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*

Abstract

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.

  • Abbreviations:
    PKA
    cAMP-dependent protein kinase
    RII
    regulatory subunit II of A-kinase
    GST
    glutathioneS-transferase
    AMCA
    aminomethyl coumarin acetic acid
    GALAD
    GAL4 activation domain
    • Received May 1, 2001.
    • Revision received July 23, 2001.
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    This Article

    1. The Journal of Biological Chemistry 276, 36647-36651.
    1. All Versions of this Article:
      1. M103885200v1
      2. 276/39/36647 (most recent)

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