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J. Biol. Chem., Vol. 276, Issue 39, 36647-36651, September 28, 2001
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From the We have reported that a novel c-Myc-binding
protein, AMY-1 (associate of Myc-1), stimulated
the transcription activity of c-Myc. To access the molecular function
of AMY-1, a two-hybrid screening of cDNAs encoding AMY-1-binding
proteins was carried out with AMY-1 as a bait using a human HeLa
cDNA library, and a clone encoding cAMP-dependent
protein kinase anchor protein 149 (AKAP149), was obtained. AMY-1 was
found to bind in vitro and in vivo to the
regulatory subunit II binding region of AKAP149 and S-AKAP84, a
splicing variant of AKAP149 expressed in the testis. AMY-1 was
expressed postmeiotically in the testis, as S-AKAP84 was expressed.
Furthermore, S-AKAP84 and regulatory subunit II, a regulatory
subunit of cAMP-dependent protein kinase, made a ternary
complex in cells, and AMY-1 was localized in the mitochondria of HeLa
and sperm in association with AKAP149 and S-AKAP84, respectively. These
results suggest that AMY-1 plays a role in spermatogenesis.
AMY-1, a c-Myc-binding Protein, Is Localized in the
Mitochondria of Sperm by Association with S-AKAP84, an Anchor
Protein of cAMP-dependent Protein Kinase*
§,,§,§
Graduate School of Pharmaceutical Sciences,
¶ College of Medical Technology, Hokkaido University, Kita-ku,
Sapporo 060-0812 and § CREST, Japan Science and Technology
Corporation, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan
*
This work was supported by grants-in-aid from the Ministry
of Education, Science, Culture and Sport of Japan.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.
To whom correspondence should be addressed: Graduate School of
Pharmaceutical Sciences, Hokkaido University, Kita 12, Nishi 6, Kita-ku, Sapporo 060-0812, Japan. Tel.: 81-11-706-3745; Fax: 81-11-706-4988; E-mail: hiro@pharm.hokudai.ac.jp.
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