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J. Biol. Chem., Vol. 283, Issue 17, 11743-11751, April 25, 2008
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From the Howard Hughes Medical Institute and the Department of Chemistry and Biochemistry, and Department of Pharmacology, University of California, San Diego, La Jolla, California 92093
DAKAP1 (AKAP121, S-AKAP84), a dual specificity PKA scaffold protein, exists in several forms designated as a, b, c, and d. Whether DAKAP1 targets to endoplasmic reticulum (ER) or mitochondria depends on the presence of the N-terminal 33 amino acids (N1), and these N-terminal variants are generated by either alternative splicing and/or differential initiation of translation. The mitochondrial targeting motif, which is localized between residues 49 and 63, is comprised of a hydrophobic helix followed by positive charges (
Ma, Y., and Taylor, S. (2002) J. Biol. Chem. 277, 27328-27336
Received for publication, December 26, 2007 , and in revised form, February 14, 2008.
* This work was partially supported by National Institutes of Health Grant DK54441 (to S. T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains a supplemental figure.
1 To whom correspondence should be addressed: Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, and Department of Pharmacology, University of California, San Diego, 9500 Gilman Dr., MC 0654, La Jolla, CA 92093. Tel.: 858-534-3677; Fax: 858-534-8193; E-mail: staylor{at}ucsd.edu.
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