Evidence map›Paper›PMID 8491187›Full record

ArticleThe EMBO journal1993

Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation.

A J Flint, M F Gebbink, B R Franza, D E Hill, N K Tonks

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
6.6field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

45 citing papers in PubMed, 158 citations in OpenAlex.

  1. Review
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  9. Article
  10. Review
  11. S-Nitrosation ofFrontiers in plant science · 2022
    Article
  12. Review
  13. Protein-tyrosine phosphatase 1B substrates and metabolic regulation.Seminars in cell & developmental biology · 2015
    Review
  14. Article
  15. Review
  16. PTP1B: a double agent in metabolism and oncogenesis.Trends in biochemical sciences · 2010
    Review
  17. Article
  18. Article
  19. VCAM-1 activation of endothelial cell protein tyrosine phosphatase 1B.Journal of immunology (Baltimore, Md. : 1950) · 2007
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

A J FlintCold Spring Harbor Laboratory, NY 11724.
M F Gebbink
B R Franza
D E Hill
N K Tonks
Cold Spring Harbor Laboratory · US

Funding

PROTEIN TYROSINE DEPHOSPHORYLATION &SIGNAL TRANSDUCTIONR01CA053840 · NCI · COLD SPRING HARBOR LABORATORY · PI TONKS, NICHOLAS K · 1991 to 2025
$11.8M
Protein Tyrosine Dephosphorylation &signal TransductionR37CA053840 · NCI · COLD SPRING HARBOR LABORATORY · PI TONKS, NICHOLAS K · 2001 to 2008
$5.2M
IDENTIFICATION OF CELL CYCLE SPECIFIC PROTEINS AFFECTEDR01CA040512 · NCI · COLD SPRING HARBOR LABORATORY · PI FRANZA, B ROBERT · 1985 to 1994
–
NCI NIH HHS CA40512NCI NIH HHS CA53840
6 · The paper itself

Abstract

The non-transmembrane protein tyrosine phosphatase, PTP1B, comprises 435 amino acids, of which the C-terminal 114 residues have been implicated in controlling both localization and function of this enzyme. Inspection of the sequence of the C-terminal segment reveals a number of potential sites of phosphorylation. We show that PTP1B is phosphorylated on seryl residues in vivo. Increased phosphorylation of PTP1B is seen to accompany the transition from G2 to M phase of the cell cycle. Two major tryptic phosphopeptides appear in two-dimensional maps of PTP1B from mitotic cells. One of these comigrates with the peptide generated following phosphorylation of PTP1B in vitro at Ser386 by the mitotic protein Ser/Thr kinase p34cdc2:cyclin B. The site of phosphorylation that is responsible for the pronounced retardation in the electrophoretic mobility of PTP1B from mitotic cells has been identified by site directed mutagenesis as Ser352. The identify of the kinase responsible for this modification is presently unknown. We also show that stimulation of HeLa cells with the phorbol ester TPA enhances phosphorylation of PTP1B. Two dimensional phosphopeptide mapping reveals that the bulk of the phosphate is in a single tryptic peptide. The site, identified as Ser378, is also the site of phosphorylation by protein kinase C (PKC) in vitro. Thus the TPA-stimulated phosphorylation of PTP1B in vivo appears to result directly from phosphorylation by PKC. The effect of phosphorylation on the activity of PTP1B has been examined in immunoprecipitates from TPA-treated and nocodazole-arrested cells. TPA treatment does not appear to affect activity directly, whereas the activity of PTP1B from nocodazole-arrested cells is only 70% of that from asynchronous populations.

Indexed as

AlanineAmino Acid SequenceCDC2 Protein KinaseCell CycleElectrophoresis, Polyacrylamide GelHeLa CellsHumansMolecular Sequence DataMutationPhosphorylationProtein Kinase CProtein Tyrosine PhosphatasesSerineTetradecanoylphorbol AcetateAlanineCDC2 Protein KinaseProtein Kinase CProtein Tyrosine PhosphatasesSerineTetradecanoylphorbol Acetate

Identifiers

PMID8491187
PMCPMC413415
OpenAlexW1950041808

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.