메뉴 건너뛰기




Volumn 19, Issue 8, 2014, Pages 508-515

Retention mechanisms for ER and Golgi membrane proteins

Author keywords

COPI subpopulations; Dilysine motif; ER retrieval; Golgi retention; KXD E motif

Indexed keywords

ARABIDOPSIS; EUKARYOTA;

EID: 84905175185     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2014.04.004     Document Type: Review
Times cited : (84)

References (75)
  • 1
    • 8444242974 scopus 로고    scopus 로고
    • Bi-directional protein transport between the ER and Golgi
    • Lee M.C., et al. Bi-directional protein transport between the ER and Golgi. Annu. Rev. Cell Dev. Biol. 2004, 20:87-123.
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 87-123
    • Lee, M.C.1
  • 2
    • 34547632308 scopus 로고    scopus 로고
    • Membrane dynamics in the early secretory pathway
    • Robinson D.G., et al. Membrane dynamics in the early secretory pathway. Crit. Rev. Plant Sci. 2007, 26:199-225.
    • (2007) Crit. Rev. Plant Sci. , vol.26 , pp. 199-225
    • Robinson, D.G.1
  • 3
    • 84878253184 scopus 로고    scopus 로고
    • Organization of the ER-Golgi interface for membrane traffic control
    • Brandizzi F., Barlowe C. Organization of the ER-Golgi interface for membrane traffic control. Nat. Rev. Mol. Cell Biol. 2013, 14:382-392.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 382-392
    • Brandizzi, F.1    Barlowe, C.2
  • 4
    • 84891959607 scopus 로고    scopus 로고
    • A crucial role of the RGS domain in Trans-Golgi network export of AtRGS1 in the protein secretory pathway
    • Hu G.Z., et al. A crucial role of the RGS domain in Trans-Golgi network export of AtRGS1 in the protein secretory pathway. Mol. Plant 2013, 6:1933-1944.
    • (2013) Mol. Plant , vol.6 , pp. 1933-1944
    • Hu, G.Z.1
  • 5
    • 84883776424 scopus 로고    scopus 로고
    • Organelle pH in the Arabidopsis endomembrane system
    • Shen J., et al. Organelle pH in the Arabidopsis endomembrane system. Mol. Plant 2013, 6:1419-1437.
    • (2013) Mol. Plant , vol.6 , pp. 1419-1437
    • Shen, J.1
  • 6
    • 84883767223 scopus 로고    scopus 로고
    • An in vivo expression system for the identification of cargo proteins of vacuolar sorting receptors in Arabidopsis culture cells
    • Shen J., et al. An in vivo expression system for the identification of cargo proteins of vacuolar sorting receptors in Arabidopsis culture cells. Plant J. 2013, 75:1003-1017.
    • (2013) Plant J. , vol.75 , pp. 1003-1017
    • Shen, J.1
  • 7
    • 34249787044 scopus 로고    scopus 로고
    • Rice SCAMP1 defines clathrin-coated, trans-golgi-located tubular-vesicular structures as an early endosome in tobacco BY-2 cells
    • Lam S.K., et al. Rice SCAMP1 defines clathrin-coated, trans-golgi-located tubular-vesicular structures as an early endosome in tobacco BY-2 cells. Plant Cell 2007, 19:296-319.
    • (2007) Plant Cell , vol.19 , pp. 296-319
    • Lam, S.K.1
  • 8
    • 84885633266 scopus 로고    scopus 로고
    • Apical F-actin-regulated exocytic targeting of NtPPME1 is essential for construction and rigidity of the pollen tube cell wall
    • Wang H., et al. Apical F-actin-regulated exocytic targeting of NtPPME1 is essential for construction and rigidity of the pollen tube cell wall. Plant J. 2013, 76:367-379.
    • (2013) Plant J. , vol.76 , pp. 367-379
    • Wang, H.1
  • 9
    • 84860360983 scopus 로고    scopus 로고
    • V-ATPase, ScNhx1p and yeast vacuole fusion
    • Qiu Q.S. V-ATPase, ScNhx1p and yeast vacuole fusion. J. Genet. Genomics 2012, 39:167-171.
    • (2012) J. Genet. Genomics , vol.39 , pp. 167-171
    • Qiu, Q.S.1
  • 11
    • 80054729346 scopus 로고    scopus 로고
    • COPII and COPI traffic at the ER-Golgi Interface
    • Szul T., Sztul E. COPII and COPI traffic at the ER-Golgi Interface. Physiology 2011, 26:348-364.
    • (2011) Physiology , vol.26 , pp. 348-364
    • Szul, T.1    Sztul, E.2
  • 12
    • 84867141973 scopus 로고    scopus 로고
    • Retrograde vesicle transport in the Golgi
    • Cottam N.P., Ungar D. Retrograde vesicle transport in the Golgi. Protoplasma 2012, 249:943-955.
    • (2012) Protoplasma , vol.249 , pp. 943-955
    • Cottam, N.P.1    Ungar, D.2
  • 13
    • 84255188602 scopus 로고    scopus 로고
    • COPII and the regulation of protein sorting in mammals
    • Zanetti G., et al. COPII and the regulation of protein sorting in mammals. Nat. Cell Biol. 2012, 14:20-28.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 20-28
    • Zanetti, G.1
  • 14
    • 28444472038 scopus 로고    scopus 로고
    • The maturing role of COPI vesicles in intra-Golgi transport
    • Rabouille C., Klumperman J. The maturing role of COPI vesicles in intra-Golgi transport. Nat. Rev. Mol. Cell Biol. 2005, 6:812-817.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 812-817
    • Rabouille, C.1    Klumperman, J.2
  • 15
    • 77956483922 scopus 로고    scopus 로고
    • COPII-mediated traffic in plants
    • Marti L., et al. COPII-mediated traffic in plants. Trends Plant Sci. 2010, 15:522-528.
    • (2010) Trends Plant Sci. , vol.15 , pp. 522-528
    • Marti, L.1
  • 16
    • 79953026658 scopus 로고    scopus 로고
    • Multiple cytosolic and transmembrane determinants are required for the trafficking of SCAMP1 via an ER-Golgi-TGN-PM pathway
    • Cai Y., et al. Multiple cytosolic and transmembrane determinants are required for the trafficking of SCAMP1 via an ER-Golgi-TGN-PM pathway. Plant J. 2011, 65:882-896.
    • (2011) Plant J. , vol.65 , pp. 882-896
    • Cai, Y.1
  • 17
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic-reticulum retention motifs
    • Cosson P., Letourneur F. Coatomer interaction with di-lysine endoplasmic-reticulum retention motifs. Science 1994, 263:1629-1631.
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 18
    • 12444339783 scopus 로고    scopus 로고
    • Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat
    • Contreras I., et al. Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat. Plant Cell Physiol. 2004, 45:1779-1786.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 1779-1786
    • Contreras, I.1
  • 19
    • 41849085580 scopus 로고    scopus 로고
    • In vivo trafficking and localization of p24 proteins in plant cells
    • Langhans M., et al. In vivo trafficking and localization of p24 proteins in plant cells. Traffic 2008, 9:770-785.
    • (2008) Traffic , vol.9 , pp. 770-785
    • Langhans, M.1
  • 20
    • 84882394999 scopus 로고    scopus 로고
    • Putative p24 complexes in Arabidopsis contain members of the delta and beta subfamilies and cycle in the early secretory pathway
    • Montesinos J.C., et al. Putative p24 complexes in Arabidopsis contain members of the delta and beta subfamilies and cycle in the early secretory pathway. J. Exp. Bot. 2013, 64:3147-3167.
    • (2013) J. Exp. Bot. , vol.64 , pp. 3147-3167
    • Montesinos, J.C.1
  • 21
    • 84866703415 scopus 로고    scopus 로고
    • Coupled transport of Arabidopsis p24 proteins at the ER-Golgi interface
    • Montesinos J.C., et al. Coupled transport of Arabidopsis p24 proteins at the ER-Golgi interface. J. Exp. Bot. 2012, 63:4243-4261.
    • (2012) J. Exp. Bot. , vol.63 , pp. 4243-4261
    • Montesinos, J.C.1
  • 22
    • 0028643562 scopus 로고
    • Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic-reticulum
    • Letourneur F., et al. Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic-reticulum. Cell 1994, 79:1199-1207.
    • (1994) Cell , vol.79 , pp. 1199-1207
    • Letourneur, F.1
  • 23
    • 73749085462 scopus 로고    scopus 로고
    • Localization of Golgi-resident glycosyltransferases
    • Tu L.N., Banfield D.K. Localization of Golgi-resident glycosyltransferases. Cell. Mol. Life Sci. 2010, 67:29-41.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 29-41
    • Tu, L.N.1    Banfield, D.K.2
  • 25
    • 79953185070 scopus 로고    scopus 로고
    • Sub-compartmental organization of Golgi-resident N-glycan processing enzymes in plants
    • Schoberer J., Strasser R. Sub-compartmental organization of Golgi-resident N-glycan processing enzymes in plants. Mol. Plant 2011, 4:220-228.
    • (2011) Mol. Plant , vol.4 , pp. 220-228
    • Schoberer, J.1    Strasser, R.2
  • 26
    • 33845762779 scopus 로고    scopus 로고
    • Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway
    • Saint-Jore-Dupas C., et al. Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway. Plant Cell 2006, 18:3182-3200.
    • (2006) Plant Cell , vol.18 , pp. 3182-3200
    • Saint-Jore-Dupas, C.1
  • 27
    • 0027318045 scopus 로고
    • Kin recognition. A model for the retention of Golgi enzymes
    • Nilsson T., et al. Kin recognition. A model for the retention of Golgi enzymes. FEBS Lett. 1993, 330:1-4.
    • (1993) FEBS Lett. , vol.330 , pp. 1-4
    • Nilsson, T.1
  • 28
    • 52649182178 scopus 로고    scopus 로고
    • The transmembrane domain of the severe acute respiratory syndrome coronavirus ORF7b protein is necessary and sufficient for its retention in the Golgi complex
    • Schaecher S.R., et al. The transmembrane domain of the severe acute respiratory syndrome coronavirus ORF7b protein is necessary and sufficient for its retention in the Golgi complex. J. Virol. 2008, 82:9477-9491.
    • (2008) J. Virol. , vol.82 , pp. 9477-9491
    • Schaecher, S.R.1
  • 29
    • 84863097595 scopus 로고    scopus 로고
    • The Golgi-localized Arabidopsis endomembrane protein12 contains both endoplasmic reticulum export and Golgi retention signals at its C terminus
    • Gao C., et al. The Golgi-localized Arabidopsis endomembrane protein12 contains both endoplasmic reticulum export and Golgi retention signals at its C terminus. Plant Cell 2012, 24:2086-2104.
    • (2012) Plant Cell , vol.24 , pp. 2086-2104
    • Gao, C.1
  • 30
    • 47749141468 scopus 로고    scopus 로고
    • Signal-mediated dynamic retention of glycosyltransferases in the Golgi
    • Tu L., et al. Signal-mediated dynamic retention of glycosyltransferases in the Golgi. Science 2008, 321:404-407.
    • (2008) Science , vol.321 , pp. 404-407
    • Tu, L.1
  • 31
    • 41649090365 scopus 로고    scopus 로고
    • Golgi localization of glycosyltransferases requires a Vps74p oligomer
    • Burd C.G., et al. Golgi localization of glycosyltransferases requires a Vps74p oligomer. Dev. Cell 2008, 14:523-534.
    • (2008) Dev. Cell , vol.14 , pp. 523-534
    • Burd, C.G.1
  • 32
    • 33846041607 scopus 로고    scopus 로고
    • Identification and characterization of COPla- and COPlb-type vesicle classes associated with plant and algal Golgi
    • Donohoe B.S., et al. Identification and characterization of COPla- and COPlb-type vesicle classes associated with plant and algal Golgi. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:163-168.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 163-168
    • Donohoe, B.S.1
  • 33
    • 0035945347 scopus 로고    scopus 로고
    • Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: a role for ArfGAP1
    • Lanoix J., et al. Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: a role for ArfGAP1. J. Cell Biol. 2001, 155:1199-1212.
    • (2001) J. Cell Biol. , vol.155 , pp. 1199-1212
    • Lanoix, J.1
  • 34
    • 13844317835 scopus 로고    scopus 로고
    • Golgin tethers define subpopulations of COPI vesicles
    • Malsam J., et al. Golgin tethers define subpopulations of COPI vesicles. Science 2005, 307:1095-1098.
    • (2005) Science , vol.307 , pp. 1095-1098
    • Malsam, J.1
  • 35
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson M.R., et al. Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J. 1990, 9:3153-3162.
    • (1990) EMBO J. , vol.9 , pp. 3153-3162
    • Jackson, M.R.1
  • 36
    • 0024314706 scopus 로고
    • Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic-reticulum
    • Nilsson T., et al. Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic-reticulum. Cell 1989, 58:707-718.
    • (1989) Cell , vol.58 , pp. 707-718
    • Nilsson, T.1
  • 37
    • 0033883172 scopus 로고    scopus 로고
    • The C-terminal dilysine motif confers endoplasmic reticulum localization to type I membrane proteins in plants
    • Benghezal M., et al. The C-terminal dilysine motif confers endoplasmic reticulum localization to type I membrane proteins in plants. Plant Cell 2000, 12:1179-1201.
    • (2000) Plant Cell , vol.12 , pp. 1179-1201
    • Benghezal, M.1
  • 38
    • 84856775017 scopus 로고    scopus 로고
    • Subclass-specific localization and trafficking of arabidopsis p24 proteins in the ER-Golgi interface
    • Chen J., et al. Subclass-specific localization and trafficking of arabidopsis p24 proteins in the ER-Golgi interface. Traffic 2012, 13:400-415.
    • (2012) Traffic , vol.13 , pp. 400-415
    • Chen, J.1
  • 39
    • 2542632045 scopus 로고    scopus 로고
    • Sorting signals in the cytosolic tail of membrane proteins involved in the interaction with plant ARF1 and coatomer
    • Contreras I., et al. Sorting signals in the cytosolic tail of membrane proteins involved in the interaction with plant ARF1 and coatomer. Plant J. 2004, 38:685-698.
    • (2004) Plant J. , vol.38 , pp. 685-698
    • Contreras, I.1
  • 40
    • 0035956996 scopus 로고    scopus 로고
    • Analysis of endoplasmic reticulum trafficking signals by combinatorial screening in mammalian cells
    • Zerangue N., et al. Analysis of endoplasmic reticulum trafficking signals by combinatorial screening in mammalian cells. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:2431-2436.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2431-2436
    • Zerangue, N.1
  • 41
    • 0032443438 scopus 로고    scopus 로고
    • Alpha-COP can discriminate between distinct, functional di-lysine signals in vitro and regulates access into retrograde transport
    • Schroder-Kohne S., et al. alpha-COP can discriminate between distinct, functional di-lysine signals in vitro and regulates access into retrograde transport. J. Cell Sci. 1998, 111:3459-3470.
    • (1998) J. Cell Sci. , vol.111 , pp. 3459-3470
    • Schroder-Kohne, S.1
  • 42
    • 84875940159 scopus 로고    scopus 로고
    • Rules for the recognition of dilysine retrieval motifs by coatomer
    • Ma W.F., Goldberg J. Rules for the recognition of dilysine retrieval motifs by coatomer. EMBO J. 2013, 32:926-937.
    • (2013) EMBO J. , vol.32 , pp. 926-937
    • Ma, W.F.1    Goldberg, J.2
  • 43
    • 84870826366 scopus 로고    scopus 로고
    • Molecular basis for recognition of dilysine trafficking motifs by COPI
    • Jackson L.P., et al. Molecular basis for recognition of dilysine trafficking motifs by COPI. Dev. Cell 2012, 23:1255-1262.
    • (2012) Dev. Cell , vol.23 , pp. 1255-1262
    • Jackson, L.P.1
  • 44
    • 0141429975 scopus 로고    scopus 로고
    • The retrieval function of the KDEL receptor requires PKA phosphorylation of its C-terminus
    • Cabrera M., et al. The retrieval function of the KDEL receptor requires PKA phosphorylation of its C-terminus. Mol. Biol. Cell 2003, 14:4114-4125.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4114-4125
    • Cabrera, M.1
  • 45
    • 1642523685 scopus 로고    scopus 로고
    • Membrane-bound fatty acid desaturases are inserted co-translationally into the ER and contain different ER retrieval motifs at their carboxy termini
    • McCartney A.W., et al. Membrane-bound fatty acid desaturases are inserted co-translationally into the ER and contain different ER retrieval motifs at their carboxy termini. Plant J. 2004, 37:156-173.
    • (2004) Plant J. , vol.37 , pp. 156-173
    • McCartney, A.W.1
  • 46
    • 68149099015 scopus 로고    scopus 로고
    • Arabidopsis thaliana GPAT8 and GPAT9 are localized to the ER and possess distinct ER retrieval signals: functional divergence of the dilysine ER retrieval motif in plant cells
    • Gidda S.K., et al. Arabidopsis thaliana GPAT8 and GPAT9 are localized to the ER and possess distinct ER retrieval signals: functional divergence of the dilysine ER retrieval motif in plant cells. Plant Physiol. Biochem. 2009, 47:867-879.
    • (2009) Plant Physiol. Biochem. , vol.47 , pp. 867-879
    • Gidda, S.K.1
  • 47
    • 74049141753 scopus 로고    scopus 로고
    • Cytosolic N-terminal arginine-based signals together with a luminal signal target a type II membrane protein to the plant ER
    • Boulaflous A., et al. Cytosolic N-terminal arginine-based signals together with a luminal signal target a type II membrane protein to the plant ER. BMC Plant Biol. 2009, 9:144.
    • (2009) BMC Plant Biol. , vol.9 , pp. 144
    • Boulaflous, A.1
  • 48
    • 77954385031 scopus 로고    scopus 로고
    • A plasma-membrane E-MAP reveals links of the eisosome with sphingolipid metabolism and endosomal trafficking
    • Aguilar P.S., et al. A plasma-membrane E-MAP reveals links of the eisosome with sphingolipid metabolism and endosomal trafficking. Nat. Struct. Mol. Biol. 2010, 17:901-908.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 901-908
    • Aguilar, P.S.1
  • 49
    • 73849124226 scopus 로고    scopus 로고
    • The human homologue of Dictyostelium discoideum phg1A is expressed by human metastatic melanoma cells
    • Lozupone F., et al. The human homologue of Dictyostelium discoideum phg1A is expressed by human metastatic melanoma cells. EMBO Rep. 2009, 10:1348-1354.
    • (2009) EMBO Rep. , vol.10 , pp. 1348-1354
    • Lozupone, F.1
  • 50
    • 58149374223 scopus 로고    scopus 로고
    • High-throughput functional screening for autophagy-related genes and identification of TM9SF1 as an autophagosome-inducing gene
    • He P.F., et al. High-throughput functional screening for autophagy-related genes and identification of TM9SF1 as an autophagosome-inducing gene. Autophagy 2009, 5:52-60.
    • (2009) Autophagy , vol.5 , pp. 52-60
    • He, P.F.1
  • 51
    • 84862262971 scopus 로고    scopus 로고
    • Vacuolar degradation of two integral plasma membrane proteins, AtLRR84A and OsSCAMP1, is cargo ubiquitination-independent and prevacuolar compartment-mediated in plant cells
    • Cai Y., et al. Vacuolar degradation of two integral plasma membrane proteins, AtLRR84A and OsSCAMP1, is cargo ubiquitination-independent and prevacuolar compartment-mediated in plant cells. Traffic 2012, 13:1023-1040.
    • (2012) Traffic , vol.13 , pp. 1023-1040
    • Cai, Y.1
  • 52
    • 0030755580 scopus 로고    scopus 로고
    • Bidirectional transport by distinct populations of COPI-coated vesicles
    • Orci L., et al. Bidirectional transport by distinct populations of COPI-coated vesicles. Cell 1997, 90:335-349.
    • (1997) Cell , vol.90 , pp. 335-349
    • Orci, L.1
  • 53
    • 79751495582 scopus 로고    scopus 로고
    • Electron tomography of RabA4b-and PI-4K beta 1-labeled trans Golgi network compartments in Arabidopsis
    • Kang B.H., et al. Electron tomography of RabA4b-and PI-4K beta 1-labeled trans Golgi network compartments in Arabidopsis. Traffic 2011, 12:313-329.
    • (2011) Traffic , vol.12 , pp. 313-329
    • Kang, B.H.1
  • 54
    • 84876106182 scopus 로고    scopus 로고
    • Cis-Golgi cisternal assembly and biosynthetic activation occur sequentially in plants and algae
    • Donohoe B.S., et al. Cis-Golgi cisternal assembly and biosynthetic activation occur sequentially in plants and algae. Traffic 2013, 14:551-567.
    • (2013) Traffic , vol.14 , pp. 551-567
    • Donohoe, B.S.1
  • 55
    • 84887455695 scopus 로고    scopus 로고
    • A three-stage model of Golgi structure and function
    • Day K.J., et al. A three-stage model of Golgi structure and function. Histochem. Cell Biol. 2013, 140:239-249.
    • (2013) Histochem. Cell Biol. , vol.140 , pp. 239-249
    • Day, K.J.1
  • 56
    • 70450176713 scopus 로고    scopus 로고
    • Transport vesicle formation in plant cells
    • Hwang I., Robinson D.G. Transport vesicle formation in plant cells. Curr. Opin. Plant Biol. 2009, 12:660-669.
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 660-669
    • Hwang, I.1    Robinson, D.G.2
  • 57
    • 69249213354 scopus 로고    scopus 로고
    • The COPI system: molecular mechanisms and function
    • Beck R., et al. The COPI system: molecular mechanisms and function. FEBS Lett. 2009, 583:2701-2709.
    • (2009) FEBS Lett. , vol.583 , pp. 2701-2709
    • Beck, R.1
  • 58
    • 70450223889 scopus 로고    scopus 로고
    • Mechanisms of COPI vesicle formation
    • Hsu V.W., Yang J.S. Mechanisms of COPI vesicle formation. FEBS Lett. 2009, 583:3758-3763.
    • (2009) FEBS Lett. , vol.583 , pp. 3758-3763
    • Hsu, V.W.1    Yang, J.S.2
  • 59
    • 77954915341 scopus 로고    scopus 로고
    • Crystal structure of alpha-COP in complex with epsilon-COP provides insight into the architecture of the COPI vesicular coat
    • Hsia K.C., Hoelz A. Crystal structure of alpha-COP in complex with epsilon-COP provides insight into the architecture of the COPI vesicular coat. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:11271-11276.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 11271-11276
    • Hsia, K.C.1    Hoelz, A.2
  • 60
    • 77954310096 scopus 로고    scopus 로고
    • Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle coats
    • Lee C., Goldberg J. Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle coats. Cell 2010, 142:123-132.
    • (2010) Cell , vol.142 , pp. 123-132
    • Lee, C.1    Goldberg, J.2
  • 61
    • 67349283054 scopus 로고    scopus 로고
    • The evolving understanding of COPI vesicle formation
    • Hsu V.W., et al. The evolving understanding of COPI vesicle formation. Nat. Rev. Mol. Cell Biol. 2009, 10:360-364.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 360-364
    • Hsu, V.W.1
  • 62
    • 1642580789 scopus 로고    scopus 로고
    • Novel isotypic gamma/zeta subunits reveal three coatomer complexes in mammals
    • Wegmann D., et al. Novel isotypic gamma/zeta subunits reveal three coatomer complexes in mammals. Mol. Cell. Biol. 2004, 24:1070-1080.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1070-1080
    • Wegmann, D.1
  • 63
    • 34248394745 scopus 로고    scopus 로고
    • Differential localization of coatomer complex isoforms within the Golgi apparatus
    • Moelleken J., et al. Differential localization of coatomer complex isoforms within the Golgi apparatus. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:4425-4430.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 4425-4430
    • Moelleken, J.1
  • 64
    • 77954265667 scopus 로고    scopus 로고
    • Copy coats: COPI mimics clathrin and COPII
    • Hughson F.M. Copy coats: COPI mimics clathrin and COPII. Cell 2010, 142:19-21.
    • (2010) Cell , vol.142 , pp. 19-21
    • Hughson, F.M.1
  • 65
    • 70450193252 scopus 로고    scopus 로고
    • The secretory system of Arabidopsis
    • Bassham D.C., et al. The secretory system of Arabidopsis. Arabidopsis Book 2008, 6:e0116.
    • (2008) Arabidopsis Book , vol.6
    • Bassham, D.C.1
  • 66
    • 1542344041 scopus 로고    scopus 로고
    • The alpha- and beta'-COP WD40 domains mediate cargo-selective interactions with distinct di-lysine motifs
    • Eugster A., et al. The alpha- and beta'-COP WD40 domains mediate cargo-selective interactions with distinct di-lysine motifs. Mol. Biol. Cell 2004, 15:1011-1023.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1011-1023
    • Eugster, A.1
  • 67
    • 58149185093 scopus 로고    scopus 로고
    • Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes
    • Schoberer J., et al. Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes. Traffic 2009, 10:101-115.
    • (2009) Traffic , vol.10 , pp. 101-115
    • Schoberer, J.1
  • 68
    • 77952934647 scopus 로고    scopus 로고
    • Lipids and cholesterol as regulators of traffic in the endomembrane system
    • Lippincott-Schwartz J., Phair R.D. Lipids and cholesterol as regulators of traffic in the endomembrane system. Annu. Rev. Biophys. 2010, 39:559-578.
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 559-578
    • Lippincott-Schwartz, J.1    Phair, R.D.2
  • 69
    • 0036016439 scopus 로고    scopus 로고
    • The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain
    • Brandizzi F., et al. The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain. Plant Cell 2002, 14:1077-1092.
    • (2002) Plant Cell , vol.14 , pp. 1077-1092
    • Brandizzi, F.1
  • 70
    • 77954299061 scopus 로고    scopus 로고
    • A comprehensive comparison of transmembrane domains reveals organelle-specific properties
    • Sharpe H.J., et al. A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell 2010, 142:158-169.
    • (2010) Cell , vol.142 , pp. 158-169
    • Sharpe, H.J.1
  • 71
    • 0033944545 scopus 로고    scopus 로고
    • Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae
    • Levine T.P., et al. Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae. Mol. Biol. Cell 2000, 11:2267-2281.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2267-2281
    • Levine, T.P.1
  • 72
    • 42049097236 scopus 로고    scopus 로고
    • Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum
    • Ronchi P., et al. Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum. J. Cell Biol. 2008, 181:105-118.
    • (2008) J. Cell Biol. , vol.181 , pp. 105-118
    • Ronchi, P.1
  • 73
    • 0031027758 scopus 로고    scopus 로고
    • COPI-independent anterograde transport: Cargo-selective ER to Golgi protein transport in yeast COPI mutants
    • Gaynor E.C., Emr S.D. COPI-independent anterograde transport: Cargo-selective ER to Golgi protein transport in yeast COPI mutants. J. Cell Biol. 1997, 136:789-802.
    • (1997) J. Cell Biol. , vol.136 , pp. 789-802
    • Gaynor, E.C.1    Emr, S.D.2
  • 74
    • 17544372313 scopus 로고    scopus 로고
    • A single point mutation in epsilon-COP results in temperature-sensitive, lethal defects in membrane transport in a Chinese hamster ovary cell mutant
    • Guo Q., et al. A single point mutation in epsilon-COP results in temperature-sensitive, lethal defects in membrane transport in a Chinese hamster ovary cell mutant. J. Biol. Chem. 1996, 271:11191-11196.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11191-11196
    • Guo, Q.1
  • 75
    • 84879487599 scopus 로고    scopus 로고
    • Comprehensive protein-based artificial microRNA screens for effective gene silencing in plants
    • Li J.F., et al. Comprehensive protein-based artificial microRNA screens for effective gene silencing in plants. Plant Cell 2013, 25:1507-1522.
    • (2013) Plant Cell , vol.25 , pp. 1507-1522
    • Li, J.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.