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The PACT domain, a conserved centrosomal targeting motif in the coiled‐coil proteins AKAP450 and pericentrin
Author(s) -
Gillingham Alison K,
Munro Sean
Publication year - 2000
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kvd105
Subject(s) - centrosome , coiled coil , biology , microbiology and biotechnology , fusion protein , scaffold protein , protein domain , dynein , calmodulin , nuclear protein , genetics , microtubule , biochemistry , signal transduction , gene , recombinant dna , cell cycle , transcription factor , enzyme
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.