Mapping the functional yeast ABC transporter interactome

Snider, Jamie; Hanif, Asad; Lee, Mid Eum; Jin, Ke; Yu, Analyn R.; Graham, Chris; Chuk, Matthew; Damjanovic, Dunja; Wierzbicka, Marta; Tang, Priscilla; Balderes, Dina; Wong, Victoria; Jessulat, Matthew; Darowski, Katelyn Dawn; Luis, Bryan Joseph San; Shevelev, I. A.; Sturley, Stephen L.; Boone, Charles; Greenblatt, Jack; Zhang, Zhaolei; Paumi, Christian M.; Babu, Mohan; Park, Hay-Oak; Michaelis, Susan; Štagljar, Igor

doi:10.1038/nchembio.1293

Cited by 76 publications

(79 citation statements)

References 48 publications

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“…A novel S. cerevisiae glutathione exporter ABC protein (Adp1 or Gxa1p) was recently characterized (Kiriyama et al 2012), and has subsequently been located in the vacuole (Snider et al 2013). The role of this transporter in polyfunctional thiol release remains to be investigated.…”

Section: Discussionmentioning

confidence: 99%

Unravelling glutathione conjugate catabolism in Saccharomyces cerevisiae: the role of glutathione/dipeptide transporters and vacuolar function in the release of volatile sulfur compounds 3-mercaptohexan-1-ol and 4-mercapto-4-methylpentan-2-one

Cordente

Capone

Curtin

2015

Appl Microbiol Biotechnol

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Sulfur-containing aroma compounds are key contributors to the flavour of a diverse range of foods and beverages, such as wine. The tropical fruit characters of Sauvignon Blanc wines are attributed to the presence of the aromatic thiols 3-mercaptohexan-1-ol (3-MH), its acetate ester 3-mercaptohexyl acetate (3-MHA), and 4-mercapto-4-methylpentan-2-one (4-MMP). These aromatic thiols are not detectable in grape juice to any significant extent but are released by yeast during alcoholic fermentation. While the processes involved in the release of 3-MH and 4-MMP from their cysteinylated precursors have been studied extensively, degradation pathways for glutathione S-conjugates (GSH-3-MH and GSH-4-MMP) have not. In this study, a candidate gene approach was taken, focusing on genes known to play a role in glutathione and glutathione-S-conjugate turnover in Saccharomyces cerevisiae. Our results confirm the role of Opt1p as the major transporter responsible for uptake of GSH-3-MH and GSH-4-MMP, and identify vacuolar Ecm38p as a key determinant of 3-MH release from GSH-3-MH. ECM38 was unimportant, on the other hand, for release of 4-MMP, and abolition of vacuolar biogenesis caused an increase in the amount of 4-MMP released. The alternative cytosolic glutathione degradation pathway was not involved in release of either thiol from their glutathionylated precursors. Finally, cycling of GSH-3-MH and/or its breakdown intermediates between the cytosol and the vacuole or extracellular space was implicated in modulation of 3-MH formation. Together, these results provide new targets for development of yeast strains that optimize release of these potent volatile sulfur compounds, and further our understanding of the processes involved in glutathione-S-conjugate turnover.

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Section: Discussionmentioning

confidence: 99%

Unravelling glutathione conjugate catabolism in Saccharomyces cerevisiae: the role of glutathione/dipeptide transporters and vacuolar function in the release of volatile sulfur compounds 3-mercaptohexan-1-ol and 4-mercapto-4-methylpentan-2-one

Cordente

Capone

Curtin

2015

Appl Microbiol Biotechnol

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“…Therefore, the study of the PPIs involved in the HOG pathway is important for determining the methods by which proteins come together to mediate a proper cellular reaction to extracellular stress. In this study, we took advantage of the MYTH method in budding yeast, already proven to be useful in the elucidation of protein interactors of several yeast and human integral membrane proteins [22,24,26], to search for physical interactors of Sho1p, and therefore find additional regulators of the Sho1p branch of the HOG pathway. Using the MYTH method, along with two other complementary PPI assays, we generated for the first time a high-quality Sho1p interactome, which includes 40 novel Sho1p interactors.…”

Section: Discussionmentioning

confidence: 99%

“…Cells were grown, lysed, immunoprecipitated, and Western blotted with rabbit anti-HA antibody as previously described [24]. …”

Section: Methodsmentioning

confidence: 99%

A Comprehensive Membrane Interactome Mapping of Sho1p Reveals Fps1p as a Novel Key Player in the Regulation of the HOG Pathway in S. cerevisiae

Lam

Snider

Rehal

et al. 2015

Journal of Molecular Biology

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Sho1p, an integral membrane protein, plays a vital role in the high-osmolarity glycerol (HOG) mitogen-activated protein kinase pathway in the yeast Saccharomyces cerevisiae. Activated under conditions of high osmotic stress, it interacts with other HOG pathway proteins to mediate cell signaling events, ensuring that yeast cells can adapt and remain viable. In an attempt to further understand how the function of Sho1p is regulated through its protein–protein interactions (PPIs), we identified 49 unique Sho1p PPIs through the use of membrane yeast two-hybrid (MYTH), an assay specifically suited to identify PPIs of full-length integral membrane proteins in their native membrane environment. Secondary validation by literature search, or two complementary PPI assays, confirmed 80% of these interactions, resulting in a high-quality Sho1p interactome. This set of putative PPIs included both previously characterized interactors, along with a large subset of interactors that have not been previously identified as binding to Sho1p. The SH3 domain of Sho1p was found to be important for binding to many of these interactors. One particular novel interactor of interest is the glycerol transporter Fps1p, which was shown to require the SH3 domain of Sho1p for binding via its N-terminal soluble regulatory domain. Furthermore, we found that Fps1p is involved in the positive regulation of Sho1p function and plays a role in the phosphorylation of the downstream kinase Hog1p. This study represents the largest membrane interactome analysis of Sho1p to date and complements past studies on the HOG pathway by increasing our understanding of Sho1p regulation.

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“…Paumi et al (2007) reported the identification of six potential partners of the yeast ABC transporter of the ABCC subclass, YCF1 (Yeast Cadmium Factor1). In a follow-up report, the same consortium provided the first yeast ABC interactome by analyzing 19 of all 22 yeast ABC transporters (Snider et al 2013). An unexpected outcome was the large number of functionally diverse interactors.…”

Section: Toward An Identification Of Abc Transporter Interactomes Durmentioning

confidence: 99%

A Critical View on ABC Transporters and Their Interacting Partners in Auxin Transport

Geisler

Aryal

Donato

et al. 2017

Plant and Cell Physiology

131

117

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Different subclasses of ATP-binding cassette (ABC) transporters have been implicated in the transport of native variants of the phytohormone auxin. Here, the putative, individual roles of key members belonging to the ABCB, ABCD and ABCG families, respectively, are highlighted and the knowledge of their assumed expression and transport routes is reviewed and compared with their mutant phenotypes. Protein-protein interactions between ABC transporters and regulatory components during auxin transport are summarized and their importance is critically discussed. There is a focus on the functional interaction between members of the ABCB family and the FKBP42, TWISTED DWARF1, acting as a chaperone during plasma membrane trafficking of ABCBs. Further, the mode and relevance of functional ABCB-PIN interactions is diagnostically re-evaluated. A new nomenclature describing precisely the most likely ABCB-PIN interaction scenarios is suggested. Finally, available tools for the detection and prediction of ABC transporter interactomes are summarized and the potential of future ABC transporter interactome maps is highlighted.

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Mapping the functional yeast ABC transporter interactome

Cited by 76 publications

References 48 publications

Unravelling glutathione conjugate catabolism in Saccharomyces cerevisiae: the role of glutathione/dipeptide transporters and vacuolar function in the release of volatile sulfur compounds 3-mercaptohexan-1-ol and 4-mercapto-4-methylpentan-2-one

Unravelling glutathione conjugate catabolism in Saccharomyces cerevisiae: the role of glutathione/dipeptide transporters and vacuolar function in the release of volatile sulfur compounds 3-mercaptohexan-1-ol and 4-mercapto-4-methylpentan-2-one

A Comprehensive Membrane Interactome Mapping of Sho1p Reveals Fps1p as a Novel Key Player in the Regulation of the HOG Pathway in S. cerevisiae

A Critical View on ABC Transporters and Their Interacting Partners in Auxin Transport

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