Abstract
AKAP450 (also known as AKAP350, CG-NAP or Hyperion) and pericentrin are large coiled-coil proteins found in mammalian centrosomes that serve to recruit structural and regulatory components including dynein and protein kinase A. We find that these proteins share a well conserved 90 amino acid domain near their C-termini that is also found in coiled-coil proteins of unknown function from Drosophila and fission yeast. Fusion of the C-terminal region from either protein to a reporter protein confers a centrosomal localization, and overexpression of the domain from AKAP450 displaces endogenous pericentrin, suggesting recruitment to a shared site. When isolated from transfected cells the C-terminal domain of AKAP450 was associated with calmodulin, suggesting that this protein could contribute to centrosome assembly.
MeSH terms
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A Kinase Anchor Proteins
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Adaptor Proteins, Signal Transducing*
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Amino Acid Sequence
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Animals
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Antigens / chemistry*
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Antigens / genetics
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Antigens / metabolism
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COS Cells
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Calmodulin / metabolism
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Carrier Proteins*
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Centrosome / ultrastructure*
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Conserved Sequence
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Cyclic AMP-Dependent Protein Kinases / chemistry
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Cyclic AMP-Dependent Protein Kinases / metabolism
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Cytoskeletal Proteins*
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Drosophila / chemistry
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Green Fluorescent Proteins
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Humans
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Luminescent Proteins / chemistry
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Luminescent Proteins / metabolism
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Microscopy, Fluorescence
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Microtubule-Associated Proteins / chemistry*
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Models, Genetic
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Molecular Sequence Data
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Plasmids / metabolism
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Promoter Regions, Genetic
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Protein Binding
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / metabolism
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Schizosaccharomyces / chemistry
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Sequence Homology, Amino Acid
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Transfection
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Tubulin / chemistry
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Tubulin / metabolism
Substances
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A Kinase Anchor Proteins
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AKAP9 protein, human
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Adaptor Proteins, Signal Transducing
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Antigens
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Calmodulin
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Carrier Proteins
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Cytoskeletal Proteins
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Luminescent Proteins
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Microtubule-Associated Proteins
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Recombinant Fusion Proteins
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Tubulin
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pericentrin
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Green Fluorescent Proteins
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Cyclic AMP-Dependent Protein Kinases