Bos1p, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence

Lian, Jian; Ferro‐Novick, Susan

doi:10.1016/0092-8674(93)90253-m

Cited by 136 publications

(106 citation statements)

References 32 publications

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“…In Vitro Transport Assay-Standard transport assays, as well as the preparation of fractions and reagents, were performed as described previously (20,21). In all assays where antibody was included, a 20-min preincubation was performed on ice prior to the 20°C incubation.…”

Section: Methodsmentioning

confidence: 99%

“…In all assays where antibody was included, a 20-min preincubation was performed on ice prior to the 20°C incubation. Vesicles used for immunoprecipitation were produced during an in vitro budding reaction as described previously (20). Reactions were performed in the presence or absence of antibody (8 -12 g of anti-Yif1p or anti-Yip1p) as indicated with the exception that the protein A-Sepharose beads were washed four times with TBS buffer before boiling in sample buffer.…”

Section: Methodsmentioning

confidence: 99%

“…To begin to determine if the Yip1p⅐Yif1p machinery interacts with the SNAREs, we examined the binding affinity of Yip1p for Bos1p in vitro. Bos1p is a stage-specific v-SNARE that is packaged into vesicles and required for anterograde ER-Golgi transport (20,32,33). For our studies, full-length Yip1p was fused to maltose-binding protein (MBPYip1p) and purified.…”

Section: Fig 4 Membrane Attachment and Localization Of Ypt1p Is Notmentioning

confidence: 99%

“…Fractions (1 ml) were collected and processed with ConA-Sepharose followed by precipitation with anti-outer chain serum as described previously (20,22). A, vesicles formed in the presence of anti-Yif1p antibody peak in fraction 5.…”

Section: Fig 3 Vesicle Fusion But Not Vesicle Tethering Is Blockementioning

confidence: 99%

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The Yip1p·Yif1p Complex Is Required for the Fusion Competence of Endoplasmic Reticulum-derived Vesicles

Barrowman¹,

Wang²,

Zhang

et al. 2003

Journal of Biological Chemistry

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Here we report that Yip1p and Yif1p, two members of an integral membrane protein complex that bind to the Rab Ypt1p, are required for membrane fusion with the Golgi in vitro. To block fusion, anti-Yip1p or anti-Yif1p antibodies must be added before vesicles bud from the endoplasmic reticulum (ER). These antibodies do not block the packaging of Yip1p, Yif1p, or the soluble NSF attachment protein receptor (SNAREs) into vesicles. We propose that Yip1p and Yif1p perform a critical role in establishing the fusion competence of ER to Golgi vesicles at the time of budding. Consistent with this proposal, we observe that the Yip1p⅐Yif1p complex binds to the ER to Golgi SNAREs Bos1p and Sec22p, two components of the membrane fusion machinery.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Fig 4 Membrane Attachment and Localization Of Ypt1p Is Notmentioning

confidence: 99%

Section: Fig 3 Vesicle Fusion But Not Vesicle Tethering Is Blockementioning

confidence: 99%

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The Yip1p·Yif1p Complex Is Required for the Fusion Competence of Endoplasmic Reticulum-derived Vesicles

Barrowman¹,

Wang²,

Zhang

et al. 2003

Journal of Biological Chemistry

Self Cite

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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).…”

mentioning

confidence: 99%

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

McNew¹,

Søgaard²,

Lampen³

et al. 1997

Journal of Biological Chemistry

224

223

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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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TheSaccharomyces cerevisiae early secretion mutanttip20 is synthetic lethal with mutants in yeast coatomer and the SNARE proteins Sec22p and Ufe1p

Frigerio

1998

Yeast

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Tip20p is an 80 kDa cytoplasmic protein bound to the cytoplasmic surface of the endoplasmic reticulum (ER) by interaction with the type II integral membrane protein Sec20p. Both proteins are required for vesicular transport between the ER and Golgi complex. Recently, sec20–1 was found to be defective in retrograde transport. A collection of temperature‐sensitive tip20 mutants are shown to be lethal in combination with ufe1–1, a target SNARE of the ER and ret2–1, yeast δ‐COP. A subset of tip20 mutants was found to be lethal in combination with sec20–1, sec21–1, sec22–3 and sec27–1. Since all pairwise combinations of a tip20 mutant, sec20–1, and ufe1–1 are lethal, Tip20p and Sec20p might be part of the docking complex for Golgi‐derived retrograde transport vesicles. Since carboxy‐terminal tip20 truncations are lethal in combination with mutants in three coatomer subunits, Tip20p might be involved in binding or uncoating of COPI coated retrograde transport vesicles. © 1998 John Wiley & Sons, Ltd.

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Bos1p, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence

Cited by 136 publications

References 32 publications

The Yip1p·Yif1p Complex Is Required for the Fusion Competence of Endoplasmic Reticulum-derived Vesicles

The Yip1p·Yif1p Complex Is Required for the Fusion Competence of Endoplasmic Reticulum-derived Vesicles

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

TheSaccharomyces cerevisiae early secretion mutanttip20 is synthetic lethal with mutants in yeast coatomer and the SNARE proteins Sec22p and Ufe1p

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