T, Hartmann A, Bosserhoff AK (2008) The novel gene MIA2 acts as a tumour suppressor in hepatocellular carcinoma. Gut 57(2):243-251. doi: 10.1136/gut.2007.129544
    • (2008) Gut , vol.57 , Issue.2 , pp. 243-251
    • Hellerbrand, C.1    Amann, T.2    Schlegel, J.3    Wild, P.4    Bataille, F.5    Spruss, T.6    Hartmann, A.7    Bosserhoff, A.K.8
  • 96
    • 84876489901 scopus 로고    scopus 로고
    • Protumoral roles of melanoma inhibitory activity 2 in oral squamous cell carcinoma
    • 10.1038/bjc.2013.27 3629429 1:CAS:528:DC%2BC3sXmt1OjsLs%3D
    • Kurihara M, Kirita T, Sasahira T, Ohmori H, Matsushima S, Yamamoto K, Bosserhoff AK, Kuniyasu H (2013) Protumoral roles of melanoma inhibitory activity 2 in oral squamous cell carcinoma. Br J Cancer 108(7):1460-1469. doi: 10.1038/bjc.2013.27
    • (2013) Br J Cancer , vol.108 , Issue.7 , pp. 1460-1469
    • Kurihara, M.1    Kirita, T.2    Sasahira, T.3    Ohmori, H.4    Matsushima, S.5    Yamamoto, K.6    Bosserhoff, A.K.7    Kuniyasu, H.8
  • 97
    • 84959373394 scopus 로고    scopus 로고
    • A common genetic variation of melanoma inhibitory activity-2 labels a subtype of pancreatic adenocarcinoma with high endoplasmic reticulum stress levels
    • 10.1038/srep08109 4319175 1:CAS:528:DC%2BC2MXhtFKju7bO
    • Kong B, Wu W, Valkovska N, Jager C, Hong X, Nitsche U, Friess H, Esposito I, Erkan M, Kleeff J, Michalski CW (2015) A common genetic variation of melanoma inhibitory activity-2 labels a subtype of pancreatic adenocarcinoma with high endoplasmic reticulum stress levels. Sci Rep 5:8109. doi: 10.1038/srep08109
    • (2015) Sci Rep , vol.5 , pp. 8109
    • Kong, B.1    Wu, W.2    Valkovska, N.3    Jager, C.4    Hong, X.5    Nitsche, U.6    Friess, H.7    Esposito, I.8    Erkan, M.9    Kleeff, J.10    Michalski, C.W.11
  • 98
    • 80052226774 scopus 로고    scopus 로고
    • Protein export at the ER: Loading big collagens into COPII carriers
    • 10.1038/emboj.2011.255 3181478 1:CAS:528:DC%2BC3MXhtFSltb3E
    • Malhotra V, Erlmann P (2011) Protein export at the ER: loading big collagens into COPII carriers. EMBO J 30(17):3475-3480. doi: 10.1038/emboj.2011.255
    • (2011) EMBO J , vol.30 , Issue.17 , pp. 3475-3480
    • Malhotra, V.1    Erlmann, P.2
  • 99
    • 84907072338 scopus 로고    scopus 로고
    • Concentration of Sec12 at ER exit sites via interaction with cTAGE5 is required for collagen export
    • 10.1083/jcb.201312062 4164946 1:CAS:528:DC%2BC2cXhs1enu77E
    • Saito K, Yamashiro K, Shimazu N, Tanabe T, Kontani K, Katada T (2014) Concentration of Sec12 at ER exit sites via interaction with cTAGE5 is required for collagen export. J Cell Biol 206(6):751-762. doi: 10.1083/jcb.201312062
    • (2014) J Cell Biol , vol.206 , Issue.6 , pp. 751-762
    • Saito, K.1    Yamashiro, K.2    Shimazu, N.3    Tanabe, T.4    Kontani, K.5    Katada, T.6
  • 100
    • 84871556241 scopus 로고    scopus 로고
    • The structure of Sec12 implicates potassium ion coordination in Sar1 activation
    • 10.1074/jbc.M112.420141 3527946 1:CAS:528:DC%2BC38XhvVOrt73E
    • McMahon C, Studer SM, Clendinen C, Dann GP, Jeffrey PD, Hughson FM (2012) The structure of Sec12 implicates potassium ion coordination in Sar1 activation. J Biol Chem 287(52):43599-43606. doi: 10.1074/jbc.M112.420141
    • (2012) J Biol Chem , vol.287 , Issue.52 , pp. 43599-43606
    • McMahon, C.1    Studer, S.M.2    Clendinen, C.3    Dann, G.P.4    Jeffrey, P.D.5    Hughson, F.M.6
  • 101
    • 0036193747 scopus 로고    scopus 로고
    • Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif
    • 1:CAS:528:DC%2BD38Xit1Gltbs%3D
    • Yamaguchi T, Dulubova I, Min SW, Chen X, Rizo J, Sudhof TC (2002) Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Dev Cell 2(3):295-305
    • (2002) Dev Cell , vol.2 , Issue.3 , pp. 295-305
    • Yamaguchi, T.1    Dulubova, I.2    Min, S.W.3    Chen, X.4    Rizo, J.5    Sudhof, T.C.6
  • 102
    • 0033840553 scopus 로고    scopus 로고
    • Syntaxin 17 is abundant in steroidogenic cells and implicated in smooth endoplasmic reticulum membrane dynamics
    • 14951 1:CAS:528:DC%2BD3cXmtV2rtbk%3D
    • Steegmaier M, Oorschot V, Klumperman J, Scheller RH (2000) Syntaxin 17 is abundant in steroidogenic cells and implicated in smooth endoplasmic reticulum membrane dynamics. Mol Biol Cell 11(8):2719-2731
    • (2000) Mol Biol Cell , vol.11 , Issue.8 , pp. 2719-2731
    • Steegmaier, M.1    Oorschot, V.2    Klumperman, J.3    Scheller, R.H.4
  • 103
    • 84900992942 scopus 로고    scopus 로고
    • SLY1 and Syntaxin 18 specify a distinct pathway for procollagen VII export from the endoplasmic reticulum
    • 10.7554/eLife.02784 4054776
    • Nogueira C, Erlmann P, Villeneuve J, Santos AJ, Martinez-Alonso E, Martinez-Menarguez JA, Malhotra V (2014) SLY1 and Syntaxin 18 specify a distinct pathway for procollagen VII export from the endoplasmic reticulum. eLife 3:e02784. doi: 10.7554/eLife.02784
    • (2014) ELife , vol.3 , pp. e02784
    • Nogueira, C.1    Erlmann, P.2    Villeneuve, J.3    Santos, A.J.4    Martinez-Alonso, E.5    Martinez-Menarguez, J.A.6    Malhotra, V.7
  • 104
    • 84921720415 scopus 로고    scopus 로고
    • Procollagen export from the endoplasmic reticulum
    • 10.1042/BST20140286 1:CAS:528:DC%2BC2MXhsV2msbg%3D
    • Malhotra V, Erlmann P, Nogueira C (2015) Procollagen export from the endoplasmic reticulum. Biochem Soc Trans 43(1):104-107. doi: 10.1042/BST20140286
    • (2015) Biochem Soc Trans , vol.43 , Issue.1 , pp. 104-107
    • Malhotra, V.1    Erlmann, P.2    Nogueira, C.3
  • 105
    • 84857377700 scopus 로고    scopus 로고
    • Ubiquitin-dependent regulation of COPII coat size and function
    • 10.1038/nature10822 3292188 1:CAS:528:DC%2BC38Xis1Cjtbw%3D
    • Jin L, Pahuja KB, Wickliffe KE, Gorur A, Baumgartel C, Schekman R, Rape M (2012) Ubiquitin-dependent regulation of COPII coat size and function. Nature 482(7386):495-500. doi: 10.1038/nature10822
    • (2012) Nature , vol.482 , Issue.7386 , pp. 495-500
    • Jin, L.1    Pahuja, K.B.2    Wickliffe, K.E.3    Gorur, A.4    Baumgartel, C.5    Schekman, R.6    Rape, M.7
  • 106
    • 77958487311 scopus 로고    scopus 로고
    • TRAPP complexes in membrane traffic: Convergence through a common Rab
    • 10.1038/nrm2999 1:CAS:528:DC%2BC3cXhtlWmu7bO
    • Barrowman J, Bhandari D, Reinisch K, Ferro-Novick S (2010) TRAPP complexes in membrane traffic: convergence through a common Rab. Nat Rev Mol Cell Biol 11(11):759-763. doi: 10.1038/nrm2999
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.11 , pp. 759-763
    • Barrowman, J.1    Bhandari, D.2    Reinisch, K.3    Ferro-Novick, S.4
  • 109
    • 0033991176 scopus 로고    scopus 로고
    • A proposed model for the assembly of chylomicrons
    • 1:STN:280:DC%2BD3c%2FkslKqsA%3D%3D
    • Hussain MM (2000) A proposed model for the assembly of chylomicrons. Atherosclerosis 148(1):1-15
    • (2000) Atherosclerosis , vol.148 , Issue.1 , pp. 1-15
    • Hussain, M.M.1
  • 110
    • 0017737407 scopus 로고
    • Electron microscopic studies of the assembly, intracellular transport, and secretion of chylomicrons by rat intestine
    • 1:STN:280:DyaE2s3ltFWqsQ%3D%3D
    • Sabesin SM, Frase S (1977) Electron microscopic studies of the assembly, intracellular transport, and secretion of chylomicrons by rat intestine. J Lipid Res 18(4):496-511
    • (1977) J Lipid Res , vol.18 , Issue.4 , pp. 496-511
    • Sabesin, S.M.1    Frase, S.2
  • 112
    • 37049038447 scopus 로고    scopus 로고
    • Anderson or chylomicron retention disease: Molecular impact of five mutations in the SAR1B gene on the structure and the functionality of Sar1b protein
    • 10.1016/j.ymgme.2007.08.120 1:CAS:528:DC%2BD2sXhsVCjsb%2FM
    • Charcosset M, Sassolas A, Peretti N, Roy CC, Deslandres C, Sinnett D, Levy E, Lachaux A (2008) Anderson or chylomicron retention disease: molecular impact of five mutations in the SAR1B gene on the structure and the functionality of Sar1b protein. Mol Genet Metab 93(1):74-84. doi: 10.1016/j.ymgme.2007.08.120
    • (2008) Mol Genet Metab , vol.93 , Issue.1 , pp. 74-84
    • Charcosset, M.1    Sassolas, A.2    Peretti, N.3    Roy, C.C.4    Deslandres, C.5    Sinnett, D.6    Levy, E.7    Lachaux, A.8
  • 113
    • 77957171872 scopus 로고    scopus 로고
    • Guidelines for the diagnosis and management of chylomicron retention disease based on a review of the literature and the experience of two centers
    • Department of Nutrition-Hepatogastroenterology HFMEBUL Department of Pediatrics CHUS-JRCUdM 10.1186/1750-1172-5-24 2956717
    • Peretti N, Sassolas A, Roy CC, Deslandres C, Charcosset M, Castagnetti J, Pugnet-Chardon L, Moulin P, Labarge S, Bouthillier L, Lachaux A, Levy E, Department of Nutrition-Hepatogastroenterology HFMEBUL, Department of Pediatrics CHUS-JRCUdM (2010) Guidelines for the diagnosis and management of chylomicron retention disease based on a review of the literature and the experience of two centers. Orphanet J Rare Dis 5:24. doi: 10.1186/1750-1172-5-24
    • (2010) Orphanet J Rare Dis , vol.5 , pp. 24
    • Peretti, N.1    Sassolas, A.2    Roy, C.C.3    Deslandres, C.4    Charcosset, M.5    Castagnetti, J.6    Pugnet-Chardon, L.7    Moulin, P.8    Labarge, S.9    Bouthillier, L.10    Lachaux, A.11    Levy, E.12
  • 114
    • 84922466650 scopus 로고    scopus 로고
    • Animal model of Sar1b deficiency presents lipid absorption deficits similar to Anderson disease
    • 10.1007/s00109-014-1247-x 1:CAS:528:DC%2BC2MXosFaqug%3D%3D
    • Levic DS, Minkel J, Wang W, Rybski WM, Melville DB, Knapik EW (2015) Animal model of Sar1b deficiency presents lipid absorption deficits similar to Anderson disease. J Mol Med 93(2):165-176. doi: 10.1007/s00109-014-1247-x
    • (2015) J Mol Med , vol.93 , Issue.2 , pp. 165-176
    • Levic, D.S.1    Minkel, J.2    Wang, W.3    Rybski, W.M.4    Melville, D.B.5    Knapik, E.W.6
  • 115
    • 46049089793 scopus 로고    scopus 로고
    • Coordination of COPII vesicle trafficking by Sec23
    • 10.1016/j.tcb.2008.04.006 1:CAS:528:DC%2BD1cXotlCktrg%3D
    • Fromme JC, Orci L, Schekman R (2008) Coordination of COPII vesicle trafficking by Sec23. Trends Cell Biol 18(7):330-336. doi: 10.1016/j.tcb.2008.04.006
    • (2008) Trends Cell Biol , vol.18 , Issue.7 , pp. 330-336
    • Fromme, J.C.1    Orci, L.2    Schekman, R.3
  • 116
    • 48649098177 scopus 로고    scopus 로고
    • Structural basis for cargo regulation of COPII coat assembly
    • 10.1016/j.cell.2008.06.024 2649882 1:CAS:528:DC%2BD1cXhtVSis7%2FJ
    • Stagg SM, LaPointe P, Razvi A, Gurkan C, Potter CS, Carragher B, Balch WE (2008) Structural basis for cargo regulation of COPII coat assembly. Cell 134(3):474-484. doi: 10.1016/j.cell.2008.06.024
    • (2008) Cell , vol.134 , Issue.3 , pp. 474-484
    • Stagg, S.M.1    LaPointe, P.2    Razvi, A.3    Gurkan, C.4    Potter, C.S.5    Carragher, B.6    Balch, W.E.7
  • 117
    • 78751580416 scopus 로고    scopus 로고
    • The structure of a COPII tubule
    • 10.1016/j.jsb.2010.09.002
    • O'Donnell J, Maddox K, Stagg S (2011) The structure of a COPII tubule. J Struct Biol 173(2):358-364. doi: 10.1016/j.jsb.2010.09.002
    • (2011) J Struct Biol , vol.173 , Issue.2 , pp. 358-364
    • O'Donnell, J.1    Maddox, K.2    Stagg, S.3
  • 118
    • 0035825157 scopus 로고    scopus 로고
    • The Sar1 GTPase coordinates biosynthetic cargo selection with endoplasmic reticulum export site assembly
    • 2193666 1:CAS:528:DC%2BD3MXjslyhtg%3D%3D
    • Aridor M, Fish KN, Bannykh S, Weissman J, Roberts TH, Lippincott-Schwartz J, Balch WE (2001) The Sar1 GTPase coordinates biosynthetic cargo selection with endoplasmic reticulum export site assembly. J Cell Biol 152(1):213-229
    • (2001) J Cell Biol , vol.152 , Issue.1 , pp. 213-229
    • Aridor, M.1    Fish, K.N.2    Bannykh, S.3    Weissman, J.4    Roberts, T.H.5    Lippincott-Schwartz, J.6    Balch, W.E.7
  • 120
    • 77954708485 scopus 로고    scopus 로고
    • Sar1 assembly regulates membrane constriction and ER export
    • 10.1083/jcb.201004132 2911667 1:CAS:528:DC%2BC3cXpsVOhtLg%3D
    • Long KR, Yamamoto Y, Baker AL, Watkins SC, Coyne CB, Conway JF, Aridor M (2010) Sar1 assembly regulates membrane constriction and ER export. J Cell Biol 190(1):115-128. doi: 10.1083/jcb.201004132
    • (2010) J Cell Biol , vol.190 , Issue.1 , pp. 115-128
    • Long, K.R.1    Yamamoto, Y.2    Baker, A.L.3    Watkins, S.C.4    Coyne, C.B.5    Conway, J.F.6    Aridor, M.7
  • 121
    • 84884689359 scopus 로고    scopus 로고
    • The structure of the COPII transport-vesicle coat assembled on membranes
    • 10.7554/eLife.00951 3778437
    • Zanetti G, Prinz S, Daum S, Meister A, Schekman R, Bacia K, Briggs JA (2013) The structure of the COPII transport-vesicle coat assembled on membranes. eLife 2:e00951. doi: 10.7554/eLife.00951
    • (2013) ELife , vol.2 , pp. e00951
    • Zanetti, G.1    Prinz, S.2    Daum, S.3    Meister, A.4    Schekman, R.5    Bacia, K.6    Briggs, J.A.7
  • 122
    • 84908199281 scopus 로고    scopus 로고
    • Insights into the mechanisms of membrane curvature and vesicle scission by the small GTPase Sar1 in the early secretory pathway
    • 10.1016/j.jmb.2014.08.023 1:CAS:528:DC%2BC2cXhsV2kt7jN
    • Hariri H, Bhattacharya N, Johnson K, Noble AJ, Stagg SM (2014) Insights into the mechanisms of membrane curvature and vesicle scission by the small GTPase Sar1 in the early secretory pathway. J Mol Biol 426(22):3811-3826. doi: 10.1016/j.jmb.2014.08.023
    • (2014) J Mol Biol , vol.426 , Issue.22 , pp. 3811-3826
    • Hariri, H.1    Bhattacharya, N.2    Johnson, K.3    Noble, A.J.4    Stagg, S.M.5
  • 123
    • 84862216994 scopus 로고    scopus 로고
    • The structure of the Sec13/31 COPII cage bound to Sec23
    • 10.1016/j.jmb.2012.04.024 3377835 1:CAS:528:DC%2BC38XntlSrsbs%3D
    • Bhattacharya N, O Donnell J, Stagg SM (2012) The structure of the Sec13/31 COPII cage bound to Sec23. J Mol Biol 420(4-5):324-334. doi: 10.1016/j.jmb.2012.04.024
    • (2012) J Mol Biol , vol.420 , Issue.4-5 , pp. 324-334
    • Bhattacharya, N.1    Donnell, J.O.2    Stagg, S.M.3
  • 125
    • 84873549557 scopus 로고    scopus 로고
    • A pseudoatomic model of the COPII cage obtained from cryo-electron microscopy and mass spectrometry
    • 10.1038/nsmb.2467 3565055 1:CAS:528:DC%2BC38XhvVOqsrvE
    • Noble AJ, Zhang Q, O'Donnell J, Hariri H, Bhattacharya N, Marshall AG, Stagg SM (2013) A pseudoatomic model of the COPII cage obtained from cryo-electron microscopy and mass spectrometry. Nat Struct Mol Biol 20(2):167-173. doi: 10.1038/nsmb.2467
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.2 , pp. 167-173
    • Noble, A.J.1    Zhang, Q.2    O'Donnell, J.3    Hariri, H.4    Bhattacharya, N.5    Marshall, A.G.6    Stagg, S.M.7
  • 126
    • 55549137036 scopus 로고    scopus 로고
    • Structural basis of cargo membrane protein discrimination by the human COPII coat machinery
    • 10.1038/emboj.2008.208 2580787 1:CAS:528:DC%2BD1cXhtlaltL7M
    • Mancias JD, Goldberg J (2008) Structural basis of cargo membrane protein discrimination by the human COPII coat machinery. EMBO J 27(21):2918-2928. doi: 10.1038/emboj.2008.208
    • (2008) EMBO J , vol.27 , Issue.21 , pp. 2918-2928
    • Mancias, J.D.1    Goldberg, J.2
  • 127
    • 34250745253 scopus 로고    scopus 로고
    • Structure and organization of coat proteins in the COPII cage
    • 10.1016/j.cell.2007.05.036 1:CAS:528:DC%2BD2sXotV2hsL8%3D
    • Fath S, Mancias JD, Bi X, Goldberg J (2007) Structure and organization of coat proteins in the COPII cage. Cell 129(7):1325-1336. doi: 10.1016/j.cell.2007.05.036
    • (2007) Cell , vol.129 , Issue.7 , pp. 1325-1336
    • Fath, S.1    Mancias, J.D.2    Bi, X.3    Goldberg, J.4
  • 128
    • 84858323525 scopus 로고    scopus 로고
    • ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p
    • 10.1126/science.1215909 3306526 1:CAS:528:DC%2BC38Xjs1Slsro%3D
    • Copic A, Latham CF, Horlbeck MA, D'Arcangelo JG, Miller EA (2012) ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p. Science 335(6074):1359-1362. doi: 10.1126/science.1215909
    • (2012) Science , vol.335 , Issue.6074 , pp. 1359-1362
    • Copic, A.1    Latham, C.F.2    Horlbeck, M.A.3    D'Arcangelo, J.G.4    Miller, E.A.5
  • 129
    • 84872511567 scopus 로고    scopus 로고
    • CK2 phosphorylates Sec31 and regulates ER-To-Golgi trafficking
    • 10.1371/journal.pone.0054382 3548793 1:CAS:528:DC%2BC3sXhvFCitrs%3D
    • Koreishi M, Yu S, Oda M, Honjo Y, Satoh A (2013) CK2 phosphorylates Sec31 and regulates ER-To-Golgi trafficking. PLoS One 8(1):e54382. doi: 10.1371/journal.pone.0054382
    • (2013) PLoS One , vol.8 , Issue.1 , pp. e54382
    • Koreishi, M.1    Yu, S.2    Oda, M.3    Honjo, Y.4    Satoh, A.5
  • 130
    • 79955880405 scopus 로고    scopus 로고
    • Sequential interactions with Sec23 control the direction of vesicle traffic
    • 10.1038/nature09969 3093450 1:CAS:528:DC%2BC3MXlsVGlsr0%3D
    • Lord C, Bhandari D, Menon S, Ghassemian M, Nycz D, Hay J, Ghosh P, Ferro-Novick S (2011) Sequential interactions with Sec23 control the direction of vesicle traffic. Nature 473(7346):181-186. doi: 10.1038/nature09969
    • (2011) Nature , vol.473 , Issue.7346 , pp. 181-186
    • Lord, C.1    Bhandari, D.2    Menon, S.3    Ghassemian, M.4    Nycz, D.5    Hay, J.6    Ghosh, P.7    Ferro-Novick, S.8
  • 131
    • 84883376346 scopus 로고    scopus 로고
    • Sit4p/PP6 regulates ER-to-Golgi traffic by controlling the dephosphorylation of COPII coat subunits
    • 10.1091/mbc.E13-02-0114 3756924 1:CAS:528:DC%2BC3sXhsVSgtr3L
    • Bhandari D, Zhang J, Menon S, Lord C, Chen S, Helm JR, Thorsen K, Corbett KD, Hay JC, Ferro-Novick S (2013) Sit4p/PP6 regulates ER-to-Golgi traffic by controlling the dephosphorylation of COPII coat subunits. Mol Biol Cell 24(17):2727-2738. doi: 10.1091/mbc.E13-02-0114
    • (2013) Mol Biol Cell , vol.24 , Issue.17 , pp. 2727-2738
    • Bhandari, D.1    Zhang, J.2    Menon, S.3    Lord, C.4    Chen, S.5    Helm, J.R.6    Thorsen, K.7    Corbett, K.D.8    Hay, J.C.9    Ferro-Novick, S.10
  • 133
  • 136
    • 77950494599 scopus 로고    scopus 로고
    • Planar cell polarity defects and defective Vangl2 trafficking in mutants for the COPII gene Sec24b
    • 10.1242/dev.041434 1:CAS:528:DC%2BC3cXmtleju7g%3D
    • Wansleeben C, Feitsma H, Montcouquiol M, Kroon C, Cuppen E, Meijlink F (2010) Planar cell polarity defects and defective Vangl2 trafficking in mutants for the COPII gene Sec24b. Development 137(7):1067-1073. doi: 10.1242/dev.041434
    • (2010) Development , vol.137 , Issue.7 , pp. 1067-1073
    • Wansleeben, C.1    Feitsma, H.2    Montcouquiol, M.3    Kroon, C.4    Cuppen, E.5    Meijlink, F.6
  • 137
    • 84862999072 scopus 로고    scopus 로고
    • Sec24b selectively sorts Vangl2 to regulate planar cell polarity during neural tube closure
    • 10.1038/ncb2002 2823131 1:CAS:528:DC%2BD1MXhsFynurrN
    • Merte J, Jensen D, Wright K, Sarsfield S, Wang Y, Schekman R, Ginty DD (2010) Sec24b selectively sorts Vangl2 to regulate planar cell polarity during neural tube closure. Nat Cell Biol 12(1):41-46. doi: 10.1038/ncb2002
    • (2010) Nat Cell Biol , vol.12 , Issue.1 , pp. 41-46
    • Merte, J.1    Jensen, D.2    Wright, K.3    Sarsfield, S.4    Wang, Y.5    Schekman, R.6    Ginty, D.D.7
  • 138
    • 84905408055 scopus 로고    scopus 로고
    • Mammalian COPII coat component SEC24C is required for embryonic development in mice
    • 10.1074/jbc.M114.566687 4110293 1:CAS:528:DC%2BC2cXht1Sksb%2FN
    • Adams EJ, Chen XW, O'Shea KS, Ginsburg D (2014) Mammalian COPII coat component SEC24C is required for embryonic development in mice. J Biol Chem 289(30):20858-20870. doi: 10.1074/jbc.M114.566687
    • (2014) J Biol Chem , vol.289 , Issue.30 , pp. 20858-20870
    • Adams, E.J.1    Chen, X.W.2    O'Shea, K.S.3    Ginsburg, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.