Reference: Roelants FM, et al. (2017) The TORC2-Dependent Signaling Network in the Yeast Saccharomyces cerevisiae. Biomolecules 7(3)

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Abstract


To grow, eukaryotic cells must expand by inserting glycerolipids, sphingolipids, sterols, and proteins into their plasma membrane, and maintain the proper levels and bilayer distribution. A fungal cell must coordinate growth with enlargement of its cell wall. In Saccharomyces cerevisiae, a plasma membrane-localized protein kinase complex, Target of Rapamicin (TOR) complex-2 (TORC2) (mammalian ortholog is mTORC2), serves as a sensor and masterregulator of these plasma membrane- and cell wall-associated events by directly phosphorylating and thereby stimulating the activity of two types of effector protein kinases: YPK1 (mammalian ortholog is SGK1), along with a paralog (YPK2); and, PKC1 (mammalian ortholog is PKN2/PRK2). YPK1 is a central regulator of pathways and processes required for plasma membrane lipid and protein homeostasis, and requires phosphorylation on its T-loop by eisosome-associated protein kinase PKH1 (mammalian ortholog is PDK1) and a paralog (PKH2). For cell survival under various stresses, YPK1 function requires TORC2-mediated phosphorylation at multiple sites near its C terminus. PKC1 controls diverse processes, especially cell wall synthesis and integrity. PKC1 is also regulated by PKH1- and TORC2-dependent phosphorylation, but, in addition, by interaction with Rho1-GTP and lipids phosphatidylserine (PtdSer) and diacylglycerol (DAG). We also describe here what is currently known about the downstream substrates modulated by YPK1-mediated and PKC1-mediated phosphorylation.

Reference Type
Journal Article | Review
Authors
Roelants FM, Leskoske KL, Martinez Marshall MN, Locke MN, Thorner J
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