gp25L/emp24/p24 Protein Family Members of the <i>cis-</i>Golgi Network Bind Both COP I and II Coatomer

Dominguez, Michel; Dejgaard, Kurt; Füllekrug, Joachim; Dahan, Sophie; Fazel, Ali; Paccaud, Jean‐Pierre; Thomas, David Y.; Bergeron, John J.M.; Nilsson, Tommy

doi:10.1083/jcb.140.4.751

Cited by 324 publications

(537 citation statements)

References 72 publications

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“…In accord with these results, previous studies have shown that VIP36 cycles between the ER and Golgi (53), although it may also operate at a post-Golgi level in some cells (54). P24 family members are known to cycle in the early secretory pathway, both in higher eukaryotes and in yeast, and to operate as cargo receptors linking cargo to COPI and COPII coats (13,(55)(56)(57)(58).…”

Section: Purification Of Ergic Membranes From Bfa-treated Cells-supporting

confidence: 64%

Proteomics of Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC) Membranes from Brefeldin A-treated HepG2 Cells Identifies ERGIC-32, a New Cycling Protein That Interacts with Human Erv46

Breuza

Halbeisen

Jenö

et al. 2004

Journal of Biological Chemistry

113

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Cycling proteins play important roles in the organization and function of the early secretory pathway by participating in membrane traffic and selective transport of cargo between the endoplasmic reticulum (ER), the intermediate compartment (ERGIC), and the Golgi. To identify new cycling proteins, we have developed a novel procedure for the purification of ERGIC membranes from HepG2 cells treated with brefeldin A, a drug known to accumulate cycling proteins in the ERGIC. Membranes enriched 110-fold over the homogenate for ERGIC-53 were obtained and analyzed by mass spectrometry. Major proteins corresponded to established and putative cargo receptors and components mediating protein maturation and membrane traffic. Among the uncharacterized proteins, a 32-kDa protein termed ERGIC-32 is a novel cycling membrane protein with sequence homology to Erv41p and Erv46p, two proteins enriched in COPII vesicles of yeast. ERGIC-32 localizes to the ERGIC and partially colocalizes with the human homologs of Erv41p and Erv46p, which mainly localize to the cis-Golgi. ERGIC-32 interacts with human Erv46 (hErv46) as revealed by covalent cross-linking and mistargeting experiments, and silencing of ERGIC-32 by small interfering RNAs increases the turnover of hErv46. We propose that ERGIC-32 functions as a modulator of the hErv41-hErv46 complex by stabilizing hErv46. Our novel approach for the isolation of the ERGIC from BFA-treated cells may ultimately lead to the identification of all proteins rapidly cycling early in the secretory pathway.

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Section: Purification Of Ergic Membranes From Bfa-treated Cells-supporting

confidence: 64%

Proteomics of Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC) Membranes from Brefeldin A-treated HepG2 Cells Identifies ERGIC-32, a New Cycling Protein That Interacts with Human Erv46

Breuza

Halbeisen

Jenö

et al. 2004

Journal of Biological Chemistry

113

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“…Because ERGIC-53 forms homohexamers (Schweizer et al, 1988), this complex can be expected to be very large so that it may not have entered the Blue Native gel. It is widely recognized that p24 family proteins form heterooligomeric complexes with one another, which complicates the functional analysis of these proteins (Dominguez et al, 1998). The current study suggests that the situation is even more complex.…”

Section: Discussionmentioning

confidence: 74%

“…The finding that a double knockdown of Surf4 and ERGIC-53 and a single knockdown of p25 induced a Golgi phenotype was unexpected because all three proteins are mainly associated with the ERGIC, although they also cycle through the Golgi to some extent (Schweizer et al, 1988;Dominguez et al, 1998;Klumperman et al, 1998). Furthermore, a study on the reconstitution of the secretory pathway in a cell-free assay suggests that p25 plays a role in the de novo formation of the ERGIC (Lavoie et al, 1999).…”

Section: Cargo Receptor Silencing Destabilizes the Ergic Without Affementioning

confidence: 99%

“…To achieve their correct targeting within the early secretory pathway they are in a dynamic equilibrium to form homo-and heterodimers with each other Jenne et al, 2002). All p24 family members are type I membrane proteins and share a common structure, with a short cytoplasmic tail containing binding signals for COP I and COP II coat complexes and a luminal domain with potential secretory cargo binding capabilities Sohn et al, 1996;Dominguez et al, 1998;Muniz et al, 2000). Proteomics analysis revealed that p24 family members are major constituents of COP I-coated vesicles (Stamnes et al, 1995).…”

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confidence: 99%

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The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi

Mitrović

Ben-Tekaya

Koegler

et al. 2008

MBoC

119

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Rapidly cycling proteins of the early secretory pathway can operate as cargo receptors. Known cargo receptors are abundant proteins, but it remains mysterious why their inactivation leads to rather limited secretion phenotypes. Studies of Surf4, the human orthologue of the yeast cargo receptor Erv29p, now reveal a novel function of cargo receptors. Surf4 was found to interact with endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53 and p24 proteins. Silencing Surf4 together with ERGIC-53 or silencing the p24 family member p25 induced an identical phenotype characterized by a reduced number of ERGIC clusters and fragmentation of the Golgi apparatus without effect on anterograde transport. Live imaging showed decreased stability of ERGIC clusters after knockdown of p25. Silencing of Surf4/ERGIC-53 or p25 resulted in partial redistribution of coat protein (COP) I but not Golgi matrix proteins to the cytosol and partial resistance of the cis-Golgi to brefeldin A. These findings imply that cargo receptors are essential for maintaining the architecture of ERGIC and Golgi by controlling COP I recruitment. INTRODUCTIONThe secretory pathway of higher eukaryotic cells is composed of the three membrane organelles endoplasmic reticulum (ER), ER-Golgi intermediate compartment (ERGIC), and Golgi (Bonifacino and Glick, 2004;Appenzeller-Herzog and Hauri, 2006). Maintenance of these organelles requires a balance of anterograde (secretory) and retrograde vesicular traffic. Anterograde traffic from ER to ERGIC is mediated by coat protein (COP) II vesicles that form at ER exit sites (Aridor et al., 1995;Zeuschner et al., 2006) and fuse with the ERGIC that consists of a few hundred tubulovesicular membrane clusters in vicinity of ER exit sites (AppenzellerHerzog and Hauri, 2006). Transport from ERGIC to Golgi is mediated by pleomorphic vesicles (Ben-Tekaya et al., 2005) that carry COP I (Presley et al., 1997;Scales et al., 1997), although the mechanism of their formation remains unknown. Retrograde traffic mediated by COP I vesicles can occur from ERGIC or Golgi and recycles membrane proteins that possess either dilysine signals, including ERGIC-53 and KDEL-receptor, or diphenylalanine signals, such as members of the 24 protein family. This rapid COP I-dependent recycling is distinct from the slow Golgi-to-ER recycling of Golgi resident proteins that is COP I independent and can be either constitutive or induced (Storrie, 2005).Major constituents of anterograde and retrograde transport vesicles are transmembrane cargo receptors that mediate protein sorting by linking soluble cargo on the luminal side and coat assembly on the cytoplasmic side. To date, only few cargo receptors have been studied in detail. The polytopic transmembrane protein Erv29p is known to cycle between ER and Golgi in yeast and to operate as a cargo receptor (Belden and Barlowe, 2001). Erv29p is required for efficient packaging of the glycosylated ␣-factor pheromone precursor into COP II vesicles departing from the ER. Maturation of carboxypeptidase Y...

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“…It is generally believed that transmembrane proteins are selectively recruited into ER exit sites by interactions of their cytoplasmic tails with the coat protein complex (COPII) coat (30,31). HLA-A2 lacks either of the putative signals for ER export, the di-phenylalanine (FF), or the diacidic (DϫE) motifs (32)(33)(34)(35)(36). Conceivably, it may contain another, yet unidentified, ER exit signal.…”

Section: Discussionmentioning

confidence: 99%

Clustering of Peptide-Loaded MHC Class I Molecules for Endoplasmic Reticulum Export Imaged by Fluorescence Resonance Energy Transfer

Pentcheva

Edidin

2001

The Journal of Immunology

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Fluorescence resonance energy transfer between cyan fluorescent protein- and yellow fluorescent protein-tagged MHC class I molecules reports on their spatial organization during assembly and export from the endoplasmic reticulum (ER). A fraction of MHC class I molecules is clustered in the ER at steady state. Contrary to expectations from biochemical models, this fraction is not bound to the TAP. Instead, it appears that MHC class I molecules cluster after peptide loading. This clustering points toward a novel step involved in the selective export of peptide-loaded MHC class I molecules from the ER. Consistent with this model, we detected clusters of wild-type HLA-A2 molecules and of mutant A2-T134K molecules that cannot bind TAP, but HLA-A2 did not detectably cluster with A2-T134K at steady state. Lactacystin treatment disrupted the HLA-A2 clusters, but had no effect on the A2-T134K clusters. However, when cells were fed peptides with high affinity for HLA-A2, mixed clusters containing both HLA-A2 and A2-T134K were detected.

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gp25L/emp24/p24 Protein Family Members of the cis-Golgi Network Bind Both COP I and II Coatomer

Cited by 324 publications

References 72 publications

Proteomics of Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC) Membranes from Brefeldin A-treated HepG2 Cells Identifies ERGIC-32, a New Cycling Protein That Interacts with Human Erv46

Proteomics of Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC) Membranes from Brefeldin A-treated HepG2 Cells Identifies ERGIC-32, a New Cycling Protein That Interacts with Human Erv46

The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi

Clustering of Peptide-Loaded MHC Class I Molecules for Endoplasmic Reticulum Export Imaged by Fluorescence Resonance Energy Transfer

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