Phosphorylation-Dependent 14-3-3 Binding to LRRK2 Is Impaired by Common Mutations of Familial Parkinson's Disease
Figure 7
PKA Phosphorylation, 14-3-3 binding of LRRK2, and the effect of common familial mutations of LRRK2 in 14-3-3 binding.
A schematic model showing PKA (or other kinase) phosphorylation of S910/S935, dimeric14-3-3 binding of LRRK2 at pS910/pS935 sites in wild type LRRK2; PD-linked mutations R1441G, Y1699C or G2019S abolishes or reduces phosphorylation of S910/S935 and impairs 14-3-3 binding. In addition, we propose that dimeric 14-3-3 bind to pS910 and pS935 in the same LRRK2 molecule and binding of 14-3-3 plays little role in LRRK2 dimer formation.