Cited by 601Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingSignaling Pathways in Disease

Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation

Chen, Jian, Martin, Bruce L., Brautigan, David L.·1992·Science

Abstract

Extracellular signals that promote cell growth activate cascades of protein kinases. The kinases are dephosphorylated and deactivated by a single type-2A protein phosphatase. The catalytic subunit of type-2A protein phosphatase was phosphorylated by tyrosine-specific protein kinases. Phosphorylation was enhanced in the presence of the phosphatase inhibitor okadaic acid, consistent with an autodephosphorylation reaction. More than 90% of the activity of phosphatase 2A was lost when thioadenosine triphosphate was used to produce a thiophosphorylated protein resistant to autodephosphorylation. Phosphorylation in vitro occurred exclusively on Tyr307. Phosphorylation was catalyzed by p60v-src, p56lck, epidermal growth factor receptors, and insulin receptors. Transient deactivation of phosphatase 2A might enhance transmission of cellular signals through kinase cascades within cells.

Integrity signals

Registry

Crossref · 10.1126/science.1325671

Cites

38 of 38 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Chen, J., Martin, B. L., & Brautigan, D. L.
Affiliations
Brown University (US)
Venue
Science
Published
1992-08-28
Volume
257
Issue
5074
Pages
1261-1264
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1997664222
Cited by
601
References
38
Citations by year
2026: 3 · 2025: 6 · 2024: 5 · 2023: 7 · 2022: 10 · 2021: 14 · 2020: 13 · 2019: 17 · 2018: 9 · 2017: 25 · 2016: 26 · 2015: 23 · 2014: 31 · 2013: 30 · 2012: 38
FWCI
8.35
Type
journal article
Language
en
Open access
closed
Locations
  • Science (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 › Signaling Pathways in Disease
Keywords
protein phosphatase 2A, tyrosine phosphorylation, okadaic acid, p60v-src, Lck, epidermal growth factor receptor, insulin receptor, protein kinase cascades, signal transduction, catalytic subunit
MeSH terms
Animals, Ethers, Cyclic, Gene Expression Regulation, Humans, Phosphoprotein Phosphatases, Phosphorylation, Protein-Tyrosine Kinases, Rabbits, Receptor, Insulin, Thionucleotides, Tyrosine, Oncogene Protein pp60(v-src), Okadaic Acid, Lymphocyte Specific Protein Tyrosine Kinase p56(lck), Protein Phosphatase 2, ErbB Receptors, In Vitro Techniques

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review