Amphipathic Helices as Mediators of the Membrane Interaction of Amphitropic Proteins, and as Modulators of Bilayer Physical Properties

Author(s): Rosemary B. Cornell, Svetla G. Taneva

Journal Name: Current Protein & Peptide Science

Volume 7 , Issue 6 , 2006

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The amphipathic helix (AH) motif is used by a subset of amphitropic proteins to accomplish reversible and controlled association with the interfacial zone of membranes. Functioning as more than mere membrane anchoring domains, amphipathic helices can serve as autoinhibitory domains to suppress the protein activity in its soluble form, and as sensors or modulators of membrane curvature. Thus amphipathic helices can both respond to and modulate membrane physical properties. These and other features are illustrated by the behavior of CTP: phosphocholine cytidylyltransferase (CCT), a key regulatory enzyme in PC synthesis. A comparison of the physico-chemical features of CCTs AH motif and 10 others reveals similarities and several differences. The importance of these parameters to the particulars of the membrane interaction and to functional consequences requires more systematic exploration. The membrane partitioning of amphitropic proteins with AH motifs can be regulated by various strategies including changes in membrane lipid composition, phosphorylation, ligand-induced conformational changes, and membrane curvature. Several amphitropic proteins that control budding or tubule formation in cells have AH motifs. The insertion of the hydrophobic face of these amphipathic helices generates an asymmetry in the lateral pressure of the two leaflets resulting in an induction of positive curvature. Curvature induction or stabilization may be a universal property of AHA proteins, not just those involved in budding, but this possibility requires further demonstration.

Keywords: AH motifs, phosphocholine cytidylyltransferase (CCT), Surface Potential, ENTH domains, Membrane Lipid

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Article Details

Year: 2006
Page: [539 - 552]
Pages: 14
DOI: 10.2174/138920306779025675
Price: $65

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PDF: 14