The pleckstrin homology domain: an intriguing multifunctional protein module.
Pleckstrin homology (PH) domains are a family of compact protein modules defined by sequences of roughly 100 amino acids. These domains are common in vertebrate, Drosophila, C. elegans and yeast proteins, suggesting an early origin and fundamental importance to eukaryotic biology. Many enzymes which have important regulatory functions contain PH domains, and mutant forms of several such proteins are implicated in oncogenesis and developmental disorders. Numerous recent studies show that PH domains bind various proteins and inositolphosphates. Here I discuss PH domains in detail and conclude that they form a versatile family of membrane binding and protein localization modules.
Shaw
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University of Florida College of Medicine, Department of Neuroscience, Gainesville 32610, USA. SHAW@NEOCORTEX.HEALTH.UFL.EDU
D000361:Agammaglobulinemia / Q000235:genetics; D000818:Animals; D001798:Blood Proteins / Q000737:chemistry*; D034281:Dynamins; D019143:Evolution, Molecular; D020558:GTP Phosphohydrolases / Q000737:chemistry; D006801:Humans; D008958:Models, Molecular; D005810:Multigene Family; D010750:Phosphoproteins; D011485:Protein Binding; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D013049:Spectrin / Q000737:chemistry; D018909:src Homology Domains
D001798:Blood Proteins; D010750:Phosphoproteins; C039077:platelet protein P47; D013049:Spectrin; D020558:GTP Phosphohydrolases; D034281:Dynamins