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J. Biochem, 1997, Vol. 122, No. 3 494-497
© 1997 Japanese Biochemical Society

other

Perinuclear Membrane Localization of {alpha}KAP, a Protein Produced from a Gene within the Gene of Calmodulin-Dependent Protein Kinase II{alpha}1

Masayuki Takeuchi and Hitoshi Fujisawa2

Department of Biochemistry, Asahikawa Medical College Asahikawa, Hokkaido 078

2To whom correspondence should be addressed. E-mail: fujisawa{at}asahikawa-med.ac.jp

{alpha}KAP is a protein produced from a gene within the gene of the {alpha} isoform of calmodulin-dependent protein kinase II (CaM-kinase II{alpha}). It consists of the association domain of CaM-kinase II{alpha} and a highly hydrophobic amino-terminal stretch consisting of 25 amino acids which is absent from CaM-kinase II{alpha}. We previously demonstrated that {alpha}KAP is an integral membrane protein by subcellular fractionation analysis [Sugai, R., Takeuchi, M., Okuno, S., and Fujisawa, H. (1996) J. Biochem. 120, 773–779], but the exact subcellular localization of {alpha}KAP was not well understood. Here we demonstrate that {alpha}KAP is localized on the nuclear membrane of COS-7 cells transiently expressing {alpha}KAP. The nuclear membrane and perinuclear small vesicles were immunostained with an antibody against a synthetic peptide corresponding to the carboxyl-terminal 15 amino acids of {alpha}KAP. In contrast to the intact {alpha}KAP, the mutant {alpha}KAP, from which the hydrophobic amino-terminal segment had been deleted, accumulated within nuclei. Thus, {alpha}KAP may function as an anchoring protein for CaM-kinase II and/or other proteins in the perinuclear membrane.

1This work was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan, the Byotai Taisha Research Foundation, the Uehara Memorial Foundation, and the Mitsubishi Foundation.


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