Abstract
The physiological functions of phosphatidylinositol (PtdIns)-transfer proteins (PITPs)/phosphatidylcholine (PtdCho)-transfer proteins are poorly characterized, even though these proteins are conserved throughout the eukaryotic kingdom. Much of the progress in elucidating PITP functions has come from exploitation of genetically tractable model organisms, but the mechanisms for how PITPs execute their biological activities remain unclear. Structural and molecular dynamics approaches are filling in the details for how these proteins actually work as molecules. In the present paper, we discuss our recent work with Sec14-like PITPs and describe how PITPs integrate diverse territories of the lipid metabolome with phosphoinositide signalling.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Binding Sites
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Biological Transport
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Cell Cycle Proteins / chemistry
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Cell Cycle Proteins / metabolism*
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Chromosomal Proteins, Non-Histone / chemistry
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Chromosomal Proteins, Non-Histone / metabolism*
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Humans
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Hydrophobic and Hydrophilic Interactions
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Ligands
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Models, Biological*
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Phosphatidylcholines / chemistry
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Phosphatidylcholines / metabolism*
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Phosphatidylinositols / chemistry
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Phosphatidylinositols / metabolism*
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Phospholipid Transfer Proteins / chemistry
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Phospholipid Transfer Proteins / metabolism*
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Phosphotransferases (Alcohol Group Acceptor) / chemistry
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Phosphotransferases (Alcohol Group Acceptor) / metabolism
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Protein Conformation
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / metabolism*
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Second Messenger Systems*
Substances
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Cell Cycle Proteins
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Chromosomal Proteins, Non-Histone
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Ligands
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Phosphatidylcholines
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Phosphatidylinositols
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Phospholipid Transfer Proteins
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SEC14 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Sfh1 protein, S cerevisiae
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Phosphotransferases (Alcohol Group Acceptor)