Structure of the Protein Phosphatase 2A Holoenzyme

Xu, Yanhui; Xing, Yongna; Chen, Yu; Chao, Yang; Lin, Zheng; Fan, Eugene; Yu, Jong W.; Strack, Stefan; Jeffrey, Philip D.; Shi, Yigong

doi:10.1016/j.cell.2006.11.033

Cited by 450Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingProtein Structure and Dynamics

Structure of the Protein Phosphatase 2A Holoenzyme

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Xu, Yanhui, Xing, Yongna, Chen, Yu, Chao, Yang, Lin, Zheng, Fan, Eugene, Yu, Jong W., Strack, Stefan +2 more·2006·Cell

DOI 10.1016/j.cell.2006.11.033

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Abstract

Protein Phosphatase 2A (PP2A) plays an essential role in many aspects of cellular physiology. The PP2A holoenzyme consists of a heterodimeric core enzyme, which comprises a scaffolding subunit and a catalytic subunit, and a variable regulatory subunit. Here we report the crystal structure of the heterotrimeric PP2A holoenzyme involving the regulatory subunit B'/B56/PR61. Surprisingly, the B'/PR61 subunit has a HEAT-like (huntingtin-elongation-A subunit-TOR-like) repeat structure, similar to that of the scaffolding subunit. The regulatory B'/B56/PR61 subunit simultaneously interacts with the catalytic subunit as well as the conserved ridge of the scaffolding subunit. The carboxyterminus of the catalytic subunit recognizes a surface groove at the interface between the B'/B56/PR61 subunit and the scaffolding subunit. Compared to the scaffolding subunit in the PP2A core enzyme, formation of the holoenzyme forces the scaffolding subunit to undergo pronounced conformational rearrangements. This structure reveals significant ramifications for understanding the function and regulation of PP2A.

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B56α and PP2Ac do not constitute a stable dimer without any scaffolding protein.
“B56α and PP2Ac, which do not constitute a stable dimer without any scaffolding protein40,41.”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [40]
The hypothetical surface area which CIP2A(1-560) could cover on B56α based on cross-link sites is highly overlapping with known sites involved in B56α interaction with the A-subunit.
“Interestingly, comparison of the hypothetical surface area which CIP2A(1-560) could cover on B56α based on the cross-link sites (Fig. 4A, red), to the known sites involved in B56α interaction with the A-subunit (Fig. 4A, purple)40,41, revealed that these surface areas are highly overlapping (Fig. 4A, right panel, shaded circle).”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [40]

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Authors: Xu, Y., Xing, Y., Chen, Y., Chao, Y., Lin, Z., Fan, E., Yu, J. W., Strack, S., Jeffrey, P. D., & Shi, Y.
Affiliations: Princeton University (US)
University of Iowa (US)
Corresponding author: Shi, Yigong
ORCID: Xu, Yanhui
Xing, Yongna
Yu, Jong W.
Strack, Stefan
Jeffrey, Philip D.
Shi, Yigong
Venue: Cell
Publisher: Elsevier BV
Published: 2006-12
Volume: 127
Issue: 6
Pages: 1239-1251
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2006.11.033
OpenAlex: W2126361876
Cited by: 450
References: 53
Citations by year: 2026: 16 · 2025: 16 · 2024: 15 · 2023: 19 · 2022: 17 · 2021: 29 · 2020: 33 · 2019: 21 · 2018: 15 · 2017: 34 · 2016: 15 · 2015: 21 · 2014: 22 · 2013: 23 · 2012: 24
FWCI: 10.73
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2456 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: protein phosphatase 2A, PP2A holoenzyme, crystal structure, catalytic subunit, HEAT repeats, conformational change, protein-protein interaction, enzyme regulation
MeSH terms: Amino Acid Sequence, Humans, Methylation, Models, Molecular, Molecular Sequence Data, Phosphoprotein Phosphatases, Protein Conformation, Software, Sequence Alignment, Protein Structure, Tertiary, Crystallography, X-Ray, Holoenzymes, Catalytic Domain, Multiprotein Complexes, Protein Phosphatase 2

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Structure of the Protein Phosphatase 2A Holoenzyme

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Integrity signals

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