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Regulation of lipid droplet and membrane biogenesis by the
acidic tail of the phosphatidate phosphatase Pah1p  Molecular
Biology of the Cell  2013;24(13):2124-2133. Binding and
dephosphorylation of the yeast lipin Pah1p by its phosphatase
Nem1p-Spo7p is essential for its membrane targeting and is
mediated by a C-terminal acidic stretch on Pah1p. This results
in the recruitment of Pah1p to the vicinity of lipid droplets,
where it controls triglyceride and droplet biogenesis in an
acidic tail–dependent manner. Lipins are evolutionarily
conserved phosphatidate phosphatases that perform key functions
in phospholipid, triglyceride, and membrane biogenesis.
Translocation of lipins on membranes requires their
dephosphorylation by the Nem1p-Spo7p transmembrane phosphatase
complex through a poorly understood mechanism. Here we identify
the carboxy-terminal acidic tail of the yeast lipin Pah1p as