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PMID: 10704443 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles.

The Journal of cell biology ·Vol. 148 ·No. 5 ·2000-03-06 ·Pages 925-30

Muñiz M, Nuoffer C, Hauri HP, Riezman H

Abstract

Members of the yeast p24 family, including Emp24p and Erv25p, form a heteromeric complex required for the efficient transport of selected proteins from the endoplasmic reticulum (ER) to the Golgi apparatus. The specific functions and sites of action of this complex are unknown. We show that Emp24p is directly required for efficient packaging of a lumenal cargo protein, Gas1p, into ER-derived vesicles. Emp24p and Erv25p can be directly cross-linked to Gas1p in ER-derived vesicles. Gap1p, which was not affected by emp24 mutation, was not cross-linked. These results suggest that the Emp24 complex acts as a cargo receptor in vesicle biogenesis from the ER.

MeSH Terms
Antibodies/pharmacology Biological Transport/drug effects,physiology Carrier Proteins/genetics,immunology,metabolism Cross-Linking Reagents/pharmacology Endoplasmic Reticulum/metabolism Endosomes/metabolism Ethylmaleimide/pharmacology Fungal Proteins/metabolism Golgi Apparatus/metabolism HSP70 Heat-Shock Proteins/metabolism Intracellular Membranes/metabolism Macromolecular Substances Membrane Glycoproteins/metabolism Membrane Proteins/genetics,immunology,metabolism Precipitin Tests Protein Processing, Post-Translational/physiology Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Sulfhydryl Reagents/pharmacology Vesicular Transport Proteins
Chemicals
Antibodies Carrier Proteins Cross-Linking Reagents EMP24 protein, S cerevisiae ERV25 protein, S cerevisiae Fungal Proteins GAS1 protein, S cerevisiae HSP70 Heat-Shock Proteins KAR2 protein, yeast Macromolecular Substances Membrane Glycoproteins Membrane Proteins Saccharomyces cerevisiae Proteins Sulfhydryl Reagents Vesicular Transport Proteins Ethylmaleimide
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Muñiz M
Biozentrum of the University of Basel, CH-4056 Basel, Switzerland.
Nuoffer C
Hauri H P
Riezman H
References (29)
29 references, click to expand
  1. The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.
    Nat Cell Biol. 1999 Oct;1(6):330-4 PMID: 10559958
  2. p24 proteins and quality control of LIN-12 and GLP-1 trafficking in Caenorhabditis elegans.
    J Cell Biol. 1999 Jun 14;145(6):1165-75 PMID: 10366590
  3. The rate of bulk flow from the endoplasmic reticulum to the cell surface.
    Cell. 1987 Jul 17;50(2):289-300 PMID: 3594573
  4. Determinants for glycophospholipid anchoring of the Saccharomyces cerevisiae GAS1 protein to the plasma membrane.
    Mol Cell Biol. 1991 Jan;11(1):27-37 PMID: 1824714
  5. Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors.
    Annu Rev Biochem. 1992;61:307-30 PMID: 1323236
  6. Analysis of the sequence requirements for glycosylphosphatidylinositol anchoring of Saccharomyces cerevisiae Gas1 protein.
    J Biol Chem. 1993 May 15;268(14):10558-63 PMID: 8486709
  7. The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene.
    Cell. 1994 May 20;77(4):579-86 PMID: 8187177
  8. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum.
    Cell. 1994 Jun 17;77(6):895-907 PMID: 8004676
  9. Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles.
    Cell. 1999 Jul 9;98(1):81-90 PMID: 10412983
  10. Roles for alpha(2)p24 and COPI in endoplasmic reticulum cargo exit site formation.
    J Cell Biol. 1999 Jul 26;146(2):285-99 PMID: 10427085
  11. Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus.
    J Cell Biol. 1994 Jul;126(1):41-52 PMID: 8027184
  12. 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 Apr 3;14(7):1329-39 PMID: 7729411
  13. An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding.
    Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):8011-5 PMID: 7644530
  14. GPI anchor attachment is required for Gas1p transport from the endoplasmic reticulum in COP II vesicles.
    EMBO J. 1996 Jan 2;15(1):182-91 PMID: 8598201
  15. Coat proteins and vesicle budding.
    Science. 1996 Mar 15;271(5255):1526-33 PMID: 8599108
  16. Protein sorting by transport vesicles.
    Science. 1996 Apr 12;272(5259):227-34 PMID: 8602507
  17. Bimodal interaction of coatomer with the p24 family of putative cargo receptors.
    Science. 1996 Sep 6;273(5280):1396-9 PMID: 8703076
  18. Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations.
    Mol Biol Cell. 1996 Jul;7(7):1043-58 PMID: 8862519
  19. 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 Oct 25;271(43):26939-46 PMID: 8900179
  20. Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro.
    J Cell Biol. 1996 Nov;135(3):585-95 PMID: 8909535
  21. A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding.
    J Cell Biol. 1996 Dec;135(5):1239-48 PMID: 8947548
  22. Involvement of the transmembrane protein p23 in biosynthetic protein transport.
    J Cell Biol. 1997 Dec 1;139(5):1119-35 PMID: 9382861
  23. Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast.
    J Cell Sci. 1997 Nov;110 ( Pt 21):2703-14 PMID: 9427388
  24. gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer.
    J Cell Biol. 1998 Feb 23;140(4):751-65 PMID: 9472029
  25. The Gas1 glycoprotein, a putative wall polymer cross-linker.
    Biochim Biophys Acta. 1999 Jan 6;1426(2):385-400 PMID: 9878845
  26. Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors.
    Cell. 1999 Feb 19;96(4):495-506 PMID: 10052452
  27. Erp1p and Erp2p, partners for Emp24p and Erv25p in a yeast p24 complex.
    Mol Biol Cell. 1999 Jun;10(6):1923-38 PMID: 10359606
  28. Localization and recycling of gp27 (hp24gamma3): complex formation with other p24 family members.
    Mol Biol Cell. 1999 Jun;10(6):1939-55 PMID: 10359607
  29. Intracellular aspects of the process of protein synthesis.
    Science. 1975 Aug 1;189(4200):347-58 PMID: 1096303
Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.148.5.925
Published
2000-03-06
Pages
925-30
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2174538
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.148.5.925 PMC Full Text View journal details
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