Specificity in pleckstrin homology (PH) domain membrane targeting: a role for a phosphoinositide-protein co-operative mechanism.
Pleckstrin 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.
Maffucci
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T
The Sackler Institute, University College London, 5 University Street, WC1E 6JJ, London, UK.
Falasca
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M
D001798:Blood Proteins / Q000737:chemistry*; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D010716:Phosphatidylinositols / Q000378:metabolism*; D054803:Phospholipase C delta; D010750:Phosphoproteins / Q000737:chemistry*; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D010738:Type C Phospholipases / Q000737:chemistry / Q000378:metabolism
D001798:Blood Proteins; D007527:Isoenzymes; D010716:Phosphatidylinositols; D010750:Phosphoproteins; D011506:Proteins; C039077:platelet protein P47; D010738:Type C Phospholipases; D054803:Phospholipase C delta