An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding.

Stamnes, Mark; Craighead, Mark; Hoe, Mee H.; Lampen, Nina; Geromanos, Scott; Tempst, Paul; Rothman, James E.

doi:10.1073/pnas.92.17.8011

Cited by 214 publications

(253 citation statements)

References 37 publications

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“…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). Their involvement in COP I vesicle formation was identified in vitro by using liposomes with Golgi-like lipid composition.…”

mentioning

confidence: 99%

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

115

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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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mentioning

confidence: 99%

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

115

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“…In a yeast strain defective for vesicle fusion, a p24 knockout reduced the number of COPI-coated vesicles (Stamnes et al 1995). These data suggested that type I transmembrane proteins represent membrane receptors for coatomer and are actively required for the formation of COPI vesicles (Stamnes et al 1995;Sohn et al 1996). Surprisingly, however, in yeast the deletion of all p24 proteins showed only a reduction in the rate of transport of some cargo proteins (Springer et al 2000).…”

Section: Coat Recruitmentmentioning

confidence: 69%

“…p24 proteins are present in COPI vesicles in amounts stoichiometric to coatomer (Sohn et al 1996). In a yeast strain defective for vesicle fusion, a p24 knockout reduced the number of COPI-coated vesicles (Stamnes et al 1995). These data suggested that type I transmembrane proteins represent membrane receptors for coatomer and are actively required for the formation of COPI vesicles (Stamnes et al 1995;Sohn et al 1996).…”

Section: Coat Recruitmentmentioning

confidence: 80%

“…Nevertheless, in the presence of a cytoplasmic domain of a p24 family protein, vesicle formation is stimulated, and independent of a wide range of lipid compositions ). As described above, the p24 proteins were initially found to be a major component of COPI-coated vesicles (Stamnes et al 1995;Sohn et al 1996) and serve as membrane machinery for these carriers.…”

Section: Budding and Scissionmentioning

confidence: 99%

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COPI Budding within the Golgi Stack

Popoff

Adolf²,

Brügger³

et al. 2011

Cold Spring Harbor Perspectives in Biology

151

169

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The Golgi serves as a hub for intracellular membrane traffic in the eukaryotic cell. Transport within the early secretory pathway, that is within the Golgi and from the Golgi to the endoplasmic reticulum, is mediated by COPI-coated vesicles. The COPI coat shares structural features with the clathrin coat, but differs in the mechanisms of cargo sorting and vesicle formation. The small GTPase Arf1 initiates coating on activation and recruits en bloc the stable heptameric protein complex coatomer that resembles the inner and the outer shells of clathrin-coated vesicles. Different binding sites exist in coatomer for membrane machinery and for the sorting of various classes of cargo proteins. During the budding of a COPI vesicle, lipids are sorted to give a liquid-disordered phase composition. For the release of a COPI-coated vesicle, coatomer and Arf cooperate to mediate membrane separation.

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“…Furthermore, the binding of the plasma membrane AP-2 adaptors to tyrosine-based motifs was shown to be strengthened upon clathrin coat formation, suggesting that cargo recognition and coat assembly are indeed coupled (49). By analogy, it has been proposed that some members of the p24 family, which can bind via their dilysine motifs to coatomer in vitro and are found in COPI-coated vesicles (13,18,27), may act in the donor membrane as cargo receptors and coatomer and/or ARF receptors. In fact, p23 and p24 cytoplasmic tails attached to artificial liposomes of physiological lipid composition appear sufficient to recruit coatomer in the presence of ARF-GTP to these membranes (21).…”

Section: ⑀-Cop-depleted Copi Binding To Membranes and Sorting Signalmentioning

confidence: 99%

Membrane Recruitment of Coatomer and Binding to Dilysine Signals Are Separate Events

Gomez

Scales

Kreis

et al. 2000

Journal of Biological Chemistry

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An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding.

Cited by 214 publications

References 37 publications

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

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

COPI Budding within the Golgi Stack

Membrane Recruitment of Coatomer and Binding to Dilysine Signals Are Separate Events

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