Sec14-like phosphatidylinositol-transfer proteins and diversification of phosphoinositide signalling outcomes. Academic Article

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.

authors

• Bankaitis, Vytas

published proceedings

• Biochem Soc Trans

altmetric score

• 0.5

author list (cited authors)

• Tripathi, A., Nile, A. H., & Bankaitis, V. A.

citation count

• 10

complete list of authors

• Tripathi, Ashutosh||Nile, Aaron H||Bankaitis, Vytas A

publication date

• October 2014

publisher

• Portland Press  Publisher

published in

• Biochemical Society Transactions  Journal

keywords

• Animals
• Binding Sites
• Biological Transport
• Cell Cycle Proteins
• Chromosomal Proteins, Non-Histone
• Humans
• Hydrophobic And Hydrophilic Interactions
• Ligands
• Models, Biological
• Phosphatidylcholines
• Phosphatidylinositols
• Phospholipid Transfer Proteins
• Phosphotransferases (Alcohol Group Acceptor)
• Protein Conformation
• Saccharomyces Cerevisiae Proteins
• Second Messenger Systems

PubMed Central ID

• 25233419

Digital Object Identifier (DOI)

• 10.1042/BST20140187

start page

• 1383

end page

• 1388

volume

• 42

issue

• 5

URL

• http://dx.doi.org/10.1042/bst20140187