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G? and G? Identity Dictate a G-Protein Heterotrimer Plasma Membrane Targeting.

ABSTRACT: Heterotrimeric G-proteins along with G-protein-coupled receptors (GPCRs) regulate many biochemical functions by relaying the information from the plasma membrane to the inside of the cell. The lipid modifications of G? and G? subunits, together with the charged regions on the membrane interaction surface, provide a peculiar pattern for various heterotrimeric complexes. In a previous study, we found that G?s and G?i3 prefer different types of membrane-anchor and subclass-specific lipid domains. In the present report, we examine the role of distinct G? subunits in the membrane localization and spatiotemporal dynamics of G?s and G?i3 heterotrimers. We characterized lateral diffusion and G-protein subunit interactions in living cells using fluorescence recovery after photobleaching (FRAP) microscopy and fluorescence resonance energy transfer (FRET) detected by fluorescence lifetime imaging microscopy (FLIM), respectively. The interaction of G? subunits with specific lipids was confirmed, and thus the modulation of heterotrimeric G-protein localization. However, the G? subunit also modulates trimer localization, and so the membrane distribution of heterotrimeric G-proteins is not dependent on G? only.

SUBMITTER: Mystek P

PROVIDER: S-EPMC6829862 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

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Gγ and Gα Identity Dictate a G-Protein Heterotrimer Plasma Membrane Targeting.

Mystek Paweł P Rysiewicz Beata B Gregrowicz Jan J Dziedzicka-Wasylewska Marta M Polit Agnieszka A

Cells 20191013 10

Heterotrimeric G-proteins along with G-protein-coupled receptors (GPCRs) regulate many biochemical functions by relaying the information from the plasma membrane to the inside of the cell. The lipid modifications of Gα and Gγ subunits, together with the charged regions on the membrane interaction surface, provide a peculiar pattern for various heterotrimeric complexes. In a previous study, we found that Gαs and Gαi<sub>3</sub> prefer different types of membrane-anchor and subclass-specific lipid ...[more]

PMID: 31614907

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Project description:Fungal Oligopeptide Transporters (Fot) Fot1, Fot2 and Fot3 have been found in Saccharomyces cerevisiae wine strains, but not in strains from other environments. In the S. cerevisiae wine strain EC1118, Fot1 and Fot2 are responsible for a broader range of oligopeptide utilization in comparison with strains not containing any Fot. This leads to better fermentation efficiency and an increased production of desirable organoleptic compounds in wine. Despite the benefits associated with Fot activity in S. cerevisiae within the wine environment, little is known about this family of transporters in yeast. The presence of Fot1, Fot2 and Fot3 in S. cerevisiae wine strains is due to horizontal gene transfer from the yeast Torulaspora microellipsoides, which harbors Fot2Tm, FotX and FotY proteins. Sequence analyses revealed that Fot family members have a high sequence identity in these yeast species. In this work, we aimed to further characterize the different Fot family members in terms of subcellular localization, gene expression in enological fermentation and substrate specificity. Using CRISPR/Cas9, we constructed S. cerevisiae wine strains containing each different Fot as the sole oligopeptide transporter to analyze their oligopeptide preferences by phenotype microarrays. The results of oligopeptide consumption show that Fot counterparts have different di-/tripeptide specificities, suggesting that punctual sequence divergence between FOT genes can be crucial for substrate recognition, binding and transport activity. FOT gene expression levels in different S. cerevisiae wine strains during enological fermentation, together with predicted binding motifs for transcriptional regulators in nitrogen metabolism, indicate that these transporters may be under the control of the Nitrogen Catabolite Repression (NCR) system. Finally, we demonstrated that Fot1 is located in the yeast plasma membrane. This work contributes to a better understanding of this family of oligopeptide transporters, which have demonstrated a key role in the utilization of oligopeptides by S. cerevisiae in enological fermentation.

Dataset Information

G? and G? Identity Dictate a G-Protein Heterotrimer Plasma Membrane Targeting.

Publications

Gγ and Gα Identity Dictate a G-Protein Heterotrimer Plasma Membrane Targeting.

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