Evidence map›Paper›PMID 7507203›Full record

ArticleMolecular and cellular biology1994

Tyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphatase.

M Autero, J Saharinen, T Pessa-Morikawa, M Soula-Rothhut, C Oetken, M Gassmann, M Bergman, K Alitalo, P Burn, C G Gahmberg

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
9.5field-weighted citation impact, top 1% 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

33 citing papers in PubMed, 131 citations in OpenAlex.

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  10. Extracellular domain dependence of PTPalpha transforming activity.Genes to cells : devoted to molecular & cellular mechanisms · 2010
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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

10 authors at 1 institution in 1 country.

M AuteroDepartment of Biochemistry, University of Helsinki, Finland.
J Saharinen
T Pessa-Morikawa
M Soula-Rothhut
C Oetken
M Gassmann
M Bergman
K Alitalo
P Burn
C G Gahmberg
University of Helsinki · FI

Funding

SRC FAMILY KINASES--FUNCTION AND REGULATION IN T-CELLSR29GM048960 · NIGMS · LA JOLLA INST FOR ALLERGY &IMMUNOLGY · PI MUSTELIN, TOMAS M · 1993 to 1997
–
NIGMS NIH HHS GM48960
6 · The paper itself

Abstract

Src family protein tyrosine kinases (PTKs) play an essential role in antigen receptor-initiated lymphocyte activation. Their activity is largely regulated by a negative regulatory tyrosine which is a substrate for the activating action of the CD45 phosphotyrosine phosphatase (PTPase) or, conversely, the suppressing action of the cytosolic p50csk PTK. Here we report that CD45 was phosphorylated by p50csk on two tyrosine residues, one of them identified as Tyr-1193. This residue was not phosphorylated by T-cell PTKs p56lck and p59fyn. Tyr-1193 was phosphorylated in intact T cells, and phosphorylation increased upon treatment with PTPase inhibitors, indicating that this tyrosine is a target for a constitutively active PTK. Cotransfection of CD45 and csk into COS-1 cells caused tyrosine phosphorylation of CD45 in the intact cells. Tyrosine-phosphorylated CD45 bound p56lck through the SH2 domain of the kinase. Finally, p50csk-mediated phosphorylation of CD45 caused a severalfold increase in its PTPase activity. Our results show that direct tyrosine phosphorylation of CD45 can affect its activity and association with Src family PTKs and that this phosphorylation could be mediated by p50csk. If this is also true in the intact cells, it adds a new dimension to the physiological function of p50csk in T lymphocytes.

Indexed as

src-Family KinasesAmino Acid SequenceAntigens, CDBinding SitesCells, CulturedCSK Tyrosine-Protein KinaseEnzyme ActivationHumansKineticsLeukocyte Common AntigensLymphocyte Specific Protein Tyrosine Kinase p56(lck)Models, BiologicalMolecular Sequence DataPeptide MappingPeptidesPhosphopeptidesAntigens, CDCSK protein, humanCSK Tyrosine-Protein KinaseLeukocyte Common AntigensLymphocyte Specific Protein Tyrosine Kinase p56(lck)PeptidesPhosphopeptidesPhosphotyrosineProtein-Tyrosine KinasesProtein Tyrosine Phosphatasessrc-Family KinasesTrypsinTyrosine

Identifiers

PMID7507203
PMCPMC358486
OpenAlexW1928261030

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.