Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo.

The EMBO journal - 1 Nov 2000

Wu J, Tolstykh T, Lee J, Boyd K, Stock J B, Broach J R

Abstract excerpt

The phosphoprotein phosphatase 2A (PP2A) catalytic subunit contains a methyl ester on its C-terminus, which in mammalian cells is added by a specific carboxyl methyltransferase and removed by a specific carboxyl methylesterase. We have identified genes in yeast that show significant homology to human carboxyl methyltransferase and methylesterase. Extracts of wild-type yeast cells contain carboxyl...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Drug Resistance, Microbial
Share to Methylation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Phosphoprotein Phosphatases

Share to Protein Methyltransferases

Share to Protein Phosphatase 2

Share to Protein Subunits

Share to Schizosaccharomyces pombe Proteins

Share to Sirolimus

Source

Open in PubMed Open full text

Identifiers

PMID: 11060018
DOI: 10.1093/emboj/19.21.5672
PMCID: PMC305778

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo.PMID 11060018Read ↗

Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity responsible for modification of the major forms of protein phosphatase 2A in yeast.Semantic proximity Read ↗

Effects of carboxyl-terminal methylation on holoenzyme function of the PP2A subfamily.Semantic proximity Read ↗

Methylation of protein phosphatase 2A-Influence of regulators and environmental stress factors.Semantic proximity Read ↗

A novel assay for protein phosphatase 2A (PP2A) complexes in vivo reveals differential effects of covalent modifications on different Saccharomyces cerevisiae PP2A heterotrimers.Semantic proximity Read ↗

Methylation of the C-terminal leucine residue of the PP2A catalytic subunit is unnecessary for the catalytic activity and the binding of regulatory subunit (PR55/B).Semantic proximity Read ↗

Functional expression of human PP2Ac in yeast permits the identification of novel C-terminal and dominant-negative mutant forms.Semantic proximity Read ↗

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

Mutation of the C-terminal leucine residue of PP2Ac inhibits PR55/B subunit binding and confers supersensitivity to microtubule destabilization in Saccharomyces cerevisiae.Semantic proximity Read ↗

Regulation of PP2A, PP4, and PP6 holoenzyme assembly by carboxyl-terminal methylationSemantic proximity Read ↗

A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo.Semantic proximity Read ↗

Expression of protein phosphatase 2A mutants and silencing of the regulatory B alpha subunit induce a selective loss of acetylated and detyrosinated microtubules.Semantic proximity Read ↗

Metal-dependent Ser/Thr protein phosphatase PPM family: Evolution, structures, diseases and inhibitors.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.