Article
- The EMBO Journal (2005) 24, 1931 - 1941
- doi:10.1038/sj.emboj.7600672
Published online: 5 May 2005
Subject Categories:
The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth
Helena Santos-Rosa1,a, Joanne Leung2,a, Neil Grimsey2, Sew Peak-Chew3 and Symeon Siniossoglou2,3
- WellcomeTrust/Cancer Research UK Gurdon Institute, Cambridge, UK
- Cambridge Institute for Medical Research (CIMR), University of Cambridge, Wellcome Trust/MRC Building, Cambridge, UK
- MRC Laboratory of Molecular Biology, Cambridge, UK
Correspondence to:
Symeon Siniossoglou, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, University of Cambridge, Hills Road, Cambridge CB2 2XY, UK. Tel.: +44 1223 762641/+44 1223 331960; Fax: +44 1223 762640; E-mail: ss560@cam.ac.uk
aThese authors contributed equally to this work
Received 21 January 2005; Accepted 13 April 2005
Abstract
Remodelling of the nuclear membrane is essential for the dynamic changes of nuclear architecture at different stages of the cell cycle and during cell differentiation. The molecular mechanism underlying the regulation of nuclear membrane biogenesis is not known. Here we show that Smp2, the yeast homologue of mammalian lipin, is a key regulator of nuclear membrane growth during the cell cycle. Smp2 is phosphorylated by Cdc28/Cdk1 and dephosphorylated by a nuclear/endoplasmic reticulum (ER) membrane–localized CPD phosphatase complex consisting of Nem1 and Spo7. Loss of either SMP2 or its dephosphorylated form causes transcriptional upregulation of key enzymes involved in lipid biosynthesis concurrent with a massive expansion of the nucleus. Conversely, constitutive dephosphorylation of Smp2 inhibits cell division. We show that Smp2 associates with the promoters of phospholipid biosynthetic enzymes in a Nem1–Spo7-dependent manner. Our data suggest that Smp2 is a critical factor in coordinating phospholipid biosynthesis at the nuclear/ER membrane with nuclear growth during the cell cycle.
Keywords:
- lipin,
- nuclear membrane,
- phospholipid biosynthesis,
- Smp2
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