Journal
EUROPEAN JOURNAL OF BIOCHEMISTRY
Volume 269, Issue 2, Pages 546-552Publisher
BLACKWELL PUBLISHING LTD
DOI: 10.1046/j.0014-2956.2001.02680.x
Keywords
phosphoprotein phosphatase; PP2A; subunit interactions; phosphorylation
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Funding
- NCI NIH HHS [3P30 CA42014, R01 CA80809] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [P30CA042014, R01CA080809] Funding Source: NIH RePORTER
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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.
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