Phosphorylation-mediated regulation of the Nem1-Spo7/Pah1 phosphatase cascade in yeast lipid synthesis

TY - JOUR

T1 - Phosphorylation-mediated regulation of the Nem1-Spo7/Pah1 phosphatase cascade in yeast lipid synthesis

AU - Khondker, Shoily

AU - Han, Gil Soo

AU - Carman, George M.

N1 - Funding Information: This work was supported, in whole or in part, by United States Public Health Service Grants GM028140 , GM050679 , and GM136128 from the National Institutes of Health . The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. Publisher Copyright: © 2022 Elsevier Ltd

PY - 2022/5

Y1 - 2022/5

N2 - The PAH1-encoded phosphatidate phosphatase, which catalyzes the dephosphorylation of phosphatidate to produce diacylglycerol, controls the divergence of phosphatidate into triacylglycerol synthesis and phospholipid synthesis. Pah1 is inactive in the cytosol as a phosphorylated form and becomes active on the nuclear/endoplasmic reticulum membrane as a dephosphorylated form by the Nem1-Spo7 protein phosphatase complex. The phosphorylation of Pah1 by protein kinases, which include casein kinases I and II, Pho85-Pho80, Cdc28-cyclin B, and protein kinases A and B, controls its cellular location, catalytic activity, and susceptibility to proteasomal degradation. Nem1 (catalytic subunit) and Spo7 (regulatory subunit), which form a protein phosphatase complex catalyzing the dephosphorylation of Pah1 for its activation, are phosphorylated by protein kinases A and C. In this review, we discuss the functions and interrelationships of the protein kinases in the control of the Nem1-Spo7/Pah1 phosphatase cascade and lipid synthesis.

AB - The PAH1-encoded phosphatidate phosphatase, which catalyzes the dephosphorylation of phosphatidate to produce diacylglycerol, controls the divergence of phosphatidate into triacylglycerol synthesis and phospholipid synthesis. Pah1 is inactive in the cytosol as a phosphorylated form and becomes active on the nuclear/endoplasmic reticulum membrane as a dephosphorylated form by the Nem1-Spo7 protein phosphatase complex. The phosphorylation of Pah1 by protein kinases, which include casein kinases I and II, Pho85-Pho80, Cdc28-cyclin B, and protein kinases A and B, controls its cellular location, catalytic activity, and susceptibility to proteasomal degradation. Nem1 (catalytic subunit) and Spo7 (regulatory subunit), which form a protein phosphatase complex catalyzing the dephosphorylation of Pah1 for its activation, are phosphorylated by protein kinases A and C. In this review, we discuss the functions and interrelationships of the protein kinases in the control of the Nem1-Spo7/Pah1 phosphatase cascade and lipid synthesis.

KW - Diacylglycerol

KW - Nem1-Spo7 protein phosphatase

KW - Pah1 PA phosphatase

KW - Phosphatidic acid

KW - Phospholipid

KW - Protein kinase

KW - Triacylglycerol

KW - Yeast

UR - http://www.scopus.com/inward/record.url?scp=85125232253&partnerID=8YFLogxK

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U2 - https://doi.org/10.1016/j.jbior.2022.100889

DO - https://doi.org/10.1016/j.jbior.2022.100889

M3 - Article

VL - 84

JO - Advances in Biological Regulation

JF - Advances in Biological Regulation

SN - 2212-4926

M1 - 100889

ER -