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Article

The structural basis for tight control of PP2A methylation and function by LCMT-1.

Molecular cell - 4 Feb 2011

Stanevich Vitali, Jiang Li, Satyshur Kenneth A, Li Yongfeng, Jeffrey Philip D, Li Zhu, Menden Patrick, Semmelhack Martin F, Xing Yongna

Abstract excerpt

Proper formation of protein phosphatase 2A (PP2A) holoenzymes is essential for the fitness of all eukaryotic cells. Carboxyl methylation of the PP2A catalytic subunit plays a critical role in regulating holoenzyme assembly; methylation is catalyzed by PP2A-specific methyltransferase LCMT-1, an enzyme required for cell survival. We determined crystal structures of human LCMT-1 in isolation and in complex with PP2A...

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Source

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Identifiers

PMID: 21292165
DOI: 10.1016/j.molcel.2010.12.030
PMCID: PMC3060061

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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