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Mechanisms of the scaffold subunit in facilitating protein phosphatase 2A methylation.

The function of the biologically essential protein phosphatase 2A (PP2A) relies on formation of diverse heterotrimeric holoenzymes, which involves stable association between PP2A scaffold (A) and catalytic (C or PP2Ac) subunits and binding of variable regulatory subunits. Holoenzyme assembly is high... Full description

Journal Title: PloS one 2014, Vol.9(1), p.e86955
Main Author: Stanevich, Vitali
Other Authors: Zheng, Aiping , Guo, Feng , Jiang, Li , Wlodarchak, Nathan , Xing, Yongna
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0086955
Link: http://search.proquest.com/docview/1492707757/?pq-origsite=primo
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title: Mechanisms of the scaffold subunit in facilitating protein phosphatase 2A methylation.
format: Article
creator:
  • Stanevich, Vitali
  • Zheng, Aiping
  • Guo, Feng
  • Jiang, Li
  • Wlodarchak, Nathan
  • Xing, Yongna
subjects:
  • Blotting, Western–Chemistry
  • Calorimetry–Metabolism
  • Catalytic Domain–Metabolism
  • Fluorescence Resonance Energy Transfer–Chemistry
  • Hela Cells–Genetics
  • Holoenzymes–Metabolism
  • Humans–Metabolism
  • Methylation–Metabolism
  • Models, Molecular–Metabolism
  • Protein Conformation–Metabolism
  • Protein O-Methyltransferase–Metabolism
  • Protein Phosphatase 2–Metabolism
  • Protein Subunits–Metabolism
  • Static Electricity–Metabolism
  • Holoenzymes
  • Protein Subunits
  • Protein O-Methyltransferase
  • Leucine Carboxyl Methyltransferase-1, Human
  • Protein Phosphatase 2
ispartof: PloS one, 2014, Vol.9(1), p.e86955
description: The function of the biologically essential protein phosphatase 2A (PP2A) relies on formation of diverse heterotrimeric holoenzymes, which involves stable association between PP2A scaffold (A) and catalytic (C or PP2Ac) subunits and binding of variable regulatory subunits. Holoenzyme assembly is highly regulated by carboxyl methylation of PP2Ac-tail; methylation of PP2Ac and association of the A and C subunits are coupled to activation of PP2Ac. Here we showed that PP2A-specific methyltransferase, LCMT-1, exhibits a higher activity toward the core enzyme (A-C heterodimer) than free PP2Ac, and the A-subunit facilitates PP2A methylation via three distinct mechanisms: 1) stabilization of a proper protein fold and an active conformation of PP2Ac; 2) limiting the space of PP2Ac-tail movement for enhanced entry into the LCMT-1 active site; and 3) weak electrostatic interactions between LCMT-1 and the N-terminal HEAT repeats of the A-subunit. Our results revealed a new function and novel mechanisms of the A-subunit in PP2A methylation, and coherent control of PP2A activity, methylation, and holoenzyme assembly.
language: eng
source:
identifier: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0086955
fulltext: fulltext
issn:
  • 19326203
  • 1932-6203
url: Link


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titleMechanisms of the scaffold subunit in facilitating protein phosphatase 2A methylation.
creatorStanevich, Vitali ; Zheng, Aiping ; Guo, Feng ; Jiang, Li ; Wlodarchak, Nathan ; Xing, Yongna
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identifierE-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0086955
subjectBlotting, Western–Chemistry ; Calorimetry–Metabolism ; Catalytic Domain–Metabolism ; Fluorescence Resonance Energy Transfer–Chemistry ; Hela Cells–Genetics ; Holoenzymes–Metabolism ; Humans–Metabolism ; Methylation–Metabolism ; Models, Molecular–Metabolism ; Protein Conformation–Metabolism ; Protein O-Methyltransferase–Metabolism ; Protein Phosphatase 2–Metabolism ; Protein Subunits–Metabolism ; Static Electricity–Metabolism ; Holoenzymes ; Protein Subunits ; Protein O-Methyltransferase ; Leucine Carboxyl Methyltransferase-1, Human ; Protein Phosphatase 2
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descriptionThe function of the biologically essential protein phosphatase 2A (PP2A) relies on formation of diverse heterotrimeric holoenzymes, which involves stable association between PP2A scaffold (A) and catalytic (C or PP2Ac) subunits and binding of variable regulatory subunits. Holoenzyme assembly is highly regulated by carboxyl methylation of PP2Ac-tail; methylation of PP2Ac and association of the A and C subunits are coupled to activation of PP2Ac. Here we showed that PP2A-specific methyltransferase, LCMT-1, exhibits a higher activity toward the core enzyme (A-C heterodimer) than free PP2Ac, and the A-subunit facilitates PP2A methylation via three distinct mechanisms: 1) stabilization of a proper protein fold and an active conformation of PP2Ac; 2) limiting the space of PP2Ac-tail movement for enhanced entry into the LCMT-1 active site; and 3) weak electrostatic interactions between LCMT-1 and the N-terminal HEAT repeats of the A-subunit. Our results revealed a new function and novel mechanisms of the A-subunit in PP2A methylation, and coherent control of PP2A activity, methylation, and holoenzyme assembly.
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