The Allosteric Mechanism Induced by Protein Kinase A (PKA) Phosphorylation of Dematin (Band 4.9)
Lin Chen, Jeffrey W Brown, Yee-Foong Mok, Danny M Hatters, C James McKnight
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2013
Dematin (band 4.9) is an F-actin binding and bundling protein best known for its role within red blood cells, where it both stabilizes as well as attaches the spectrin/actin cytoskeleton to the erythrocytic membrane. Here, we investigate the structural consequences of phosphorylating serine 381, a covalent modification that turns off F-actin bundling activity. In contrast to the canonical doctrine, in which phosphorylation of an intrinsically disordered region/protein confers affinity for another domain/protein, we found the converse to be true of dematin: phosphorylation of the well folded C-terminal villin-type headpiece confers affinity for its intrinsically disordered N-terminal core dom..View full abstract
Awarded by National Institutes of Health
Awarded by NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
This work was supported, in whole or in part, by National Institutes of Health Grant GM62886 (to C. J. M.). This work was also supported by a Boston University graduate student research fellowship (to J. W. B.).