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Updated: Jul 28, 2026

Assaying the Kinase Activity of LRRK2 in vitro
Published on: January 18, 2012
AKAP-Lbc nucleates a protein kinase D activation scaffold
Graeme K Carnegie1, F Donelson Smith, George McConnachie
1Howard Hughes Medical Institute, Vollum Institute, Oregon Health and Sciences University, Portland, OR 97239, USA.
Abstract:
The transmission of cellular signals often proceeds through multiprotein complexes where enzymes are positioned in proximity to their upstream activators and downstream substrates. In this report we demonstrate that the A-kinase anchoring protein AKAP-Lbc assembles an activation complex for the lipid-dependent enzyme protein kinase D (PKD). Using a combination of biochemical, enzymatic, and immunofluorescence techniques, we show that the anchoring protein contributes to PKD activation in two ways: it recruits an upstream kinase PKCeta and coordinates PKA phosphorylation events that release activated protein kinase D. Thus, AKAP-Lbc synchronizes PKA and PKC activities in a manner that leads to the activation of a third kinase. This configuration illustrates the utility of kinase anchoring as a mechanism to constrain the action of broad-spectrum enzymes.
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