Phosphorylation of the amino-terminal region of X11L regulates its interaction with APP.

ABSTRACT: X11-like (X11L) is neuronal adaptor protein that interacts with the amyloid beta-protein precursor (APP) and regulates its metabolism. The phosphotyrosine interaction/binding (PI/PTB) domain of X11L interacts with the cytoplasmic region of APP695. We found that X11L-APP interaction is enhanced in osmotically stressed cells and X11L modification is required for the enhancement. Amino acids 221-250 (X11L(221-250)) are required for the enhanced association with APP in osmotically stressed cells; this motif is 118 amino acids closer to the amino-terminal end of the protein than the PI/PTB domain (amino acids 368-555). We identified two phosphorylatable seryl residues, Ser236 and Ser238, in X11L(221-250) and alanyl substitution of either seryl residue diminished the enhanced association with AP

SUBMITTER: Sakuma M 

PROVIDER: S-EPMC3846477 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature