ER-Associated Degradation of Membrane Proteins in Yeast

Thozée, Cédric Pety de; Ghislain, Michel

doi:10.1100/tsw.2006.191

Cited by 3 publications

(1 citation statement)

References 140 publications

(200 reference statements)

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“…It is hypothesized that, after blocking of the anterograde transport from the ER to the Golgi, the premature ABCG9 may be overaccumulated in the ER, and subsequently, excessive sGFP:ABCG9 proteins in the ER may trigger ER stress. The ER stress response may attenuate sGFP: ABCG9 translation to release the stress on the ER, or sGFP:ABCG9 may be subjected to proteasome-associated degradation (Pety de Thozée and Ghislain, 2006;Kakoi et al, 2013;Wan and Jiang, 2016), which also needs further investigation. Moreover, the identification of other candidates also needs to be explored.…”

Section: Discussionmentioning

confidence: 99%

Secretory COPII Protein SEC31B Is Required for Pollen Wall Development

et al. 2016

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The pollen wall protects pollen grains from abiotic and biotic stresses. During pollen wall development, tapetal cells play a vital role by secreting proteins, signals, and pollen wall material to ensure microspore development. But the regulatory mechanism underlying the secretory pathway of the tapetum is largely unknown. Here, we characterize the essential role of the Arabidopsis (Arabidopsis thaliana) COPII protein SECRETORY31B (SEC31B) in pollen wall development and the secretory activity of tapetal cells. The sporophyte-controlled atsec31b mutant exhibits severe pollen and seed abortion. Transmission electron microscopy observation indicates that pollen exine formation in the atsec31b mutant is disrupted significantly. AtSEC31B is a functional COPII protein revealed by endoplasmic reticulum (ER) exit site localization, interaction with AtSEC13A, and retarded ER-Golgi protein trafficking in the atsec31b mutant. A genetic tapetum-specific rescue assay indicates that AtSEC31B functions primarily in the tapetum. Moreover, deletion of AtSEC31B interrupted the formation of the ER-derived tapetosome and altered the location of the ATP-BINDING CASSETTE TRANSPORTER9 protein in the tapetum. Therefore, this work demonstrates that AtSEC31B plays a vital role in pollen wall development by regulating the secretory pathway of the tapetal cells.

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Section: Discussionmentioning

confidence: 99%

Secretory COPII Protein SEC31B Is Required for Pollen Wall Development

et al. 2016

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The secretory pathway: exploring yeast diversity

et al. 2013

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Protein secretion is an essential process for living organisms. In eukaryotes, this encompasses numerous steps mediated by several hundred cellular proteins. The core functions of translocation through the endoplasmic reticulum membrane, primary glycosylation, folding and quality control, and vesicle-mediated secretion are similar from yeasts to higher eukaryotes. However, recent research has revealed significant functional differences between yeasts and mammalian cells, and even among diverse yeast species. This review provides a current overview of the canonical protein secretion pathway in the model yeast Saccharomyces cerevisiae, highlighting differences to mammalian cells as well as currently unresolved questions, and provides a genomic comparison of the S. cerevisiae pathway to seven other yeast species where secretion has been investigated due to their attraction as protein production platforms, or for their relevance as pathogens. The analysis of Candida albicans, Candida glabrata, Kluyveromyces lactis, Pichia pastoris, Hansenula polymorpha, Yarrowia lipolytica, and Schizosaccharomyces pombe reveals that many - but not all - secretion steps are more redundant in S. cerevisiae due to duplicated genes, while some processes are even absent in this model yeast. Recent research obviates that even where homologous genes are present, small differences in protein sequence and/or differences in the regulation of gene expression may lead to quite different protein secretion phenotypes.

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Yeast ATP-Binding Cassette Transporters Conferring Multidrug Resistance

Prasad

Goffeau

2012

Annu. Rev. Microbiol.

200

176

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Overexpression of the ATP-binding cassette (ABC) drug transporter P-glycoprotein (P-gp) is often responsible for the failure of chemotherapy as a treatment for human tumors. The presence of proteins homologous to P-gp in organisms ranging from prokaryotes to eukaryotes indicates that drug export is a general mechanism of multidrug resistance. Yeasts are no exception. They have developed a large subfamily of ABC exporters involved in pleiotropic drug resistance (PDR) and in the cellular efflux of a wide variety of drugs. The PDR transporters Pdr5p of Saccharomyces cerevisiae and Cdr1p of Candida albicans are important members of this PDR subfamily, which comprises up to 10 phylogenetic clusters in fungi. Here, we review current achievements concerning the structure, molecular mechanism, and physiological functions of yeast Pdr transporters.

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ER-Associated Degradation of Membrane Proteins in Yeast

Cited by 3 publications

References 140 publications

Secretory COPII Protein SEC31B Is Required for Pollen Wall Development

Secretory COPII Protein SEC31B Is Required for Pollen Wall Development

The secretory pathway: exploring yeast diversity

Yeast ATP-Binding Cassette Transporters Conferring Multidrug Resistance

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