• E. Klussmann
  • W. Rosenthal


  • UCSD Nature Molecule Pages


  • UCSD Nature Molecule Pages


  • AKAP7, also referred to as AKAP18, comprises a family of splice variants including alpha, beta, gamma, and delta. AKAP7alpha is also known as AKAP15. AKAP7 variants function as A-kinase anchoring proteins (AKAPs), a family of distinct but functionally conserved proteins which mediate tethering of cAMP-dependent protein kinase (PKA) to subcellular compartments. This facilitates the local activation of PKA in response to extracellular stimuli such as hormones and neurotransmitters. The compartmentalization of PKA by AKAPs contributes to the specificity of a cellular response to a given stimulus by enabling timely and spatially orchestrated cAMP-dependent signal transduction. The inactive PKA holoenzyme is a heterotetramer consisting of a homodimer of regulatory subunits (RIalpha, RIbeta, RIIalpha, or RIIbeta) and two catalytic (Calpha, Cbeta, or Cgamma) subunits each bound to a regulatory one. Cyclic AMP binds to two sites on each regulatory subunit and induces dissociation of the catalytic subunits. AKAPs interact with the dimeric regulatory subunits. Most AKAPs interact with RII subunits. Some, however, also bind RI subunits (dual-specificity AKAPs). AKAP7 belongs to this group of AKAPs.