Abstract
The phosphatidylinositol 4,5-bisphosphate (PtdIns P 2)-regulated actin-binding protein gelsolin and most phosphoinositide-specific phospholipases C (PLCs) comprise a basic amino acid motif ((K/R)xxxKxK(K/R); x denotes any amino acid) which was previously suggested to represent a PtdIns P 2-binding site commonly present in these proteins. We have challenged this hypothesis for PLC β 2 by replacing one or several residues of this motif (KILIKNKK; residues 457–464) and examining the functional consequences of these alterations. The results show that the integrity of the basic motif is important for PtdIns P 2 hydrolysis by PLC β 2. Replacement of lysines 463 or 461 by arginine led to reduction or complete loss, respectively, of enzyme activity. The results provide further support to the concept that the function of the basic motif within the various PLCs is to bind the enzyme substrate PtdIns P 2.
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