Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function.

ABSTRACT: Phosducin (Pdc) is a conserved phosphoprotein that, when unphosphorylated, binds with high affinity to the complex of βγ-subunits of G protein transducin (G_tβγ). The ability of Pdc to bind to G_tβγ is inhibited through its phosphorylation at S54 and S73 within the N-terminal domain (Pdc-ND) followed by association with the scaffolding protein 14-3-3. However, the molecular basis for the 14-3-3-dependent inhibition of Pdc binding to G_tβγ is unclear. By using small-angle x-ray scattering, high-resolution NMR spectroscopy, and limited proteolysis coupled with mass spectrometry, we show that phosphorylated Pdc and 14-3-3 form a complex in which the Pdc-ND region 45-80, which forms a part of Pdc's G_tβγ binding surface and contains both phosphorylation

SUBMITTER: Kacirova M 

PROVIDER: S-EPMC5390052 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature