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J Biol Chem, Vol. 274, Issue 12, 7689-7694, March 19, 1999
,
From the Neurogranin is a neural-specific, calmodulin
(CaM)-binding protein that is phosphorylated by protein kinase C (PKC)
within its IQ domain at serine 36. Since CaM binds to neurogranin
through the IQ domain, PKC phosphorylation and CaM binding are mutually exclusive. Consequently, we hypothesize that neurogranin may function to concentrate CaM at specific sites in neurons and release free CaM in
response to increased Ca2+ and PKC activation.
However, it has not been established that neurogranin interacts with
CaM in vivo. In this study, we examined this question using
yeast two-hybrid methodology. We also searched for additional proteins
that might interact with neurogranin by screening brain cDNA
libraries. Our data illustrate that CaM binds to neurogranin in
vivo and that CaM is the only neurogranin-interacting protein
isolated from brain cDNA libraries. Single amino acid mutagenesis
indicated that residues within the IQ domain are important for CaM
binding to neurogranin in vivo. The Ile-33 Department of Pharmacology, University of
Washington, Seattle, Washington 98195 and ¶ INSERM U 244, DBMS/BRCE, CENG, 17 rue des Martyrs,
38054 Grenoble Cedex 9, France
Gln point mutant completely inhibited and Arg-38 Gln and Ser-36 Asp point
mutants reduced neurogranin/CaM interactions. These data demonstrate
that CaM is the major protein that interacts with neurogranin in
vivo and support the hypothesis that phosphorylation of
neurogranin at Ser-36 regulates its binding to CaM.
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