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Pleckstrin homology domains: two halves make a hole?Lemmon MACell 2005[Mar]; 120 (5): 574-6In a recent issue of Nature, van Rossum et al. report binding of a "split" pleckstrin homology (PH) domain from phospholipase C-gamma(1) to the TRPC3 ion channel. Through sequence analyses and in vitro studies, they suggest a novel mode of protein-protein interaction in which two PH domain fragments in distinct proteins associate to form an "intermolecular" PH domain that binds inositol phospholipids and is required for ion channel location and function.|Animals[MESH]|Binding Sites/physiology[MESH]|Humans[MESH]|Intracellular Signaling Peptides and Proteins/metabolism[MESH]|Ion Channels/chemistry/*metabolism[MESH]|Membrane Proteins/metabolism[MESH]|Phosphatidylinositols/metabolism[MESH]|Phospholipase C gamma[MESH]|Protein Binding/*physiology[MESH]|Protein Structure, Tertiary/physiology[MESH]|TRPC Cation Channels[MESH]|Type C Phospholipases/chemistry/*metabolism[MESH] |
