Phosphorylation of T897 in the dimerization domain of Gemin5 modulates protein interactions and translation regulation.

ABSTRACT: Gemin5 is a multifunctional RNA binding protein (RBP) organized in domains with a distinctive structural organization. The protein is a hub for several protein networks performing diverse RNA-dependent functions including regulation of translation, and recognition of small nuclear RNAs (snRNAs). Here we sought to identify the presence of phosphoresidues on the C-terminal half of Gemin5, a region of the protein that harbors a tetratricopeptide repeat (TPR)-like dimerization domain and a non-canonical RNA binding site (RBS1). We identified two phosphoresidues in the purified protein: P-T897 in the dimerization domain and P-T1355 in RBS1. Replacing T897 and T1355 with alanine led to decreased translation, and mass spectrometry analysis revealed that mutation T897A strongly abrogates the assoc

SUBMITTER: Francisco-Velilla R 

PROVIDER: S-EPMC9676205 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature