| First Author | Li X | Year | 2002 |
| Journal | Eur J Biochem | Volume | 269 |
| Issue | 2 | Pages | 546-52 |
| PubMed ID | 11856313 | Mgi Jnum | J:74544 |
| Mgi Id | MGI:2158603 | Doi | 10.1046/j.0014-2956.2001.02680.x |
| Citation | Li X, et al. (2002) Two conserved domains in regulatory B subunits mediate binding to the A subunit of protein phosphatase 2A. Eur J Biochem 269(2):546-52 |
| abstractText | Protein phosphatase 2A (PP2A) is an abundant heterotrimeric serine/threonine phosphatase containing highly conserved structural (A) and catalytic (C) subunits. Its diverse functions in the cell are determined by its association with a highly variable regulatory and targeting B subunit. At least three distinct gene families encoding B subunits are known: B/B55/CDC55, B'/B56/RTS1 and B'/PR72/130. No homology has been identified among the B families, and little is known about how these B subunits interact with the PP2A A and C subunits. In vitro expression of a series of B56alpha fragments identified two distinct domains that bound independently to the A subunit. Sequence alignment of these A subunit binding domains (ASBD) identified conserved residues in B/B55 and PR72 family members. The alignment successfully predicted domains in B55 and PR72 subunits that similarly bound to the PP2A A subunit. These results suggest that these B subunits share a common core structure and mode of interaction with the PP2A holoenzyme. |
