Molecular characterization of AKAP149, a novel A kinase anchor protein with a KH domain.

@article{Trendelenburg1996MolecularCO,
  title={Molecular characterization of AKAP149, a novel A kinase anchor protein with a KH domain.},
  author={George Trendelenburg and Manfred W Hummel and E. O. Riecken and Christoph Hanski},
  journal={Biochemical and biophysical research communications},
  year={1996},
  volume={225 1},
  pages={313-9}
}
The cytosolic cAMP activates in eukaryotic cells several isoforms of cAMP-dependent protein kinase (PKAs) involved in signal transduction. The effects of individual PKA isoforms are determined by their cellular localisation, specified through binding to distinct A Kinase Anchor Proteins (AKAPs). A new member of the AKAP family, a membrane-anchored 903 amino acid long protein, designated AKAP149, is characterized in the present work. It is a putative splicing variant of S-AKAP84 with the… CONTINUE READING