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PubMed: 19277525

Title
Assembly and structure of protein phosphatase 2A.
Journal
Science in China. Series C, Life sciences
Volume
52
Issue
None
Pages
135-46
Date
2009-02-01
Authors
Shi Y

Evidence 28af554815
JSON

Two potent tumor-inducing toxins, okadaic acid (OA) and microcystin-LR (MCLR), specifically inhibit PP2A

a(CHEBI:"microcystin-LR") decreases act(complex(GO:"protein phosphatase type 2A complex")) View Subject | View Object

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a(CHEBI:"okadaic acid") decreases act(complex(GO:"protein phosphatase type 2A complex")) View Subject | View Object

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Evidence 74b49cc92f
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The structural feature that PME-1 binds directly to the PP2A active site, overlapping the binding sites for OA and MCLR, also explains why these phosphatase inhibitors blocked the methylesterase activity of PME-1

a(CHEBI:"microcystin-LR") decreases act(p(HGNC:PPME1)) View Subject | View Object

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a(CHEBI:"okadaic acid") decreases act(p(HGNC:PPME1)) View Subject | View Object

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p(HGNC:PPME1) directlyIncreases complex(a(GO:"protein phosphatase type 2A complex"), p(HGNC:PPME1)) View Subject | View Object

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Evidence 31c5669563
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The catalytic subunit of PP2A is the primary cellular target of OA

a(CHEBI:"okadaic acid") decreases act(p(HGNC:PPP2CA)) View Subject | View Object

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Evidence a41bcce7a4
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PP2A plays a critical role in cellular physiology including cell cycle regulation, cell proliferation and death, development, cytoskeleton dynamics, cell mobility, and regulation of multiple signal transduction pathways

complex(GO:"protein phosphatase type 2A complex") regulates bp(GO:"cell cycle") View Subject | View Object

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complex(GO:"protein phosphatase type 2A complex") regulates bp(GO:"cell population proliferation") View Subject | View Object

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complex(GO:"protein phosphatase type 2A complex") regulates bp(GO:"cell death") View Subject | View Object

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complex(GO:"protein phosphatase type 2A complex") regulates act(a(GO:cytoskeleton)) View Subject | View Object

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complex(GO:"protein phosphatase type 2A complex") regulates bp(GO:"cell motility") View Subject | View Object

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complex(GO:"protein phosphatase type 2A complex") regulates bp(GO:"signal transduction") View Subject | View Object

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Evidence 2409ac15c3
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PP2A functions by removing phosphate groups from substrate phosphoproteins

complex(GO:"protein phosphatase type 2A complex") increases bp(GO:"protein dephosphorylation") View Subject | View Object

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Evidence 9eafef5d52
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A key function of PP2A is thought to dephosphorylate the hyperphosphorylated Tau protein

complex(GO:"protein phosphatase type 2A complex") decreases p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)) View Subject | View Object

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Evidence 37d16a719c
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The PP2A core enzyme, upon initial incubation with various concentrations of PME-1, exhibited full Ser/Thr phosphatase activity and, only after prolonged incubation time, had substantial loss of the phosphatase activity

act(complex(GO:"protein phosphatase type 2A complex")) negativeCorrelation composite(p(HGNC:PPME1), p(HGNC:PPP2CA), p(HGNC:PPP2R1A)) View Subject | View Object

Appears in Networks:

composite(p(HGNC:PPME1), p(HGNC:PPP2CA), p(HGNC:PPP2R1A)) negativeCorrelation act(complex(GO:"protein phosphatase type 2A complex")) View Subject | View Object

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Evidence d7782020aa
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Thus, PME-1 appears to exist in an inactive conformation in the absence of PP2A binding.

complex(a(GO:"protein phosphatase type 2A complex"), p(HGNC:PPME1)) increases act(p(HGNC:PPME1)) View Subject | View Object

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Evidence 76e6c5146e
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Structural analysis of the heterotrimeric PME-1-PP2A complex showed that PME-1 is only activated upon binding to PP2A (Figure 4, left panel).

complex(a(GO:"protein phosphatase type 2A complex"), p(HGNC:PPME1)) increases act(p(HGNC:PPME1)) View Subject | View Object

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Evidence b5be95159f
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Interestingly, although PME-1 is activated by PP2A binding, the catalytic subunit of PP2A is inactivated in this process, not just through demethylation but also by loss of the catalytic metal ions

complex(a(GO:"protein phosphatase type 2A complex"), p(HGNC:PPME1)) increases act(p(HGNC:PPME1)) View Subject | View Object

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complex(a(GO:"protein phosphatase type 2A complex"), p(HGNC:PPME1)) decreases act(p(HGNC:PPP2CA)) View Subject | View Object

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complex(a(GO:"protein phosphatase type 2A complex"), p(HGNC:PPME1)) decreases p(HGNC:PPP2CA, pmod(Me, Leu, 309)) View Subject | View Object

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p(HGNC:PPP2CA, pmod(Me, Leu, 309)) increases act(p(HGNC:PPP2CA)) View Subject | View Object

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Evidence d9a5259d63
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A portion of cellular PP2A stably associated with PME-1 and was catalytically inactive [80]; intriguingly, this inactive portion of PP2A could be re-activated by PP2A phosphatase activator (PTPA), but not by LCMT1, ruling out the possibility that inactivation was solely caused by demethylation

complex(a(GO:"protein phosphatase type 2A complex"), p(HGNC:PPME1)) decreases act(p(HGNC:PPP2CA)) View Subject | View Object

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p(HGNC:PPME1) increases complex(a(GO:"protein phosphatase type 2A complex"), p(HGNC:PPME1)) View Subject | View Object

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p(HGNC:LCMT1) causesNoChange act(complex(GO:"protein phosphatase type 2A complex")) View Subject | View Object

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p(HGNC:PTPA) increases act(complex(GO:"protein phosphatase type 2A complex")) View Subject | View Object

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Evidence db6e68f550
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Furthermore, formation of a stable complex between PP2A and PME-1 likely blocks LCMT1-catalyzed methylation.

complex(a(GO:"protein phosphatase type 2A complex"), p(HGNC:PPME1)) decreases p(HGNC:PPP2CA, pmod(Me, Leu, 309)) View Subject | View Object

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p(HGNC:LCMT1) increases p(HGNC:PPP2CA, pmod(Me, Leu, 309)) View Subject | View Object

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Evidence 966ab11883
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Reversible methylation of PP2A is catalyzed by two highly conserved and PP2A-specific enzymes, leucine carboxyl methyltransferase (LCMT1)[21,33] and PP2A methylesterase (PME-1)[17] (Figure 1).

p(HGNC:PPME1) decreases p(HGNC:PPP2CA, pmod(Me, Leu, 309)) View Subject | View Object

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p(HGNC:LCMT1) increases p(HGNC:PPP2CA, pmod(Me, Leu, 309)) View Subject | View Object

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Evidence c0041e3953
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PME-1 catalyzes removal of the methyl group, thus reversing the activity of LCMT1

p(HGNC:PPME1) decreases p(HGNC:PPP2CA, pmod(Me, Leu, 309)) View Subject | View Object

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act(p(HGNC:PPME1)) negativeCorrelation act(p(HGNC:LCMT1)) View Subject | View Object

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act(p(HGNC:LCMT1)) negativeCorrelation act(p(HGNC:PPME1)) View Subject | View Object

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Evidence 72f4d75f79
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Recent evidence suggests a broader role for PME-1 than just being a demethylating enzyme for the catalytic subunit of PP2A

p(HGNC:PPME1) decreases p(HGNC:PPP2CA, pmod(Me, Leu, 309)) View Subject | View Object

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Evidence 2ee6e28223
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Structural observations clearly indicate that PME-1 inactivates the phosphatase activity of PP2A

p(HGNC:PPME1) decreases act(complex(GO:"protein phosphatase type 2A complex")) View Subject | View Object

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Evidence ed85027719
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Structures of the PP2A core enzyme reveal that the catalytic subunit recognizes one end of the scaffold subunit through interactions with the conserved ridge of HEAT repeats 11–15

p(HGNC:PPP2CA) increases complex(p(HGNC:PPP2CA), p(INTERPRO:"HEAT repeat")) View Subject | View Object

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Evidence dc0bee175d
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Previous studies suggested that carboxy-methylation of the catalytic subunit played an important role in the assembly of heterotrimeric PP2A holoenzymes in cells

p(HGNC:PPP2CA) increases complex(GO:"protein phosphatase type 2A complex") View Subject | View Object

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Evidence 7cc18fb24f
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This analysis suggests that at least two non-overlapping fragments of Tau, both within the microtubule-binding repeats, have the ability to interact with the acidic top face of the B subunit

p(HGNC:MAPT) increases complex(p(HGNC:MAPT), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

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Evidence e8ec14f96f
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To gain full activity towards specific substrates, the PP2A core enzyme interacts with a variable regulatory subunit to form a heterotrimeric holoenzyme. The variable regulatory subunits consist of four families: B (also known as B55 or PR55), B′ (B56 or PR61), B′′ (PR48/PR72/PR130), and B′′′ (PR93/PR110), with at least 16 members in these families

p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55") increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

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p(HGNC:PPP2R3A) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:PPP2R3A)) View Subject | View Object

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p(HGNC:PPP2R3B) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:PPP2R3B)) View Subject | View Object

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p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56") increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56")) View Subject | View Object

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p(HGNC:STRN) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:STRN)) View Subject | View Object

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p(HGNC:STRN3) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:STRN3)) View Subject | View Object

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Evidence 72b87a6295
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Except the B′′′ subunits, direct interactions between the PP2A core enzyme and the regulatory subunits have been demonstrated

p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55") directlyIncreases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

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p(HGNC:PPP2R3A) directlyIncreases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:PPP2R3A)) View Subject | View Object

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p(HGNC:PPP2R3B) directlyIncreases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:PPP2R3B)) View Subject | View Object

Appears in Networks:

p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56") directlyIncreases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56")) View Subject | View Object

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p(HGNC:STRN) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:STRN)) View Subject | View Object

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p(HGNC:STRN3) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:STRN3)) View Subject | View Object

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Evidence 1beae3aa74
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Structure of the heterotrimeric PP2A holoenzyme involving a regulatory B subunit (Figure 2D) reveals how B subunit specifically recognizes the PP2A core enzyme and how it may facilitate substrate dephosphorylation

p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55") increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

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p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55") increases bp(GO:"protein dephosphorylation") View Subject | View Object

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Evidence 0b4d7e8585
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In fact, the B subunit is now known to contain multiple WD40 repeats [28], whereas B′′/PR72 is thought to contain two calcium-binding EF hands

p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55") association p(INTERPRO:"WD40 repeat") View Subject | View Object

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p(HGNC:PPP2R3A) association p(INTERPRO:"EF-hand domain") View Subject | View Object

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p(INTERPRO:"EF-hand domain") association p(HGNC:PPP2R3A) View Subject | View Object

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p(INTERPRO:"WD40 repeat") association p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55") View Subject | View Object

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Evidence c880739ddb
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Unlike the PP2A holoenzyme involving the B′ subunit, B makes few interactions with the catalytic subunit

p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55") increases complex(p(HGNC:PPP2CA), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

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Evidence 92502fe89d
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This analysis further suggests that the B subunit may form a relatively stable complex with the isolated scaffold subunit and does not seem to support the notion that the catalytic subunit is required for interaction between the scaffold and the B subunits

p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55") increases complex(p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

Appears in Networks:

Evidence 648fa0ba5f
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Previous investigations indicate that specific dephosphorylation of Tau appeared to be mediated by the B family of regulatory subunits

p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55") decreases p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)) View Subject | View Object

Appears in Networks:

Evidence 2ca31ca902
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The specificity in this in vitro system is quite robust, as evidenced by the observation that the PP2A core enzyme exhibited a lower activity to dephosphorylate the Tau protein than the PP2A holoenzyme involving the B subunit, but a higher activity than the holoenzyme involving the B′ subunit

complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A)) decreases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

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complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) decreases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

Appears in Networks:

complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56")) decreases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

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Evidence 2221ec0303
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In fact, competition experiments using recombinant proteins suggested that, compared to the unmethylated form, the methylated PP2A core enzyme exhibited a higher binding affinity for the B subunit

complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A)) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

Appears in Networks:

complex(p(HGNC:PPP2CA, pmod(Me)), p(HGNC:PPP2R1A)) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

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Evidence 011b0feb90
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The scaffold subunit of PP2A contains 15 tandem repeats of a conserved 39-amino-acid sequence known as a HEAT (huntingtin-elongation-A subunit-TOR) motif

p(INTERPRO:"HEAT repeat") association p(HGNC:PPP2R1A) View Subject | View Object

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p(HGNC:PPP2R1A) association p(INTERPRO:"HEAT repeat") View Subject | View Object

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Evidence 6ac64080b6
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First, conformational flexibility of the scaffold subunit is required for binding to the catalytic subunit and possibly other interacting proteins such as the regulatory subunits.

act(p(HGNC:PPP2R1A)) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A)) View Subject | View Object

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act(p(HGNC:PPP2R1A)) increases complex(p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56")) View Subject | View Object

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act(p(HGNC:PPP2R1A)) increases complex(p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

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act(p(HGNC:PPP2R1A)) increases complex(p(HGNC:PPP2R1A), p(HGNC:PPP2R3B)) View Subject | View Object

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act(p(HGNC:PPP2R1A)) increases complex(p(HGNC:PPP2R1A), p(HGNC:PPP2R3A)) View Subject | View Object

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act(p(HGNC:PPP2R1A)) increases complex(p(HGNC:PPP2R1A), p(HGNC:STRN3)) View Subject | View Object

Appears in Networks:

act(p(HGNC:PPP2R1A)) increases complex(p(HGNC:PPP2R1A), p(HGNC:STRN)) View Subject | View Object

Appears in Networks:

Evidence 2f4f5ca13b
JSON

Second, conformational flexibility of the scaffold subunit might be important for the phosphatase activity of the catalytic subunit

act(p(HGNC:PPP2R1A)) increases act(p(HGNC:PPP2CA)) View Subject | View Object

Appears in Networks:

Evidence 35e65b0af9
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For example, the PP2A holoenzyme involving the B′ family plays an essential role in cell-cycle progression, through direct interaction with the protein Shugoshin

complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:SGO1), p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56")) increases bp(GO:"cell cycle") View Subject | View Object

Appears in Networks:

complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56")) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:SGO1), p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56")) View Subject | View Object

Appears in Networks:

Evidence fa8a88d354
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The B′ regulatory subunit shows remarkable structural mimicry to the scaffold subunit and contains 8 HEAT-like repeats

p(INTERPRO:"HEAT repeat") association p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56") View Subject | View Object

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p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56") association p(INTERPRO:"HEAT repeat") View Subject | View Object

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Evidence 7a1a8bf972
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For example, two regions of the B′ subunit were found to mediate interaction with the scaffold subunit of PP2A

p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56") regulates complex(p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56")) View Subject | View Object

Appears in Networks:

Evidence e6628845c1
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Furthermore, the B′ subunit makes significant interactions with the catalytic subunit of PP2A, which consequently strengthens the inter-subunit packing, making the resulting holoenzyme relatively compact and rigid (Figure 2B).

p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56") increases complex(p(HGNC:PPP2CA), p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56")) View Subject | View Object

Appears in Networks:

Evidence 0ea7367314
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For example, the small tumor antigen derived from the DNA tumor viruses SV40 and polyoma viruses was shown to only interact with the PP2A core enzyme, but not the holoenzyme

p(UNIPROT:P03081) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(UNIPROT:P03081)) View Subject | View Object

Appears in Networks:

Evidence 24028719b2
JSON

In addition, the methylated carboxy-terminus might help recruit assembly factors that actively promote assembly of the PP2A holoenzymes in cells.

complex(p(HGNC:PPP2CA, pmod(Me)), p(HGNC:PPP2R1A)) increases complex(GO:"protein phosphatase type 2A complex") View Subject | View Object

Appears in Networks:

Evidence 6189775c94
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Intriguingly, changes in this peptide motif also affected interaction of the catalytic subunit with the alpha4 protein (α4), presumably through alteration of methylation[ 29], and led to a complex with distinct substrate specificity that is essential for cell survival

p(HGNC:PPP2CA, pmod(Me)) decreases complex(p(HGNC:IGBP1), p(HGNC:PPP2CA)) View Subject | View Object

Appears in Networks:

Evidence 9ac65da310
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By contrast, several recent studies using purified, recombinant proteins showed that the methylation status of the catalytic subunit did not play a decisive role for the in vitro assembly of PP2A holoenzymes involving the B and B′ subunit

p(HGNC:PPP2CA, pmod(Me)) causesNoChange complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

Appears in Networks:

p(HGNC:PPP2CA, pmod(Me)) causesNoChange complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56")) View Subject | View Object

Appears in Networks:

Evidence 520f0889c6
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It had also been demonstrated that methylation levels of PP2A changed during a cell cycle, suggesting a critical role of methylation in cell cycle regulation

p(FPLX:PPP2, pmod(Me)) regulates bp(GO:"cell cycle") View Subject | View Object

Appears in Networks:

Evidence 2abcbec214
JSON

Upon hyperphosphorylation, the protein Tau has a strong tendency to polymerize into neurofibrillary tangles in the brain, a hallmark of Alzheimer’s disease

p(HGNC:MAPT, pmod(HBP:hyperphosphorylation)) increases a(GO:"neurofibrillary tangle") View Subject | View Object

Appears in Networks:
Annotations
MeSH
Brain
MeSH
Alzheimer Disease

Evidence 4a7d01727f
JSON

Methylation of the carboxy-terminal Leu309 in a conserved TPDYFL309 motif of the catalytic subunit has been shown to enhance the affinity of the PP2A core enzyme for some, but not all, regulatory subunits

p(HGNC:PPP2CA, pmod(Me, Leu, 309)) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

Appears in Networks:

p(HGNC:PPP2CA, pmod(Me, Leu, 309)) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56")) View Subject | View Object

Appears in Networks:

p(HGNC:PPP2CA, pmod(Me, Leu, 309)) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:PPP2R3B)) View Subject | View Object

Appears in Networks:

p(HGNC:PPP2CA, pmod(Me, Leu, 309)) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:PPP2R3A)) View Subject | View Object

Appears in Networks:

p(HGNC:PPP2CA, pmod(Me, Leu, 309)) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:STRN3)) View Subject | View Object

Appears in Networks:

p(HGNC:PPP2CA, pmod(Me, Leu, 309)) increases complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(HGNC:STRN)) View Subject | View Object

Appears in Networks:

Evidence 0655c1b10f
JSON

Neither mutation of the carboxy-terminal Leu residue nor removal of the carboxy-terminal 14 amino acids of the catalytic subunit prevented formation of heterotrimeric holoenzymes involving the B or B′ subunits

p(HGNC:PPP2CA, var("?")) causesNoChange complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A regulatory subunit PR55")) View Subject | View Object

Appears in Networks:

p(HGNC:PPP2CA, var("?")) causesNoChange complex(p(HGNC:PPP2CA), p(HGNC:PPP2R1A), p(INTERPRO:"Protein phosphatase 2A, regulatory B subunit, B56")) View Subject | View Object

Appears in Networks:

Evidence 4dde02c9ee
JSON

Deletion of PTPA homologs in yeast, rrd1/rrd2, resulted in elevated levels of stable PP2A-PME-1 complexes, accompanied by decreased methylation

p(HGNC:PTPA) increases p(HGNC:PPP2CA, pmod(Me, Leu, 309)) View Subject | View Object

Appears in Networks:

p(HGNC:PTPA) decreases complex(a(GO:"protein phosphatase type 2A complex"), p(HGNC:PPME1)) View Subject | View Object

Appears in Networks:

Evidence f1fc6ac81a
JSON

The important interactions mediated by Arg418 and Val533 (corresponding to Val545 in the β isoform) provide a plausible explanation to the biochemical finding that these mutations crippled binding to the catalytic subunit

p(INTERPRO:"HEAT repeat", var("p.Arg418Trp")) decreases complex(p(HGNC:PPP2CA), p(INTERPRO:"HEAT repeat")) View Subject | View Object

Appears in Networks:

p(INTERPRO:"HEAT repeat", var("p.Val545Ala")) decreases complex(p(HGNC:PPP2CA), p(INTERPRO:"HEAT repeat")) View Subject | View Object

Appears in Networks:

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