A5047459828- Ubiquitin and proteasome pathways
- Peptidase Inhibition and Analysis
- Cancer, Hypoxia, and Metabolism
- Cancer-related Molecular Pathways
- Signaling Pathways in Disease
- Biochemical and Molecular Research
Temple University
2023-2024
Abstract The Ser/Thr protein phosphatase 2 A (PP2A) regulates the dephosphorylation of many phosphoproteins. Substrate recognition are mediated by B regulatory subunits. Here, we report identification a substrate conserved motif [RK]-V-x-x-[VI]-R in FAM122A, an inhibitor B55α/PP2A. This is necessary for FAM122A binding to B55α, and computational structure prediction suggests motif, which helical, blocks docking same site. In this model, also spatially constrains access occluding catalytic...
The Ser/Thr protein phosphatase 2A (PP2A) is a highly conserved collection of heterotrimeric holoenzymes responsible for the dephosphorylation many regulated phosphoproteins. Substrate recognition and integration regulatory cues are mediated by B subunits that complexed to catalytic subunit (C) scaffold (A). PP2A/B55 substrate recruitment was thought be charge-charge interactions between surface B55α its substrates. Challenging this view, we recently discovered SLiM [ RK ]- V -x-x-[ VI R in...
Serine/threonine protein phosphatase 2 (PP2A) forms heterotrimeric holoenzymes, where a scaffold subunit bridges the PP2A catalytic to B regulatory subunit, e.g., B55α. The PP2A/B55α holoenzyme plays key roles in signaling and cell-cycle control targeting multiple substrates. Here, we describe semiquantitative approaches determine substrate specificity. Parts I II detail assess PP2A/B55α-mediated dephosphorylation of immobilized peptide variants. III IV methods PP2A/B55α-substrate-binding...