COPII and secretory cargo capture into transport vesicles

Current Opinion in Cell Biology

Volumn 9, Issue 4, 1997, Pages 477-483

  Kuehn, Meta J ^a   Schekman, Randy ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; MEMBRANE PROTEIN; PROTEIN SUBUNIT;

COATED VESICLE; ENDOPLASMIC RETICULUM; GOLGI COMPLEX; MEMBRANE FUSION; MEMBRANE VESICLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECRETION; PROTEIN TARGETING; PROTEIN TRANSPORT; REVIEW; YEAST;

EID: 0030814254     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(97)80022-1     Document Type: Article

References (57)

1. Schekman R, Barlowe C, Bednarek S, Campbell J, Doering T, Duden R, Kuehn M, Rexach M, Yeung T, Orci L: Coat proteins and selective protein packaging into transport vesicles. Cold Spring Harb Symp Quant Biol 1995, 60:11-21.
2. Schekman R, Orci L: Coat proteins and vesicle budding. Science 1996, 271:1526-1533.
3. Bednarek SY, Ravazzola M, Hosobuchi M, Amherdt M, Perrelet A, Schekman R, Orci L: COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast Cell 1995, 83:1183-1196.
4. Hardwick KG, Pelham HRB: SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex. J Cell Biol 1992, 119:513-521.
5. Lupashin VV, Hamamoto S, Schekman RW: Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes. J Cell Biol 1996, 132:277-289.
6. Lewis MJ, Pelham HRB: SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum. Cell 1996, 85:205-215.
7. Cosson P, Letourneur F: Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 1994, 263:1629-1631.
8. Letourneur FE, Gaynor EC, Hennecke S, Demolliere C, Duden R, Emr SD, Riezman H, Cosson P: Coatomer is essential for retrieval of dilysine-tagged proteins to the ER. Cell 1994, 79:1199-1207.
9. Hosobuchi M, Kreis T, Schekman R: SEC21 is a gene required for ER to Golgi protein transport that encodes a subunit of a yeast coatomer. Nature 1992, 360:603-605.
10. Duden R, Hosobuchi M, Hamamoto S, Winey M, Byers B, Schekman R: Yeast beta- and beta′-coat proteins (COP): two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic. J Biol Chem 1994, 269:24486-24495.
11. Gaynor EC Emr SD: COPI-independent anterograde transport: cargo-selective ER to Golgi protein transport in yeast COPI mutants. J Cell Biol 1997, 136:789-802.
12. Pelham HRB: Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus. Cur Opin Cell Biol 1995, 7:530-535.
13. Schimmöller F, Singer-Krüger B, Schröder S, Krüger U, Barlowe C, Riezman H: The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBO J 1995, 14:1329-1339.
14. Stamnes JA, Craighead MW, Hoe MH, Lampen N, Germomanos S, Tempst P, Rothman JE: An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding. Proc Natl Acad Sci USA 1995, 92:8011-8015.
15. Fiedler K, Veit M, Stamnes MA, Rothman JE: Bimodal interaction of coatomer with the p24 family of putative cargo receptors. Science 1996, 273:1396-1399.
16. Barlowe C, Schekman R: SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER. Nature 1993, 365:347-349.
17. Yoshihisa T, Barlowe C, Schekman R: Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science 1993, 259:1466-1468.
18. Salama NR, Yeung T, Schekman RW: The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins. EMBO J 1993, 12:4073-4082.
19. Salama NR, Chuang JS, Schekman RW: SEC31 encodes an essential component of the COPII coat required for transport vesicle budding from the endoplasmic reticulum. Mol Biol Cell 1997, 8:205-217.
20. Barlowe C, Orci L, Yeung T, Hosobuchi M, Hamamoto S, Salama N, Rexach MF, Ravazzola M, Amherdt M, Schekman R: COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 1994, 77:895-907.
21. Aridor M, Bannykh SI, Rowe T, Balch WE: Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport J Cell Biol 1995, 131:875-893.
22. Rowe T, Aridor M, McCaffery JM, Plutner H, Nuoffer C, Balch WE: COPII vesicles derived from mammalian endoplasmic reticulum microsomes recruit COPI. J Cell Biol 1996, 135:895-911.
23. Espenshade P, Gimeno RE, Holzmacher E, Teung P, Kaiser CA: Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p. J Cell Biol 1995, 131:311-324.
24. Gimeno RE, Espenshade P, Kaiser CA: COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p. Mol Biol Cell 1996, 7:1815-1823.
25. Campbell JL, Schekman R: Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles. Proc Natl Acad Sci USA 1997, 94:837-842.
26. Nakano A, Muramatsu M: A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus. J Cell Biol 1989, 109:2677-2691.
27. Orci L, Palmer DJ, Amherdt M, Rothman JE: Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. Nature 1993, 364:732-734.
28. Kuge O, Dascher C, Orci L, Rowe T, Amherdt M, Plutner H, Ravazzola M, Tanigawa G, Rothman JE, Balch WE: Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments. J Cell Biol 1994, 125:51-65.
29. D'Enfert C, Gensse M, Gaillardin C: Fission yeast and a plant have functional homologues of the Sar1 and Sec12 proteins involved in ER to Golgi traffic in budding yeast EMBO J 1992, 11:4205-41211.
30. Orci L, Ravazzola M, Meda P, Holcomb C, Moore H-P, Hicke L, Schekman R: Mammalian Sec23p homologue is restricted to the endoplasmic reticulum transitional cytoplasm. Proc Natl Acad Sci USA 1991, 88:8611-8615.
31. Paccaud J-P, Reith W, Carpentier JL, Ravazzola M, Amherdt M, Schekman R, Orci L: Cloning and functional characterization of mammalian homologues of the COPII component Sec23. Mol Biol Cell 1996, 7:1535-1546.
32. Shaywitz DA, Orci L, Ravazzola M, Swaroop A, Kaiser CA: Human SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulum. J Cell Biol 1995, 128:769-777.
33. Tang BL, Peter F, Krijnse-Locker J, Low SH, Griffiths G, Hong W: The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus. Mol Cell Biol 1997, 17:256-266.
34. Siniossoglou S, Wimmer C, Rieger M, Doye V, Tekotte H, Weise C, Emig S, Segref A, Hurt EC: A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 1996, 84:265-275.
35. Hay JC, Hirling H, Scheller RH: Mammalian vesicle trafficking proteins of the endoplasmic reticulum and Golgi apparatus. J Biol Chem 1996, 271:5671-5679.
36. Munro S, Pelham HR: An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 1986, 46:291-300.
37. Hammond C, Helenius A: Quality control in the secretory pathway. Curr Opin Cell Biol 1995, 7:523-529.
38. Smith T, Ferreira LR, Hebert C, Norris K, Sauk JJ: Hsp47 and cyclophilin P traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. J Biol Chem 1995, 270:18323-18328.
39. Sato M, Sato K, Nakano A: Endoplasmic reticulum localization of Sec12p is achieved by two mechanisms: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain. J Cell Biol 1996, 134:279-293. A comprehensive study of chimeric proteins that dissects the localization domains of Sec12p. These data and the thorough discussion argue that Sec12p employs two signals to maintain ER localization.
40. Doering TL, Schekman R: GPI anchor attachment is required for Gas1p transport from the endoplasmic reticulum in COPII vesicles. EMBO J 1996, 15:182-191.
41. Kuehn MJ, Schekman R, Ljungdahl PO: Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro. J Cell Biol 1996, 135:585-595. Provides in vitro evidence for a specific secretion defect observed in vivo. The data show membrane proteins packaged into COPII-coated vesicles and that ER membranes lacking Shr3p are defective for permease packaging. Further work is necessary to determine whether such ER chaperones act distantly from the budding event, directly bind COPII components, or localize cargo to a site of vesicle budding.
42. +-ATPase subunits onto the vacuolar membrane in Saccharomyces cerevisiae. J Biol Chem 1993, 268:961-967.
43. +-ATPase complex. Mol Biol Cell 1994, 5:1039-1050.
44. +-ATPase complex. J Biol Chem 1995, 270:22329-22336.
45. Mizuno M, Singer SJ: A soluble secretory protein is first concentrated in the endoplasmic reticulum before transfer to the Golgi apparatus. Proc Natl Acad Sci USA 1993, 90:5732-5736.
46. Balch WE, McCaffery JM, Plutner H, Farquhar MG Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum. Cell 1994, 76:841-852.
47. Yeung T, Barlowe C, Schekman R: Uncoupled packaging of targeting and cargo molecules during transport vesicle budding from the endoplasmic reticulum. J Biol Chem 1995, 270:30567-30570,
48. Belden WJ, Barlowe C: Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport. J Biol Chem 1996, 271:26939-26946. This is the first account of genetic and biochemical interactions between p24 family members. These data argue that Emp24p and Erv25p are homologous but not functionally redundant. Putative membrane proteins of lower molecular weight that are also abundant members of COPII vesicles have not yet been examined.
49. Bannykh SI, Rowe T, Balch WE: The organization of endoplasmic reticulum export complexes. J Cell Biol 1996, 135:19-35.
50. Blurn R, Feick P, Puype M, Vandekerckhove J, Klengel R, Nastainczyk W, Schulz I: Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal membranes, are members of a protein family involved in vesiclular trafficking. J Biol Chem 1996, 271:17183-17189.
51. Sohn K, Orci L, Ravazzola M, Amherdt M, Bremser M, Lottspeich F, Fiedler K, Helms JB, Wieland FT: A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding. J Cell Biol 1996, 135:1239-1248.
52. Elrod-Erickson MJ, Kaiser CA: Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations. Mol Biol Cell 1996, 7:1043-1058. A revealing study showing mutational suppression of a sec13 defect that allows cell viability without a functional member of the COPII coat. ER-Golgi transport occurs in these double mutants, albeit at a reduced rate. One of the three suppressors identified (bst2) encodes Emp24p. BST proteins may play a role in selective cargo packaging.
53. Itin C, Schindler R, Hauri H-P: Targeting of protein ERGIC-53 to the ER/ERGIC/cis-Golgi recycling pathway. J Cell Biol 1995, 131:57-67.
54. Lahtinen U, Hellman U, Wemstedt C, Saraste J, Pettersson RF: Molecular cloning and expression of a 58-kDa cis-Golgi and intermediate compartment protein. J Biol Chem 1996, 271:4031-4037.
55. Fiedler K, Simons K: The role of N-glycans in the secretory pathway. Cell 1995, 81:309-312.
56. Shröder S, Schimmöller F, Singer-Krüger B, Riezman H: The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the ret1-1 mutation In α-COP. J Cell Biol 1995, 131:895-912.
57. Arar C, Carpentier V, Le Caer J-P, Monsigny M, Legrand A, Roche A-C: ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells. J Biol Chem 1995, 270:3551-3553.