Ontology highlight
ABSTRACT:
SUBMITTER: Ueki Y
PROVIDER: S-EPMC6981294 | biostudies-literature | 2019 Dec
REPOSITORIES: biostudies-literature
Molecular cell 20191001 6
Dynamic protein phosphorylation constitutes a fundamental regulatory mechanism in all organisms. Phosphoprotein phosphatase 4 (PP4) is a conserved and essential nuclear serine and threonine phosphatase. Despite the importance of PP4, general principles of substrate selection are unknown, hampering the study of signal regulation by this phosphatase. Here, we identify and thoroughly characterize a general PP4 consensus-binding motif, the FxxP motif. X-ray crystallography studies reveal that FxxP m ...[more]