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TitleIntrinsic disorder within an AKAP-protein kinase A complex guides local substrate phosphorylation.
Journal, issue, pagesElife, Vol. 2, Page e01319, Year 2013
Publish dateNov 5, 2013
AuthorsF Donelson Smith / Steve L Reichow / Jessica L Esseltine / Dan Shi / Lorene K Langeberg / John D Scott / Tamir Gonen /
PubMed AbstractAnchoring proteins sequester kinases with their substrates to locally disseminate intracellular signals and avert indiscriminate transmission of these responses throughout the cell. Mechanistic ...Anchoring proteins sequester kinases with their substrates to locally disseminate intracellular signals and avert indiscriminate transmission of these responses throughout the cell. Mechanistic understanding of this process is hampered by limited structural information on these macromolecular complexes. A-kinase anchoring proteins (AKAPs) spatially constrain phosphorylation by cAMP-dependent protein kinases (PKA). Electron microscopy and three-dimensional reconstructions of type-II PKA-AKAP18γ complexes reveal hetero-pentameric assemblies that adopt a range of flexible tripartite configurations. Intrinsically disordered regions within each PKA regulatory subunit impart the molecular plasticity that affords an ∼16 nanometer radius of motion to the associated catalytic subunits. Manipulating flexibility within the PKA holoenzyme augmented basal and cAMP responsive phosphorylation of AKAP-associated substrates. Cell-based analyses suggest that the catalytic subunit remains within type-II PKA-AKAP18γ complexes upon cAMP elevation. We propose that the dynamic movement of kinase sub-structures, in concert with the static AKAP-regulatory subunit interface, generates a solid-state signaling microenvironment for substrate phosphorylation. DOI: http://dx.doi.org/10.7554/eLife.01319.001.
External linksElife / PubMed:24192038 / PubMed Central
MethodsEM (single particle)
Resolution35.0 Å
Structure data

5755

3j4q

EMDB-5755: 3D EM Reconstruction of the AKAP18-PKA Complex in a Bent Conformation
PDB-3j4q: Pseudo-atomic model of the AKAP18-PKA complex in a bent conformation derived from electron microscopy
Method: EM (single particle) / Resolution: 35.0 Å

5756

3j4r

EMDB-5756: 3D EM Reconstruction of the AKAP18-PKA Complex in a Linear Conformation
PDB-3j4r: Pseudo-atomic model of the AKAP18-PKA Complex in a linear conformation derived from electron microscopy
Method: EM (single particle) / Resolution: 35.0 Å

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsTRANSFERASE / A-kinase anchoring protein / cAMP-Dependent Kinase / RII / PKA regulatory subunit II / phosphorylation / anchoring / intrinsic disorder

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