Ontology highlight
ABSTRACT:
SUBMITTER: Kim TS
PROVIDER: S-EPMC2755843 | biostudies-other | 2009 Aug
REPOSITORIES: biostudies-other
Kim Tae-Sung TS Kim Hag Dong HD Shin Hyun-Seock HS Kim Joon J
The Journal of biological chemistry 20090520 32
It has been shown previously that ribosomal protein S3 (rpS3) has an endonuclease activity, which is increased by protein kinase Cdelta (PKCdelta)-dependent phosphorylation. However, the reciprocal mechanism for rpS3 dephosphorylation is not known. In this study, we examined phosphatases involved in rpS3 dephosphorylation, and we determined that rpS3 is specifically dephosphorylated by protein phosphatase 2A (PP2A). By immunoprecipitation assay, rpS3 only interacted with PP2Ac but not with prote ...[more]