Phosphoproteomic Analysis across the Yeast Life Cycle Reveals Control of Fatty Acyl Chain Length by Phosphorylation of the Fatty Acid Synthase Complex

Martínez-Montañés, Fernando; Casanovas, Albert; Sprenger, Richard R.; Topolska, Magdalena; Marshall, David L.; Moreno-Torres, Marta; Poad, Berwyck L. J.; Blanksby, Stephen J.; Hermansson, Martin; Jensen, Ole N.; Ejsing, Christer S.

doi:10.1016/j.celrep.2020.108024

Cited by 16 publications

(16 citation statements)

References 89 publications

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“…3). In yeast, phosphorylation of Ser1140, Ser1640 and Ser1827 are associated with increased 18:0-CoA production 231 , while in a breast cancer cell line, FAS is phosphorylated at Tyr66 when in complex with human epidermal growth factor receptor 2 (reF. 232 ).…”

Section: Regulation and Structurementioning

confidence: 99%

Lipogenesis inhibitors: therapeutic opportunities and challenges

Batchuluun

Pinkosky

Steinberg

2022

Nat Rev Drug Discov

214

135

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Section: Regulation and Structurementioning

confidence: 99%

Lipogenesis inhibitors: therapeutic opportunities and challenges

Batchuluun

Pinkosky

Steinberg

2022

Nat Rev Drug Discov

214

135

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“…cerevisiae, where over 4500 proteins were quantified across 10 time points, and the set of Hap2-regulated proteins was identified . Recently, an investigation reported phosphorylation dynamics during the diauxic shift at four time points using label-free quantitation and demonstrated regulation of the fatty acyl chain length by phosphorylation …”

Section: Introductionmentioning

confidence: 99%

Categorization of Phosphorylation Site Behavior during the Diauxic Shift in Saccharomyces cerevisiae

2021

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Protein phosphorylation has long been recognized as an essential regulator of protein activity, structure, complex formation, and subcellular localization among other cellular mechanisms. However, interpretation of the changes in protein phosphorylation is difficult. To address this difficulty, we measured protein and phosphorylation site changes across 11 points of a time course and developed a method for categorizing phosphorylation site behavior relative to protein level changes using the diauxic shift in yeast as a model and TMT11 sample multiplexing. We classified quantified proteins into behavioral categories that reflected differences in kinase activity, protein complex structure, and growth and metabolic pathway regulation across different phases of the diauxic shift. These data also provide a valuable resource for the study of fermentative versus respiratory growth and set a new benchmark for temporal quantitative proteomics and phosphoproteomics for the diauxic shift in Saccharomyces cerevisiae. Data are available via ProteomeXchange with identifier PXD022741.

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“…Yeast strains used in this study are isogenic to either BY4741 (MATa ura3Δ0 his3Δ1 leu2Δ0 met15Δ0) or BY4742 (MATα ura3Δ0 his3Δ1 leu2Δ0 lys2Δ0) and are listed in Table S1. Tagging of proteins, replacement of promoters, and individual gene deletions were performed by standard PCR-based homologous recombination (Longtine et al, 1998;Janke et al, 2004). Point mutations, protein tagging, replacement of regions within the ORF for chimeric constructs, partial gene deletions, and full gene deletions were performed by CRISPR-based gene editing (adapted from Laughery et al, 2015).…”

Section: Yeast Strains and Plasmidsmentioning

confidence: 99%

Pex30-like proteins function as adaptors at distinct ER membrane contact sites

Ferreira

Carvalho

2021

Journal of Cell Biology

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Membrane lipids and proteins synthesized in the ER are used for de novo assembly of organelles, such as lipid droplets and peroxisomes. After assembly, the growth of these organelles is supported by ER-derived lipids transferred at membrane contact sites (MCSs). How ER sites for organelle biogenesis and lipid transfer are established and regulated is unclear. Here, we investigate how the ER membrane protein Pex30 and its family members Pex28, Pex29, Pex31, and Pex32 target and function at multiple MCSs. We show that different Pex30 complexes function at distinct ER domains and MCSs. Pex30 targets ER–peroxisome MCSs when bound to Pex28 and Pex32, organizes the nuclear–vacuolar junction when bound to Pex29, and promotes the biogenesis of lipid droplets independently of other family members. Importantly, the reticulon homology domain (RHD) mediates the assembly of the various Pex30 complexes. Given the role of RHD in membrane shaping, our findings offer a mechanistic link between MCS and regulation of membrane curvature.

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Phosphoproteomic Analysis across the Yeast Life Cycle Reveals Control of Fatty Acyl Chain Length by Phosphorylation of the Fatty Acid Synthase Complex

Cited by 16 publications

References 89 publications

Lipogenesis inhibitors: therapeutic opportunities and challenges

Lipogenesis inhibitors: therapeutic opportunities and challenges

Categorization of Phosphorylation Site Behavior during the Diauxic Shift in Saccharomyces cerevisiae

Pex30-like proteins function as adaptors at distinct ER membrane contact sites

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