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PDBsum entry 1m2v
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protein metals Protein-protein interface(s) links
Protein transport PDB id
1m2v

 

 

 

 

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Contents
Protein chains
705 a.a. *
748 a.a. *
Metals
_ZN ×2
Waters ×69
* Residue conservation analysis
PDB id:
1m2v
Name: Protein transport
Title: Crystal structure of the yeast sec23/24 heterodimer
Structure: Protein transport protein sec23. Chain: a. Synonym: sec23. Sec23p. Cytoplasmic gtpase-activating protein. Sec23 copii-coat protein. Engineered: yes. Protein transport protein sec24. Chain: b. Synonym: sec24. Sec24p. Sec24 protein. Abnormal nuclear morphology 1 sec24 copii-coat protein.
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: sec23. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: sar1. Expression_system_taxid: 562
Resolution:
2.75Å     R-factor:   0.210     R-free:   0.257
Authors: X.Bi,R.A.Corpina,J.Goldberg
Key ref:
X.Bi et al. (2002). Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature, 419, 271-277. PubMed id: 12239560 DOI: 10.1038/nature01040
Date:
25-Jun-02     Release date:   20-Sep-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P15303  (SEC23_YEAST) -  Protein transport protein SEC23 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		 
Seq:
Struc: 		768 a.a.
705 a.a.
Protein chain
Pfam   ArchSchema ?
P40482  (SEC24_YEAST) -  Protein transport protein SEC24 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc: 		 
Seq:
Struc: 		926 a.a.
748 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 12 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1038/nature01040 Nature 419:271-277 (2002)
PubMed id: 12239560  
 
 
Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat.
X.Bi, R.A.Corpina, J.Goldberg.
 
  ABSTRACT  
 
COPII-coated vesicles form on the endoplasmic reticulum by the stepwise recruitment of three cytosolic components: Sar1-GTP to initiate coat formation, Sec23/24 heterodimer to select SNARE and cargo molecules, and Sec13/31 to induce coat polymerization and membrane deformation. Crystallographic analysis of the Saccharomyces cerevisiae Sec23/24-Sar1 complex reveals a bow-tie-shaped structure, 15 nm long, with a membrane-proximal surface that is concave and positively charged to conform to the size and acidic-phospholipid composition of the COPII vesicle. Sec23 and Sar1 form a continuous surface stabilized by a non-hydrolysable GTP analogue, and Sar1 has rearranged from the GDP conformation to expose amino-terminal residues that will probably embed in the bilayer. The GTPase-activating protein (GAP) activity of Sec23 involves an arginine side chain inserted into the Sar1 active site. These observations establish the structural basis for GTP-dependent recruitment of a vesicular coat complex, and for uncoating through coat-controlled GTP hydrolysis.
 
  Selected figure(s)  
 
Figure 1.
Figure 1: Structure of the Sec23/24 -Sar1 pre-budding complex. Ribbon representation is shown as successive 90° rotations. Sec23 is yellow, Sec24 green and Sar1 red. a, Front view along the dyad relating the coat subunits, with the membrane-proximal surface facing forward. b, Side view. The grey line indicates the curvature of a 60-nm COPII vesicle, drawn to scale. c, Top view. The three regions of Sar1 that would face the membrane are labelled C, N and 2 - 3. 		Figure 3.
Figure 3: Surface features of the Sec23/24 complex a, Molecular surface coloured according to electrostatic potential50: negative potential is red and positive potential blue. Sar1 is drawn as a backbone tube in magenta. The three views are successive 90° rotations around a vertical axis. In the left image, the membrane-proximal surface faces forwards. b, Surface of Sec23/24 coloured according to sequence conservation of the underlying residues in an alignment of Sec23 sequences from six organisms (human Sec23A, Drosophila melanogaster, Neurospora crassa, Schizosaccharomyces pombe, Arabidopsis thaliana and Saccharomyces cerevisiae) and Sec24 sequences from four organisms (human Sec24A, S. pombe, A. thaliana and S. cerevisiae). Labels I, II and III indicate three highly conserved patches (see text for details). The orientations are the same as in a, with Sar1 omitted.
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (2002, 419, 271-277) copyright 2002.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
22193160 G.Zanetti, K.B.Pahuja, S.Studer, S.Shim, and R.Schekman (2012).
COPII and the regulation of protein sorting in mammals.
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20643221 C.G.Angers, and A.J.Merz (2011).
New links between vesicle coats and Rab-mediated vesicle targeting.
  Semin Cell Dev Biol, 22, 18-26.  
21291503 C.Kodera, T.Yorimitsu, A.Nakano, and K.Sato (2011).
Sed4p stimulates Sar1p GTP hydrolysis and promotes limited coat disassembly.
  Traffic, 12, 591-599.  
21532587 C.Lord, D.Bhandari, S.Menon, M.Ghassemian, D.Nycz, J.Hay, P.Ghosh, and S.Ferro-Novick (2011).
Sequential interactions with Sec23 control the direction of vesicle traffic.
  Nature, 473, 181-186.  
21040296 F.Brandizzi (2011).
Is there a COPII-mediated membrane traffic in chloroplasts?
  Traffic, 12, 9.  
21129209 A.F.Neuwald (2010).
Bayesian classification of residues associated with protein functional divergence: Arf and Arf-like GTPases.
  Biol Direct, 5, 66.  
20015893 A.Iolascon, R.Russo, M.R.Esposito, R.Asci, C.Piscopo, S.Perrotta, M.Fénéant-Thibault, L.Garçon, and J.Delaunay (2010).
Molecular analysis of 42 patients with congenital dyserythropoietic anemia type II: new mutations in the SEC23B gene and a search for a genotype-phenotype relationship.
  Haematologica, 95, 708-715.  
21145455 J.H.Hurley, E.Boura, L.A.Carlson, and B.Różycki (2010).
Membrane budding.
  Cell, 143, 875-887.  
19966784 J.Merte, D.Jensen, K.Wright, S.Sarsfield, Y.Wang, R.Schekman, and D.D.Ginty (2010).
Sec24b selectively sorts Vangl2 to regulate planar cell polarity during neural tube closure.
  Nat Cell Biol, 12, 41.  
21054154 K.E.Routledge, V.Gupta, and W.E.Balch (2010).
Emergent properties of proteostasis-COPII coupled systems in human health and disease.
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20624903 K.R.Long, Y.Yamamoto, A.L.Baker, S.C.Watkins, C.B.Coyne, J.F.Conway, and M.Aridor (2010).
Sar1 assembly regulates membrane constriction and ER export.
  J Cell Biol, 190, 115-128.  
21142873 K.Schmidt, and D.J.Stephens (2010).
Cargo loading at the ER.
  Mol Membr Biol, 27, 398-411.  
21054155 M.Anitei, T.Wassmer, C.Stange, and B.Hoflack (2010).
Bidirectional transport between the trans-Golgi network and the endosomal system.
  Mol Membr Biol, 27, 443-456.  
20520821 M.Norum, E.Tång, T.Chavoshi, H.Schwarz, D.Linke, A.Uv, and B.Moussian (2010).
Trafficking through COPII stabilises cell polarity and drives secretion during Drosophila epidermal differentiation.
  PLoS One, 5, e10802.  
20477990 R.Buchanan, A.Kaufman, L.Kung-Tran, and E.A.Miller (2010).
Genetic analysis of yeast Sec24p mutants suggests cargo binding is not co-operative during ER export.
  Traffic, 11, 1034-1043.  
20442775 S.Sarmah, A.Barrallo-Gimeno, D.B.Melville, J.Topczewski, L.Solnica-Krezel, and E.W.Knapik (2010).
Sec24D-dependent transport of extracellular matrix proteins is required for zebrafish skeletal morphogenesis.
  PLoS One, 5, e10367.  
20214751 X.Jian, M.Cavenagh, J.M.Gruschus, P.A.Randazzo, and R.A.Kahn (2010).
Modifications to the C-terminus of Arf1 alter cell functions and protein interactions.
  Traffic, 11, 732-742.  
19906579 A.V.Shnyrova, V.A.Frolov, and J.Zimmerberg (2009).
Domain-driven morphogenesis of cellular membranes.
  Curr Biol, 19, R772-R780.  
19183188 B.Zhang (2009).
Recent developments in the understanding of the combined deficiency of FV and FVIII.
  Br J Haematol, 145, 15-23.  
19338667 C.D.Lee, and T.F.Wang (2009).
The N-terminal domain of Escherichia coli RecA have multiple functions in promoting homologous recombination.
  J Biomed Sci, 16, 37.  
19325869 E.Petsalaki, A.Stark, E.García-Urdiales, and R.B.Russell (2009).
Accurate prediction of peptide binding sites on protein surfaces.
  PLoS Comput Biol, 5, e1000335.  
19759175 E.S.Sevova, and J.D.Bangs (2009).
Streamlined architecture and glycosylphosphatidylinositol-dependent trafficking in the early secretory pathway of African trypanosomes.
  Mol Biol Cell, 20, 4739-4750.  
19561605 K.Schwarz, A.Iolascon, F.Verissimo, N.S.Trede, W.Horsley, W.Chen, B.H.Paw, K.P.Hopfner, K.Holzmann, R.Russo, M.R.Esposito, D.Spano, L.De Falco, K.Heinrich, B.Joggerst, M.T.Rojewski, S.Perrotta, J.Denecke, U.Pannicke, J.Delaunay, R.Pepperkok, and H.Heimpel (2009).
Mutations affecting the secretory COPII coat component SEC23B cause congenital dyserythropoietic anemia type II.
  Nat Genet, 41, 936-940.  
19763084 K.V.Tabata, K.Sato, T.Ide, T.Nishizaka, A.Nakano, and H.Noji (2009).
Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane.
  EMBO J, 28, 3279-3289.  
19621418 P.Bianchi, E.Fermo, C.Vercellati, C.Boschetti, W.Barcellini, A.Iurlo, A.P.Marcello, P.G.Righetti, and A.Zanella (2009).
Congenital dyserythropoietic anemia type II (CDAII) is caused by mutations in the SEC23B gene.
  Hum Mutat, 30, 1292-1298.  
19481110 T.Itoh, and T.Takenawa (2009).
Mechanisms of membrane deformation by lipid-binding domains.
  Prog Lipid Res, 48, 298-305.  
19729648 T.J.Pucadyil, and S.L.Schmid (2009).
Conserved functions of membrane active GTPases in coated vesicle formation.
  Science, 325, 1217-1220.  
19357197 T.K.Taneja, J.Mankouri, R.Karnik, S.Kannan, A.J.Smith, T.Munsey, H.B.Christesen, D.J.Beech, and A.Sivaprasadarao (2009).
Sar1-GTPase-dependent ER exit of KATP channels revealed by a mutation causing congenital hyperinsulinism.
  Hum Mol Genet, 18, 2400-2413.  
19368893 T.Zhang, S.Li, Y.Zhang, C.Zhong, Z.Lai, and J.Ding (2009).
Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition and binding mode of small GTPase with effector.
  Structure, 17, 602-610.
PDB codes: 3doe 3dof
19575675 Y.Shibata, J.Hu, M.M.Kozlov, and T.A.Rapoport (2009).
Mechanisms shaping the membranes of cellular organelles.
  Annu Rev Cell Dev Biol, 25, 329-354.  
18309292 A.Scrima, C.Thomas, D.Deaconescu, and A.Wittinghofer (2008).
The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues.
  EMBO J, 27, 1145-1153.
PDB code: 3brw
18620527 A.V.Bryksin, and P.P.Laktionov (2008).
Role of glyceraldehyde-3-phosphate dehydrogenase in vesicular transport from golgi apparatus to endoplasmic reticulum.
  Biochemistry (Mosc), 73, 619-625.  
19015319 C.Weimer, R.Beck, P.Eckert, I.Reckmann, J.Moelleken, B.Brügger, and F.Wieland (2008).
Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI trafficking.
  J Cell Biol, 183, 725-735.  
18692460 F.M.Hughson (2008).
Both layers of the COPII coat come into view.
  Cell, 134, 384-385.  
18650939 H.Farhan, M.Weiss, K.Tani, R.J.Kaufman, and H.P.Hauri (2008).
Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load.
  EMBO J, 27, 2043-2054.  
17973654 H.Higashio, K.Sato, and A.Nakano (2008).
Smy2p Participates in COPII Vesicle Formation Through the Interaction with Sec23p/Sec24p Subcomplex.
  Traffic, 9, 79-93.  
18060556 H.Hughes, and D.J.Stephens (2008).
Assembly, organization, and function of the COPII coat.
  Histochem Cell Biol, 129, 129-151.  
18843296 J.D.Mancias, and J.Goldberg (2008).
Structural basis of cargo membrane protein discrimination by the human COPII coat machinery.
  EMBO J, 27, 2918-2928.
PDB codes: 3efo 3eg9 3egd 3egx 3eh1 3eh2
18410493 M.C.Lee, P.A.Moura, E.A.Miller, and D.A.Fidock (2008).
Plasmodium falciparum Sec24 marks transitional ER that exports a model cargo via a diacidic motif.
  Mol Microbiol, 68, 1535-1546.  
18469070 P.D.Blood, R.D.Swenson, and G.A.Voth (2008).
Factors influencing local membrane curvature induction by N-BAR domains as revealed by molecular dynamics simulations.
  Biophys J, 95, 1866-1876.  
18322804 S.L.Hanton, L.Chatre, L.A.Matheson, M.Rossi, M.A.Held, and F.Brandizzi (2008).
Plant Sar1 isoforms with near-identical protein sequences exhibit different localisations and effects on secretion.
  Plant Mol Biol, 67, 283-294.  
18692470 S.M.Stagg, P.LaPointe, A.Razvi, C.Gürkan, C.S.Potter, B.Carragher, and W.E.Balch (2008).
Structural basis for cargo regulation of COPII coat assembly.
  Cell, 134, 474-484.  
18376416 S.Veltel, R.Gasper, E.Eisenacher, and A.Wittinghofer (2008).
The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3.
  Nat Struct Mol Biol, 15, 373-380.
PDB codes: 3bh6 3bh7
18331383 W.J.Brown, H.Plutner, D.Drecktrah, B.L.Judson, and W.E.Balch (2008).
The lysophospholipid acyltransferase antagonist CI-976 inhibits a late step in COPII vesicle budding.
  Traffic, 9, 786-797.  
17506703 A.K.Gillingham, and S.Munro (2007).
The small G proteins of the Arf family and their regulators.
  Annu Rev Cell Dev Biol, 23, 579-611.  
17981132 J.C.Fromme, M.Ravazzola, S.Hamamoto, M.Al-Balwi, W.Eyaid, S.A.Boyadjiev, P.Cosson, R.Schekman, and L.Orci (2007).
The genetic basis of a craniofacial disease provides insight into COPII coat assembly.
  Dev Cell, 13, 623-634.  
17499046 J.D.Mancias, and J.Goldberg (2007).
The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope.
  Mol Cell, 26, 403-414.
PDB codes: 2nup 2nut
17540168 J.L.Bos, H.Rehmann, and A.Wittinghofer (2007).
GEFs and GAPs: critical elements in the control of small G proteins.
  Cell, 129, 865-877.  
17428919 L.P.Sun, J.Seemann, J.L.Goldstein, and M.S.Brown (2007).
Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: Insig renders sorting signal in Scap inaccessible to COPII proteins.
  Proc Natl Acad Sci U S A, 104, 6519-6526.  
17686639 M.C.Lee, and E.A.Miller (2007).
Molecular mechanisms of COPII vesicle formation.
  Semin Cell Dev Biol, 18, 424-434.  
17547699 M.Zuzarte, S.Rinné, G.Schlichthörl, A.Schubert, J.Daut, and R.Preisig-Müller (2007).
A di-acidic sequence motif enhances the surface expression of the potassium channel TASK-3.
  Traffic, 8, 1093-1100.  
17604721 S.Fath, J.D.Mancias, X.Bi, and J.Goldberg (2007).
Structure and organization of coat proteins in the COPII cage.
  Cell, 129, 1325-1336.
PDB codes: 2pm6 2pm7 2pm9
17604713 T.Kirchhausen (2007).
Making COPII coats.
  Cell, 129, 1251-1252.  
16782321 B.Antonny (2006).
Membrane deformation by protein coats.
  Curr Opin Cell Biol, 18, 386-394.  
16990852 C.Gürkan, S.M.Stagg, P.Lapointe, and W.E.Balch (2006).
The COPII cage: unifying principles of vesicle coat assembly.
  Nat Rev Mol Cell Biol, 7, 727-738.  
16410510 C.Smith (2006).
Structural biology. Two geometric solutions to a transporting problem.
  Science, 311, 182-183.  
16553898 G.Stefano, L.Renna, L.Chatre, S.L.Hanton, P.Moreau, C.Hawes, and F.Brandizzi (2006).
In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulum and of ER export sites depends on active COPI machinery.
  Plant J, 46, 95.  
17041781 J.Béthune, F.Wieland, and J.Moelleken (2006).
COPI-mediated transport.
  J Membr Biol, 211, 65-79.  
16365634 J.Zimmerberg, and M.M.Kozlov (2006).
How proteins produce cellular membrane curvature.
  Nat Rev Mol Cell Biol, 7, 9.  
16980978 M.R.Lang, L.A.Lapierre, M.Frotscher, J.R.Goldenring, and E.W.Knapik (2006).
Secretory COPII coat component Sec23a is essential for craniofacial chondrocyte maturation.
  Nat Genet, 38, 1198-1203.  
16439358 O.Schlenker, A.Hendricks, I.Sinning, and K.Wild (2006).
The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains.
  J Biol Chem, 281, 8898-8906.
PDB code: 2fh5
17008407 P.D.Blood, and G.A.Voth (2006).
Direct observation of Bin/amphiphysin/Rvs (BAR) domain-induced membrane curvature by means of molecular dynamics simulations.
  Proc Natl Acad Sci U S A, 103, 15068-15072.  
16505163 R.A.Kahn, J.Cherfils, M.Elias, R.C.Lovering, S.Munro, and A.Schurmann (2006).
Nomenclature for the human Arf family of GTP-binding proteins: ARF, ARL, and SAR proteins.
  J Cell Biol, 172, 645-650.  
16980979 S.A.Boyadjiev, J.C.Fromme, J.Ben, S.S.Chong, C.Nauta, D.J.Hur, G.Zhang, S.Hamamoto, R.Schekman, M.Ravazzola, L.Orci, and W.Eyaid (2006).
Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking.
  Nat Genet, 38, 1192-1197.  
17098186 T.A.Springer (2006).
Complement and the multifaceted functions of VWA and integrin I domains.
  Structure, 14, 1611-1616.  
16344311 A.Bielli, C.J.Haney, G.Gabreski, S.C.Watkins, S.I.Bannykh, and M.Aridor (2005).
Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission.
  J Cell Biol, 171, 919-924.  
16251943 G.Drin, and B.Antonny (2005).
Cell biology: helices sculpt membrane.
  Nature, 437, 1247-1249.  
16319878 H.T.McMahon, and J.L.Gallop (2005).
Membrane curvature and mechanisms of dynamic cell membrane remodelling.
  Nature, 438, 590-596.  
15719017 I.Leiros, J.Timmins, D.R.Hall, and S.McSweeney (2005).
Crystal structure and DNA-binding analysis of RecO from Deinococcus radiodurans.
  EMBO J, 24, 906-918.
PDB code: 1w3s
15520000 J.C.Amor, J.Swails, X.Zhu, C.R.Roy, H.Nagai, A.Ingmundson, X.Cheng, and R.A.Kahn (2005).
The structure of RalF, an ADP-ribosylation factor guanine nucleotide exchange factor from Legionella pneumophila, reveals the presence of a cap over the active site.
  J Biol Chem, 280, 1392-1400.
PDB codes: 1xsz 1xt0
15752134 J.D.Mancias, and J.Goldberg (2005).
Exiting the endoplasmic reticulum.
  Traffic, 6, 278-285.  
15665868 K.Sato, and A.Nakano (2005).
Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis.
  Nat Struct Mol Biol, 12, 167-174.  
16122427 M.C.Lee, L.Orci, S.Hamamoto, E.Futai, M.Ravazzola, and R.Schekman (2005).
Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle.
  Cell, 122, 605-617.  
15891388 M.M.Hussain, S.Fatma, X.Pan, and J.Iqbal (2005).
Intestinal lipoprotein assembly.
  Curr Opin Lipidol, 16, 281-285.  
15634214 S.Grimmer, M.Ying, S.Wälchli, B.van Deurs, and K.Sandvig (2005).
Golgi vesiculation induced by cholesterol occurs by a dynamin- and cPLA2-dependent mechanism.
  Traffic, 6, 144-156.  
15632943 W.Antonin, and I.W.Mattaj (2005).
Nuclear pore complexes: round the bend?
  Nat Cell Biol, 7, 10-12.  
14645856 B.J.Peter, H.M.Kent, I.G.Mills, Y.Vallis, P.J.Butler, P.R.Evans, and H.T.McMahon (2004).
BAR domains as sensors of membrane curvature: the amphiphysin BAR structure.
  Science, 303, 495-499.
PDB code: 1uru
15017362 C.C.Shoulders, D.J.Stephens, and B.Jones (2004).
The intracellular transport of chylomicrons requires the small GTPase, Sar1b.
  Curr Opin Lipidol, 15, 191-197.  
15261670 H.T.McMahon, and I.G.Mills (2004).
COP and clathrin-coated vesicle budding: different pathways, common approaches.
  Curr Opin Cell Biol, 16, 379-391.  
15117975 J.C.Kagan, M.P.Stein, M.Pypaert, and C.R.Roy (2004).
Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle.
  J Exp Med, 199, 1201-1211.  
15093828 L.C.Bickford, E.Mossessova, and J.Goldberg (2004).
A structural view of the COPII vesicle coat.
  Curr Opin Struct Biol, 14, 147-153.  
15473836 M.C.Lee, E.A.Miller, J.Goldberg, L.Orci, and R.Schekman (2004).
Bi-directional protein transport between the ER and Golgi.
  Annu Rev Cell Dev Biol, 20, 87.  
14739445 M.C.Lee, and R.Schekman (2004).
Cell biology. BAR domains go on a bender.
  Science, 303, 479-480.  
  15103397 M.Ohi, Y.Li, Y.Cheng, and T.Walz (2004).
Negative Staining and Image Classification - Powerful Tools in Modern Electron Microscopy.
  Biol Proced Online, 6, 23-34.  
15479737 X.Wang, J.Matteson, Y.An, B.Moyer, J.S.Yoo, S.Bannykh, I.A.Wilson, J.R.Riordan, and W.E.Balch (2004).
COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code.
  J Cell Biol, 167, 65-74.  
12671686 B.Antonny, P.Gounon, R.Schekman, and L.Orci (2003).
Self-assembly of minimal COPII cages.
  EMBO Rep, 4, 419-424.  
12692552 B.Jones, E.L.Jones, S.A.Bonney, H.N.Patel, A.R.Mensenkamp, S.Eichenbaum-Voline, M.Rudling, U.Myrdal, G.Annesi, S.Naik, N.Meadows, A.Quattrone, S.A.Islam, R.P.Naoumova, B.Angelin, R.Infante, E.Levy, C.C.Roy, P.S.Freemont, J.Scott, and C.C.Shoulders (2003).
Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders.
  Nat Genet, 34, 29-31.  
14580338 B.Panic, O.Perisic, D.B.Veprintsev, R.L.Williams, and S.Munro (2003).
Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus.
  Mol Cell, 12, 863-874.
PDB code: 1upt
12941266 C.Barlowe (2003).
Molecular recognition of cargo by the COPII complex: a most accommodating coat.
  Cell, 114, 395-397.  
12972562 C.G.Giraudo, and H.J.Maccioni (2003).
Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1.
  Mol Biol Cell, 14, 3753-3766.  
12941277 E.A.Miller, T.H.Beilharz, P.N.Malkus, M.C.Lee, S.Hamamoto, L.Orci, and R.Schekman (2003).
Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles.
  Cell, 114, 497-509.  
12941276 E.Mossessova, L.C.Bickford, and J.Goldberg (2003).
SNARE selectivity of the COPII coat.
  Cell, 114, 483-495.
PDB codes: 1pcx 1pd0 1pd1
12728274 J.S.Bonifacino, and J.Lippincott-Schwartz (2003).
Coat proteins: shaping membrane transport.
  Nat Rev Mol Cell Biol, 4, 409-414.  
12892776 K.Farsad, and P.De Camilli (2003).
Mechanisms of membrane deformation.
  Curr Opin Cell Biol, 15, 372-381.  
12912905 P.Pathre, K.Shome, A.Blumental-Perry, A.Bielli, C.J.Haney, S.Alber, S.C.Watkins, G.Romero, and M.Aridor (2003).
Activation of phospholipase D by the small GTPase Sar1p is required to support COPII assembly and ER export.
  EMBO J, 22, 4059-4069.  
12654246 T.Schwartz, and G.Blobel (2003).
Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor.
  Cell, 112, 793-803.
PDB code: 1nrj
12559754 V.Haucke (2003).
Vesicle budding: a coat for the COPs.
  Trends Cell Biol, 13, 59-60.  
12499351 P.Malkus, F.Jiang, and R.Schekman (2002).
Concentrative sorting of secretory cargo proteins into COPII-coated vesicles.
  J Cell Biol, 159, 915-921.  
12426381 S.Otte, and C.Barlowe (2002).
The Erv41p-Erv46p complex: multiple export signals are required in trans for COPII-dependent transport from the ER.
  EMBO J, 21, 6095-6104.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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