YET1, YET2 and YET3 of Saccharomyces cerevisiae Encode BAP31 Homologs with Partially Overlapping Functions

Toikkanen, H Jaana; Fatal, Netta; Hildén, Pekka; Makarow, Marja; Kuismanen, Esa

doi:10.3923/jbs.2006.446.456

Cited by 5 publications

(2 citation statements)

References 49 publications

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“…Surprisingly, we found one additional protein, of less characterized function, that had a similar distribution, Yet3 (Yeast Endoplasmic reticulum Transmembrane 3). Yet3 is a protein of the ER with three predicted transmembrane domains (TMD), which has two paralogs Yet1 and Yet2 34 . In addition, it is highly conserved to mammals with its human homolog being BAP31 (B-cell receptor Associated Protein of 31kDa) 34 .…”

Section: Resultsmentioning

confidence: 99%

“…Yet3 is a protein of the ER with three predicted transmembrane domains (TMD), which has two paralogs Yet1 and Yet2 34 . In addition, it is highly conserved to mammals with its human homolog being BAP31 (B-cell receptor Associated Protein of 31kDa) 34 . BAP31 is also an ER membrane protein, first discovered due to its role in B-cell receptor maturation 35 .…”

Section: Resultsmentioning

confidence: 99%

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The molecular mechanism of on-demand sterol biosynthesis at organelle contact sites

Zung,

Aravindan,

Boshnakovska

et al. 2024

Preprint

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Contact-sites are specialized zones of proximity between two organelles, essential for organelle communication and coordination. The formation of contacts between the Endoplasmic Reticulum (ER), and other organelles, relies on a unique membrane environment enriched in sterols. However, how these sterol-rich domains are formed and maintained had not been understood. We found that the yeast membrane protein Yet3, the homolog of human BAP31, is localized to multiple ER contact sites. We show that Yet3 interacts with all the enzymes of the post-squalene ergosterol biosynthesis pathway and recruits them to create sterol-rich domains. Increasing sterol levels at ER contacts causes its depletion from the plasma membrane leading to a compensatory reaction and altered cell metabolism. Our data shows that Yet3 provides on-demand sterols at contacts thus shaping organellar structure and function. A molecular understanding of this proteins functions gives new insights into the role of BAP31 in development and pathology.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

The molecular mechanism of on-demand sterol biosynthesis at organelle contact sites

Zung,

Aravindan,

Boshnakovska

et al. 2024

Preprint

View full text Add to dashboard Cite

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BAP31: Physiological functions and roles in disease

Quistgaard

2021

Biochimie

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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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YET1, YET2 and YET3 of Saccharomyces cerevisiae Encode BAP31 Homologs with Partially Overlapping Functions

Cited by 5 publications

References 49 publications

The molecular mechanism of on-demand sterol biosynthesis at organelle contact sites

The molecular mechanism of on-demand sterol biosynthesis at organelle contact sites

BAP31: Physiological functions and roles in disease

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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