Pleckstrin homology domains: two halves make a hole?
In 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.
Lemmon
Mark A
MA
Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA. mlemmon@mail.med.upenn.edu
D000818:Animals; D001665:Binding Sites / Q000502:physiology; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism; D007473:Ion Channels / Q000737:chemistry / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D010716:Phosphatidylinositols / Q000378:metabolism; D051966:Phospholipase C gamma; D011485:Protein Binding / Q000502:physiology*; D017434:Protein Structure, Tertiary / Q000502:physiology; D050052:TRPC Cation Channels; D010738:Type C Phospholipases / Q000737:chemistry / Q000378:metabolism*
D047908:Intracellular Signaling Peptides and Proteins; D007473:Ion Channels; D008565:Membrane Proteins; C435927:PLEKHA1 protein, human; D010716:Phosphatidylinositols; D050052:TRPC Cation Channels; C104603:TRPC3 cation channel; D010738:Type C Phospholipases; D051966:Phospholipase C gamma