Anti-PP4R2 PPP4R2 Antibody

Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair.<br><br>Hastie C.J., Biochem. J. 347:845-855(2000).<br>Zhang W., Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.<br>Mural R.J., Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases

DNA/RNA, Epigenetics and Nuclear Signaling, Histones, Organelles, Protein Phosphorylation, RNA Processing, Ser/Thr Phosphatases, Signal Transduction, Splicing, Subcellular Markers, Tags & Cell Markers

Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4) . May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair. .

Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Ionizing radiation induces relocalization to nuclear foci and colocalization with RPA2.