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Biochem Biophys Res Commun. 2007 Dec 28;364(4):870-6. Epub 2007 Oct 24.

The yeast VAP homolog Scs2p has a phosphoinositide-binding ability that is correlated with its activity.

Author information

1
Department of Biological Sciences, Faculty of Science, Nara Women's University, Nara 630-8506, Japan. kagiwada@cc.nara-wu.ac.jp

Erratum in

  • Biochem Biophys Res Commun. 2009 Jun 26;384(2):270.

Abstract

The yeast VAMP-associated protein (VAP) homolog Scs2p is an endoplasmic reticulum (ER)/nuclear membrane protein that binds to an FFAT (diphenylalanine in an acidic tract) motif found in various lipid-metabolic proteins, including Opi1p, a negative regulator of phospholipid biosynthesis. Here, we show that Scs2p is a novel phosphoinositide-binding protein that can bind to phosphatidylinositol monophosphates and bisphosphates in vitro. The phosphoinositide-binding domain was assigned to the N-terminal major sperm protein (MSP) domain which also contains the FFAT-binding domain. When several lysine residues in the MSP domain were substituted for alanine, the resulting mutant Scs2 proteins lost the phosphoinositide-binding ability and failed to complement the inositol auxotrophy of an scs2 deletion strain. However, the mutant proteins still localized in the ER/nuclear membrane, in a similar manner to wild-type Scs2p. These results suggest the possibility that Scs2p activity is regulated by phosphoinositides to coordinate phospholipid biosynthesis in response to changes in phospholipid composition.

PMID:
17963691
DOI:
10.1016/j.bbrc.2007.10.079
[Indexed for MEDLINE]

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