The allosteric mechanism induced by protein kinase A (PKA) phosphorylation of dematin (band 4.9).

The Allosteric Mechanism Induced by Protein Kinase A (PKA) Phosphorylation of Dematin (Band 4.9)Journal of Biological ChemistryVol. 288Issue 12PreviewBackground: Protein kinase A regulates the stability of the erythrocyte via phosphorylation of the cytoskeletal protein dematin (band 4.9).Results: We present an experimentally derived allosteric mechanism for PKA phosphorylation of dematin.Conclusion: A phosphorylation mimicking mutation in the folded headpiece causes it to bind to the natively unfolded core domain of dematin.Significance: PKA phosphorylation of dematin represents a novel conformational switch. Full-Text PDF Open Access VOLUME 288 (2013) PAGES 8313–8320 PAGE 8317: The images of actin microfilaments shown in panels B–D of Fig. 4 were not correct. Specifically, panels B and C were mistakenly made from images of the tD mutant micrograph at different magnifications when panel B should have been prepared from an rD-core micrograph. The micrograph published as rD-S381E in the original figure was also prepared from the wrong micrograph. In the corrected figure, panel B has been replaced with a micrograph of rD-core that was made by rescanning the original micrographs, and panel D has been replaced with an image from the correct micrograph. These corrections do not change the interpretation of the results or the conclusions of this work.