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Papers In Press, published online ahead of print November 20, 2002
J. Biol. Chem, 10.1074/jbc.M208579200
Submitted on August 21, 2002
Revised on November 20, 2002
Accepted on November 20, 2002

Elucidation of the interaction of calmodulin with the IQ motifs of IQGAP1

Zhigang Li and David B. Sacks

Department of Pathology, Brigham and Women's Hospital, Boston, Massachusetts 02115

Corresponding Author: dsacks{at}rics.bwh.harvard.edu

Calmodulin regulates the function of numerous proteins by binding to short regions on the target molecule. IQ motifs, which are found in over 100 human proteins, appear in tandem repeats and bind calmodulin in the absence of Ca2+. One of these IQ-containing proteins, IQGAP1, interacts with several targets - including Cdc42, beta -catenin, E-cadherin and actin - in a calmodulin-regulated manner. In order to elucidate the molecular mechanism by which apocalmodulin and Ca2+/calmodulin differentially regulate IQGAP1, a series of constructs of IQGAP1 with selected point mutations of the four tandem IQ motifs were generated. Mutating the basic charged arginine residues in all four IQ motifs abrogated binding of IQGAP1 to apocalmodulin, but had no effect on its interaction with Ca2+/calmodulin. Analysis of IQGAP1 constructs with point mutations in single, double or triple IQ motifs revealed that apocalmodulin bound only to IQ3 and IQ4. By contrast to the arginine mutant constructs, mutation of selected hydrophobic residues in the IQ motifs produced an IQGAP1 protein incapable of binding either apocalmodulin or Ca2+/calmodulin. These results, which differ from the conventional model of Ca2+-independent binding of calmodulin to IQ motifs, provide insight into the complexity of the molecular interactions between calmodulin and IQ motifs.


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