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Specificity in pleckstrin homology (PH) domain membrane targeting: a role for a phosphoinositide-protein co-operative mechanism Maffucci T; Falasca MFEBS Lett 2001[Oct]; 506 (3): 173-9Pleckstrin homology (PH) domains are protein modules found in proteins involved in many cellular processes. The majority of PH domain-containing proteins require membrane association for their function. It has been shown that most PH domains interact directly with the cell membrane by binding to phosphoinositides with a broad range of specificity and affinity. While a highly specific binding of the PH domain to a phosphoinositide can be necessary and sufficient for the correct recruitment of the host protein to the membrane, a weaker and less specific interaction may be necessary but not sufficient, thus probably requiring alternative, co-operative mechanisms.|Blood Proteins/*chemistry[MESH]|Isoenzymes/chemistry/metabolism[MESH]|Models, Molecular[MESH]|Phosphatidylinositols/*metabolism[MESH]|Phospholipase C delta[MESH]|Phosphoproteins/*chemistry[MESH]|Protein Binding[MESH]|Proteins/*metabolism[MESH]|Type C Phospholipases/chemistry/metabolism[MESH] |
