A-kinase anchor protein 84/121 are targeted to mitochondria and mitotic spindles by overlapping amino-terminal motifs (Articolo in rivista)

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  • A-kinase anchor protein 84/121 are targeted to mitochondria and mitotic spindles by overlapping amino-terminal motifs (Articolo in rivista) (literal)
Anno
  • 2002-01-01T00:00:00+01:00 (literal)
Alternative label
  • Cardone L., De Cristofaro T., Affaitati A., Garbi C., Ginsberg M. D., Saviano M., Varrone S., Rubin C. S., Gottesman M E., Avvedimento E V., Feliciello A. (2002)
    A-kinase anchor protein 84/121 are targeted to mitochondria and mitotic spindles by overlapping amino-terminal motifs
    in Journal of Molecular Biology
    (literal)
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  • Cardone L., De Cristofaro T., Affaitati A., Garbi C., Ginsberg M. D., Saviano M., Varrone S., Rubin C. S., Gottesman M E., Avvedimento E V., Feliciello A. (literal)
Pagina inizio
  • 663 (literal)
Pagina fine
  • 675 (literal)
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  • Impact Factor = 8,817; Interdisciplinariet√† del prodotto: The Authors belong to different scientific areas, sectors and Istitutions. The paper was in collaboration with International Institutions. (literal)
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  • 320 (literal)
Rivista
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  • Lavoro su rivista scientifica che riporta dati sulla regione di proteina che lega in modo specifico il mitocondrio. (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • 1Dipartimento di Biologia e Patologia Molecolare e Cellulare and BioGem Consortium and Instituto di Endocrinologia ed Oncologia Sperimentale CNR, Universita Federico II, via S. Pansini 5, 80131 Naples, Italy; 2 Institute of Cancer Research, Columbia University New York USA; 3 Centro Studi Biocristallografia CNR, via Mezzocannone 6, 80144 Napoli; 4 Department of Molecular Pharmacology Atran Laboratories Albert Einstein College of Medicine, Bronx New York USA (literal)
Titolo
  • A-kinase anchor protein 84/121 are targeted to mitochondria and mitotic spindles by overlapping amino-terminal motifs (literal)
Abstract
  • A-kinase anchor proteins (AKAPs) assemble multi-enzyme signaling complexes in proximity to substrate/effector proteins, thus directing and amplifying membrane-generated signals. S-AKAP84 and AKAP121 are alternative splicing products with identical NH2 termini. These AKAPs bind and target protein kinase A (PKA) to the outer mitochondrial membrane. Tubulin was identified as a binding partner of S-AKAP84 in a yeast two-hybrid screen. Immunopptn. and co-sedimentation expts. in rat testis exts. confirmed the interaction between microtubules and S-AKAP84. In situ immunostaining of testicular germ cells (GC2) shows that AKAP121 concs. on mitochondria in interphase and on mitotic spindles during M phase. Purified tubulin binds directly to S-AKAP84 but not to a deletion mutant lacking the mitochondrial targeting domain (MT) at residues 1-30. The MT is predicted to form a highly hydrophobic a-helical wheel that might also mediate interaction with tubulin. Disruption of the wheel by site-directed mutagenesis abolished tubulin binding and reduced mitochondrial attachment of an MT-GFP fusion protein. Some MT mutants retain tubulin binding but do not localize to mitochondria. Thus, the tubulin-binding motif lies within the mitochondrial attachment motif. Our findings indicate that S-AKAP84/AKAP121 use overlapping targeting motifs to localize signaling enzymes to mitochondrial and cytoskeletal compartments. (literal)
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