Modular PH and C2 domains in membrane attachment and other functions.
The pleckstrin homology and C2 domains are modular protein structures involved in mediating intermolecular interactions. Although they represent distinct domains, there are several parallels regarding their function and type of interactions in which they participate. Both domains are stable structural entities that incorporate variable regions which, in different proteins, can be adapted to perform a specific function through binding to membrane phospholipids or specific protein ligands. A number of recent examples illustrate the function of some of these domains in regulated membrane attachment, with an important role in many cellular signalling pathways.
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CRC Centre for Cell and Molecular Biology, Chester Beatty Laboratories, London, UK. matilda@icr.ac.uk
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D001665:Binding Sites; D001798:Blood Proteins / Q000737:chemistry* / Q000378:metabolism; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism / Q000502:physiology*; D010750:Phosphoproteins; D011493:Protein Kinase C / Q000737:chemistry* / Q000378:metabolism
D001798:Blood Proteins; D008563:Membrane Lipids; D008565:Membrane Proteins; D010446:Peptide Fragments; D010750:Phosphoproteins; C039077:platelet protein P47; D011493:Protein Kinase C