COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast

Bednarek, Sebastian Y.; Ravazzola, Mariella; Hosobuchi, Midori; Amherdt, M; Perrelet, Alain; Schekman, Randy; Orci, Lelio

doi:10.1016/0092-8674(95)90144-2

Cited by 263 publications

(188 citation statements)

References 53 publications

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“…A role for COPI in connection with ER is surprising, because coatomer prominently localizes to Golgi membranes but is not a significant morphological feature of ER membranes. But coatomer has been reported to promote vesicle budding from ER membranes in vitro (31) and to be localized to certain ER subdomains in mammalian cells (32). One possibility is that along with its classical role in vesicle formation, the multimeric network of coatomer could be involved in the clustering of proteins in subdomains of ER membranes without vesicle budding.…”

Section: Discussionmentioning

confidence: 99%

Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes

Lavieu

Orci²,

Shi

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Cortical endoplasmic reticulum (cER) is a permanent feature of yeast cells but occurs transiently in most animal cell types. Ist2p is a transmembrane protein that permanently localizes to the cER in yeast. When Ist2 is expressed in mammalian cells, it induces abundant cER containing Ist2. Ist2 cytoplasmic C-terminal peptide is necessary and sufficient to induce cER. This peptide sequence resembles classic coat protein complex I (COPI) coatomer protein-binding KKXX signals, and indeed the dimerized peptide binds COPI in vitro. Controlled dimerization of this peptide induces cER in cells. RNA interference experiments confirm that coatomer is required for cER induction in vivo, as are microtubules and the microtubule plus-end binding protein EB1. We suggest that Ist2 dimerization triggers coatomer binding and clustering of this protein into domains that traffic at the microtubule growing plus-end to generate the cER beneath the plasma membrane. Sequences similar to the Ist2 lysine-rich tail are found in mammalian STIM proteins that reversibly induce the formation of cER under calcium control

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Section: Discussionmentioning

confidence: 99%

Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes

Lavieu

Orci²,

Shi

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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“…A natural consequence of this is the tendency of GRP94-associated proteins to be co-retained in the ER compartment. Second, persistent association of GRP94 is likely to interfere with delivery of secretory proteins to ER export vesicles which (by poorly understood mechanisms) exclude the entry of ER lumenal resident proteins (57,58).…”

Section: Stoichiometry Of Immunoprecipitable Of Tg⅐grp94mentioning

confidence: 99%

Thyroglobulin Transport along the Secretory Pathway

Muresan

Arvan

1997

Journal of Biological Chemistry

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GRP94 serves as a molecular chaperone in the endoplasmic reticulum (ER). In normal thyrocytes, GRP94 interacts transiently with thyroglobulin (Tg), and in thyrocytes of animals suffering from congenital hypothyroid goiter with defective thyroglobulin, GRP94 and thyroglobulin associate in a protracted fashion. In order explore possible consequences of GRP94 binding, we have studied recombinant nonmutant thyroglobulin expressed in control Chinese hamster ovary (CHO) cells in comparison to that produced in CHO cells genetically manipulated for selectively increased GRP94 expression. Levels of ER chaperones other than GRP94 did not detectably differ, and thyroglobulin achieved transport competence in both kinds of CHO cells. However, increased availability of GRP94 caused the residence time of Tg in the ER to be remarkably prolonged. This was accompanied by a major increase in Tg directly associated with GRP94 and an increase in the ER pool size of Tg. Importantly, co-immunoprecipitation analysis revealed disulfide-linked Tg complexes (previously reported as an early Tg-folding intermediate) especially associated with GRP94. Indeed, non-native Tg, GRP94, and a 78-kDa protein likely to be BiP, appeared in ternary complexes. Under these conditions, GRP94 association appears directly involved in prolongation of Tg folding and export, consistent with a role in quality control in the ER.

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“…At the ER-Golgi transport step, the VAMP homologues Sec22p, Bos1p, and Bet1p (22)(23)(24) are required for the docking and/or fusion of ER-derived transport vesicles with the Golgi both in vitro and in vivo (25,26). Although controversial data exist about the localization of Bet1p in transport vesicles (26,27), Sec22p has been both found in COPI and COPII vesicles (28), as well as ER-Golgi transport vesicles devoid of cargo (29). These three ER-Golgi v-SNAREs interact with the t-SNARE Sed5p, which has been localized to the cis side of the Golgi stack in animal cells (30,31).…”

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confidence: 99%

Ykt6p, a Prenylated SNARE Essential for Endoplasmic Reticulum-Golgi Transport

McNew¹,

Søgaard²,

Lampen³

et al. 1997

Journal of Biological Chemistry

222

220

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Vesicular transport between secretory compartments requires specific recognition molecules called SNAREs. Here we report the identification of three putative SNAREs, p14 (Sft1p), p28 (Gos1p), and a detailed characterization of p26 (Ykt6p). All three were originally isolated as interacting partners of the cis Golgi target membrane-associated SNARE Sed5p, when Sec18p (yeast NSF) was inactivated. YKT6 is an essential gene that codes for a novel vesicle-associated SNARE functioning at the endoplasmic reticulum-Golgi transport step in the yeast secretory pathway. Depletion of Ykt6p results in the accumulation of the p1 precursor (endoplasmic reticulum form) of the vacuolar enzyme carboxypeptidase Y and morphological abnormalities consistent with a defect in secretion. Membrane localization of Ykt6p is essential for protein function and is normally mediated by isoprenylation. However, replacement of the isoprenylation motif with a bona fide transmembrane anchor results in a functional protein confirming that membrane localization, but not isoprenylation per se, is required for function. Ykt6p and its homologues are highly conserved from yeast to human as demonstrated by the functional complementation of the loss of Ykt6p by its human counterpart. This is the first example of a human SNARE protein functionally replacing a yeast SNARE. This observation implies that the specific details of the vesicle targeting code, like the genetic code, are conserved in evolution.

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COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast

Cited by 263 publications

References 53 publications

Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes

Induction of cortical endoplasmic reticulum by dimerization of a coatomer-binding peptide anchored to endoplasmic reticulum membranes

Thyroglobulin Transport along the Secretory Pathway

Ykt6p, a Prenylated SNARE Essential for Endoplasmic Reticulum-Golgi Transport

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