Format

Send to

Choose Destination
Mol Cell. 2004 Sep 24;15(6):889-99.

AKAP-Lbc nucleates a protein kinase D activation scaffold.

Author information

1
Howard 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.

PMID:
15383279
DOI:
10.1016/j.molcel.2004.09.015
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center