ArticleThe Journal of biological chemistry2010
Yet1p and Yet3p, the yeast homologs of BAP29 and BAP31, interact with the endoplasmic reticulum translocation apparatus and are required for inositol prototrophy.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
- Tomato B cell receptor-associated protein 31 homologs enhance thermotolerance by promoting chloroplast PSBW accumulation and stabilizing the PSII-LHCII complex.Plant communications · 2026Article
- Reconstitution of autophagic-like membrane tethering reveals that Atg11 can bind and cluster vesicles on cargo mimetics.Autophagy · 2026Article
- The Erv41-Erv46 complex serves as a retrograde receptor to retrieve misfolded secretory proteins that have escaped from the ER.Molecular biology of the cell · 2025Article
- The molecular mechanism of on-demand sterol biosynthesis at organelle contact sites.bioRxiv : the preprint server for biology · 2024Article
- The C-terminus of the cargo receptor Erv14 affects COPII vesicle formation and cargo delivery.Journal of cell science · 2023Article
- B-cell receptor-associated protein 31 promotes migration and invasion in ovarian cancer cells.Experimental and therapeutic medicine · 2021Article
- Molecular dissection of the Erv41-Erv46 retrograde receptor reveals a conserved cysteine-rich region in Erv46 required for retrieval activity.Molecular biology of the cell · 2020Article
- B-Cell Receptor-Associated Protein 31 Negatively Regulates the Expression of Monoamine Oxidase AFrontiers in molecular biosciences · 2020Article
- Mechanistic Connections between Endoplasmic Reticulum (ER) Redox Control and Mitochondrial Metabolism.Cells · 2019Review
- Conserved juxtamembrane domains in the yeast golgin Coy1 drive assembly of a megadalton-sized complex and mediate binding to tethering and SNARE proteins.The Journal of biological chemistry · 2019Article
- Classification of Trispanins: A Diverse Group of Proteins That Function in Membrane Synthesis and Transport Mechanisms.Frontiers in cell and developmental biology · 2019Article
- The Golgin protein Coy1 functions in intra-Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs.Molecular biology of the cell · 2017Article
- Of yeast, mice and men: MAMs come in two flavors.Biology direct · 2017Review
- Plant-specific 4/1 polypeptide interacts with an endoplasmic reticulum protein related to human BAP31.Planta · 2017Article
- Analysis of COPII Vesicles Indicates a Role for the Emp47-Ssp120 Complex in Transport of Cell Surface Glycoproteins.Traffic (Copenhagen, Denmark) · 2016Article
- Yeast Integral Membrane Proteins Apq12, Brl1, and Brr6 Form a Complex Important for Regulation of Membrane Homeostasis and Nuclear Pore Complex Biogenesis.Eukaryotic cell · 2015Article
- The Erv41-Erv46 complex serves as a retrograde receptor to retrieve escaped ER proteins.The Journal of cell biology · 2015Article
- Structural and biophysical characterization of the cytoplasmic domains of human BAP29 and BAP31.PloS one · 2013Article
- Yet1p-Yet3p interacts with Scs2p-Opi1p to regulate ER localization of the Opi1p repressor.Molecular biology of the cell · 2011Article
- Genome-wide screen for inositol auxotrophy in Saccharomyces cerevisiae implicates lipid metabolism in stress response signaling.Molecular genetics and genomics : MGG · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
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, yet1Delta and yet3Delta 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 yet1Delta or yet3Delta 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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