Two conserved domains in regulatory B subunits mediate binding to the A subunit of protein phosphatase 2A.
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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Related Subject Headings
- Substrate Specificity
- Sequence Homology, Amino Acid
- Recombinant Fusion Proteins
- Protein Phosphatase 2
- Phosphoprotein Phosphatases
- Molecular Sequence Data
- Glutathione Transferase
- Conserved Sequence
- Biochemistry & Molecular Biology
- Amino Acid Sequence
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Substrate Specificity
- Sequence Homology, Amino Acid
- Recombinant Fusion Proteins
- Protein Phosphatase 2
- Phosphoprotein Phosphatases
- Molecular Sequence Data
- Glutathione Transferase
- Conserved Sequence
- Biochemistry & Molecular Biology
- Amino Acid Sequence