The Structure of the Protein Phosphatase 2A PR65/A Subunit Reveals the Conformation of Its 15 Tandemly Repeated HEAT Motifs

@article{Groves1999TheSO,
  title={The Structure of the Protein Phosphatase 2A PR65/A Subunit Reveals the Conformation of Its 15 Tandemly Repeated HEAT Motifs},
  author={Matthew R. Groves and Neil Hanlon and Patric Turowski and Brian A. Hemmings and David Barford},
  journal={Cell},
  year={1999},
  volume={96},
  pages={99-110}
}

Figures and Tables from this paper

Structure of the Protein Phosphatase 2A Holoenzyme
Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
TLDR
The crystal structure of an AB′C heterotrimeric PP2A holoenzyme reveals that the HEAT repeats of the scaffold A subunit form a horseshoe-shaped fold, holding the catalytic C and regulatory B′ subunits together on the same side.
Structural and Biochemical Characterization of Human PR 70 in Isolation and in Complex with the Scaffolding Subunit of Protein Phosphatase 2 A
TLDR
The crystal structure of B’’/PR70 reveals a two domain elongated structure with two Ca binding EF-hands and the interaction of both binding partner and their calcium dependency is characterized using biophysical techniques.
Structural and Biochemical Characterization of Human PR70 in Isolation and in Complex with the Scaffolding Subunit of Protein Phosphatase 2A
TLDR
The crystal structure of B’’/PR70 reveals a two domain elongated structure with two Ca2+ binding EF-hands and isothermal Titration Calorimetry studies and SAXS data support that PR70 and the A-subunit have high affinity to each other.
The structure of the PP2A regulatory subunit B56γ: The remaining piece of the PP2A jigsaw puzzle
TLDR
The first structure of a free non‐complexed B subunit, B56γ is presented, which induces the formation of a binding site for the invariant C‐terminus of the catalytic subunit that locks in the complex as a last step of assembly.
Mechanisms of the Scaffold Subunit in Facilitating Protein Phosphatase 2A Methylation
TLDR
It is shown that PP2A-specific methyltransferase, LCMT-1, exhibits a higher activity toward the core enzyme (A–C heterodimer) than free PP2Ac, and the A-subunit facilitatesPP2A methylation via three distinct mechanisms: stabilization of a proper protein fold and an active conformation ofPP2Ac.
Protein Phosphatase 2A Holoenzyme Assembly
TLDR
It is shown that holoenzyme incorporation protects Bγ from rapid degradation by the ubiquitin/proteasome pathway, and requires multiple, precisely aligned contacts within a core β-propeller domain.
NMR Studies of the C-Terminus of alpha4 Reveal Possible Mechanism of Its Interaction with MID1 and Protein Phosphatase 2A
TLDR
The solution structure of a 45-amino acid region derived from the C-terminus of alpha4 (alpha45) that binds tightly to the Bbox1 domain of MID1 in aqueous solution is reported.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 128 REFERENCES
Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens
TLDR
Native gel analysis of mutant A subunits synthesized in vitro demonstrated that the binding region for the B subunit, previously thought to include repeats 2 to 8, covers repeats 1 to 10 and that the B and C subunits cooperate in binding to the A subunit.
The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR‐mediated protein–protein interactions
TLDR
The crystal structure of the TPR domain of a protein phosphatase, PP5, is reported, which indicates that multiple‐TPR motif proteins would fold into a right‐handed super‐helical structure with a continuous helical groove suitable for the recognition of target proteins, hence defining a novel mechanism for protein recognition.
The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits.
TLDR
Two protein phosphatase 2A (PP2A) holoenzymes were isolated from rabbit skeletal muscle containing, in addition to the catalytic and PR65 regulatory subunits, proteins of apparent molecular masses of 61 and 56 kDa respectively, which revealed that this protein exists in multiple isoforms encoded by at least three genes, one of which gives rise to several splicing variants.
High Complexity in the Expression of the B′ Subunit of Protein Phosphatase 2A0
TLDR
The cloning and expression of a new family of B-subunit, the B′, associated with the PP2A0 form is reported, indicating that at least seven B′ subunit isoforms may participate in the generation of a large number of PP2 A0 holoenzymes that may be spatially and/or functionally targeted to different cellular processes.
Crystal Structure of Protein Farnesyltransferase at 2.25 Angstrom Resolution
TLDR
The crystal structure of heterodimeric mammalian FTase was determined at 2.25 angstrom resolution and shows a combination of two unusual domains: a crescent-shaped seven-helical hairpin domain and an α-α barrel domain.
Identification of a New Family of Protein Phosphatase 2A Regulatory Subunits (*)
TLDR
The identification of this novel phosphatase regulator gene family will facilitate future studies on the control of protein dephosphorylation and the role of PP2A in cellular function.
A structural basis of the interactions between leucine-rich repeats and protein ligands
TLDR
The unusual non-globular structure of ribonuclease inhibitor, its solvent-exposed parallel β-sheet and the conformational flexibility of the structure are used in the interaction; they appear to be the principal reasons for the effectiveness of leucine-rich repeats as protein-binding motifs.
Identification of binding sites on the regulatory A subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of simian virus 40 and polyomavirus.
TLDR
The data suggest cooperativity between C and T antigens in binding to A, which is most apparent for medium T antigen, which can only bind to those A subunit molecules that provide the entire binding region for the C subunit.
Analysis of subunit isoforms in protein phosphatase 2A holoenzymes from rabbit and Xenopus.
Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65-kDa regulatory subunit PR65alpha.
TLDR
The identification of a site of interaction between PP2Ac and PR65alpha by disruption of a stretch of basic amino acids by introduction of a glutamate at position 416 indicated that this basic motif is an important determinant for the interaction of PR65 and PP2 Ac.
...
1
2
3
4
5
...