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Originally published In Press as doi:10.1074/jbc.M000676200 on April 20, 2000

J. Biol. Chem., Vol. 275, Issue 25, 19324-19333, June 23, 2000
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Isoforms of Kalirin, a Neuronal Dbl Family Member, Generated through Use of Different 5'- and 3'-Ends Along with an Internal Translational Initiation Site*

Richard C. Johnson, Peter Penzes, Betty A. Eipper, and Richard E. MainsDagger

From the Department of Neuroscience, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Kalirin is a neuron-specific GDP/GTP exchange factor for Rho subfamily GTP-binding proteins. The major Kalirin transcripts in adult rat brain were identified. Most include a Sec14p-like putative lipid-binding motif followed by nine spectrin-like repeats and a Dbl homology/pleckstrin homology (DH-PH) domain. Kalirin proteins with four different NH2 termini are generated through the use of five different 5'-ends; three of the proteins differ only at the extreme NH2 terminus, and one is truncated because translation is initiated at a methionine in the 5th spectrin repeat. Four different 3'-ends yield Kalirin proteins with additional functional domains. Kalirin-7 (7-kilobase pair mRNA) terminates with a PDZ-binding motif, which in Kalirin-8 is replaced by an SH3 domain. Kalirin-9 contains another pair of DH-PH and SH3 domains. Kalirin-12 additionally encodes a putative Ser/Thr protein kinase. Antisera specific for different COOH termini established Kalirin-7 as the most abundant in cortex, with significant amounts of Kalirin-9 and Kalirin-12; Kalirin-7 was less prevalent in cerebellum and olfactory bulb. Kalirin proteins lacking the Sec14p-like domain and first four spectrin-like repeats were much less prevalent. Form-specific antisera demonstrated that different forms of Kalirin were localized to distinct subcellular regions of cultured neurons. Members of the family of Kalirin proteins may subserve different functions at these different locations.

* This work was supported by National Institutes of Health Grant DK-32948.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Current address and to whom correspondence should be addressed: Dept. of Neuroscience, University of Connecticut Health Center, MC3401, 263 Farmington Ave., Farmington, CT 06030-3401. Tel.: 860-679-8894; Fax: 860-679-8766; E-mail: mains@nso.uchc.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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