Erv14p Directs a Transmembrane Secretory Protein into COPII-coated Transport Vesicles

Powers, Jacqueline; Barlowe, Charles

doi:10.1091/mbc.01-10-0499

Cited by 112 publications

(128 citation statements)

References 50 publications

(89 reference statements)

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“…No sequence similarity can be detected between these two proteins, and whereas PHO86 has four predicted transmembrane domains, PHF1 has only one. In yeast, known accessory proteins such as GSF2, SHR3, and ERV14, which are involved in the ER exit of specific hexose transporters, specific amino acid permeases, and a membrane glycoprotein, respectively, display strikingly different structures (Gilstring et al, 1999;Sherwood and Carlson, 1999;Powers and Barlowe, 2002). The fact that PHF1 and PHO86 both act on closely related proteins (Pi transporters) strongly suggests that the existence of structural diversity among accessory proteins reflects fairly loose structural constraints for performing this type of function.…”

Section: Discussionmentioning

confidence: 99%

PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 Is a Plant-Specific SEC12-Related Protein That Enables the Endoplasmic Reticulum Exit of a High-Affinity Phosphate Transporter in Arabidopsis [W]

et al. 2005

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PHOSPHATE TRANSPORTER1 (PHT1) genes encode phosphate (Pi) transporters that play a fundamental role in Pi acquisition and remobilization in plants. Mutation of the Arabidopsis thaliana PHOSPHATE TRANSPORTER TRAFFIC FACILITA-TOR1 (PHF1) impairs Pi transport, resulting in the constitutive expression of many Pi starvation-induced genes, increased arsenate resistance, and reduced Pi accumulation. PHF1 expression was detected in all tissues, particularly in roots, flowers, and senescing leaves, and was induced by Pi starvation, thus mimicking the expression patterns of the whole PHT1 gene family. PHF1 was localized in endoplasmic reticulum (ER), and mutation of PHF1 resulted in ER retention and reduced accumulation of the plasma membrane PHT1;1 transporter. By contrast, the PIP2A plasma membrane protein was not mislocalized, and the secretion of Pi starvation-induced RNases was not affected in the mutant. PHF1 encodes a plantspecific protein structurally related to the SEC12 proteins of the early secretory pathway. However, PHF1 lacks most of the conserved residues in SEC12 proteins essential as guanine nucleotide exchange factors. Although it functions in early secretory trafficking, PHF1 likely evolved a novel mechanism accompanying functional specialization on Pi transporters. The identification of PHF1 reveals that plants are also endowed with accessory proteins specific for selected plasma membrane proteins, allowing their exit from the ER, and that these ER exit cofactors may have a phylum-specific origin.

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Section: Discussionmentioning

confidence: 99%

PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 Is a Plant-Specific SEC12-Related Protein That Enables the Endoplasmic Reticulum Exit of a High-Affinity Phosphate Transporter in Arabidopsis [W]

et al. 2005

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“…In sma2D cells, not only is prospore membrane shape abnormal, but the leading edge complex is abnormally expanded in shape and spore formation is blocked (Rabitsch et al 2001). Erv14 is an ER-localized cargo receptor necessary for the export of some integral membrane proteins from the ER (Powers and Barlowe 2002). The defect in the erv14D mutant cells is likely due to effects on export of Sma2 .…”

Section: Membrane-cytoskeletal Interactionsmentioning

confidence: 99%

Sporulation in the Budding Yeast Saccharomyces cerevisiae

2011

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In response to nitrogen starvation in the presence of a poor carbon source, diploid cells of the yeast Saccharomyces cerevisiae undergo meiosis and package the haploid nuclei produced in meiosis into spores. The formation of spores requires an unusual cell division event in which daughter cells are formed within the cytoplasm of the mother cell. This process involves the de novo generation of two different cellular structures: novel membrane compartments within the cell cytoplasm that give rise to the spore plasma membrane and an extensive spore wall that protects the spore from environmental insults. This article summarizes what is known about the molecular mechanisms controlling spore assembly with particular attention to how constitutive cellular functions are modified to create novel behaviors during this developmental process. Key regulatory points on the sporulation pathway are also discussed as well as the possible role of sporulation in the natural ecology of S. cerevisiae. TABLE OF CONTENTS Abstract 737Introduction 738

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“…These observations led to the proposal that BAP31 functions as an ER export receptor (15,44). A salient feature of characterized ER export receptors is efficient incorporation into in vitro generated COPII vesicles (37,(45)(46)(47). We reasoned that if the yeast BAP31 homologs acted as ER export receptors they should be efficiently packaged into COPII vesicles.…”

Section: Expression Of Yet Proteins Is Influenced By Reductive Er Strmentioning

confidence: 99%

Yet1p and Yet3p, the Yeast Homologs of BAP29 and BAP31, Interact with the Endoplasmic Reticulum Translocation Apparatus and Are Required for Inositol Prototrophy

Wilson

Barlowe

2010

Journal of Biological Chemistry

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The mammalian B-cell receptor-associated proteins of 29 and 31 kDa (BAP29 and BAP31) are conserved integral membrane proteins that have reported roles in endoplasmic reticulum (ER) quality control, ER export of secretory cargo, and programmed cell death. In this study we investigated the yeast homologs of BAP29 and BAP31, known as Yet1p and Yet3p, to gain insight on cellular function. We found that Yet1p forms a complex with Yet3p (Yet complex) and that complex assembly was important for subunit stability and proper ER localization. The Yet complex was not efficiently packaged into ER-derived COPII vesicles and therefore does not appear to act as an ER export receptor. Instead, a fraction of the Yet complex was detected in association with the ER translocation apparatus (Sec complex). Specific mutations in the Sec complex or Yet complex influenced these interactions. Moreover, associations between the Yet complex and Sec complex were increased by ER stress and diminished when protein translocation substrates were depleted. Surprisingly, yet1⌬ and yet3⌬ mutant strains displayed inositol starvation-related growth defects. In accord with the biochemical data, these growth defects were exacerbated by a combination of certain mutations in the Sec complex with yet1⌬ or yet3⌬ mutations. We propose a model for the Yet-Sec complex interaction that places Yet1p and Yet3p at the translocation pore to manage biogenesis of specific transmembrane secretory proteins.

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Erv14p Directs a Transmembrane Secretory Protein into COPII-coated Transport Vesicles

Cited by 112 publications

References 50 publications

PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 Is a Plant-Specific SEC12-Related Protein That Enables the Endoplasmic Reticulum Exit of a High-Affinity Phosphate Transporter in Arabidopsis [W]

PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 Is a Plant-Specific SEC12-Related Protein That Enables the Endoplasmic Reticulum Exit of a High-Affinity Phosphate Transporter in Arabidopsis [W]

Sporulation in the Budding Yeast Saccharomyces cerevisiae

Yet1p and Yet3p, the Yeast Homologs of BAP29 and BAP31, Interact with the Endoplasmic Reticulum Translocation Apparatus and Are Required for Inositol Prototrophy

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