Evidence map›Paper›PMID 22998693›Full record

ArticleBiochemistry2012

Lack of Csk-mediated negative regulation in a unicellular SRC kinase.

Kira P Schultheiss, Hiroshi Suga, Iñaki Ruiz-Trillo, W Todd Miller

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. The Src module: an ancient scaffold in the evolution of cytoplasmic tyrosine kinases.Critical reviews in biochemistry and molecular biology · 2018
    Review
  6. Transfection ofDevelopment (Cambridge, England) · 2018
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Exploring the evolutionary history of centrosomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    Review
  14. Review
  15. 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

4 authors at 3 institutions in 2 countries.

Kira P SchultheissDepartment of Physiology and Biophysics, Stony Brook University, Stony Brook, NY 11794, USA.
Hiroshi Suga
Iñaki Ruiz-Trillo
W Todd Miller
Stony Brook University · USInstitució Catalana de Recerca i Estudis Avançats · ESInstitut de Biologia Evolutiva · ES

Funding

SUSTRATE SPECIFICITY OF NONRECEPTOR TYROSINE KINASER01CA058530 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI MILLER, W TODD · 1999 to 2018
$3.7M
SUBSTRATE SPECIFICITY OF NONRECEPTOR TYROSINE KINASESR29CA058530 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI MILLER, W TODD · 1993 to 1997
–
European Research Council 206883NCI NIH HHS CA58530NCI NIH HHS R01 CA058530
6 · The paper itself

Abstract

Phosphotyrosine-based signaling plays a vital role in cellular communication in multicellular organisms. Unexpectedly, unicellular choanoflagellates (the closest phylogenetic group to metazoans) possess numbers of tyrosine kinases that are comparable to those in complex metazoans. Here, we have characterized tyrosine kinases from the filasterean Capsaspora owczarzaki, a unicellular protist representing the sister group to choanoflagellates and metazoans. Two Src-like tyrosine kinases have been identified in C. owczarzaki (CoSrc1 and CoSrc2), both of which have the arrangement of SH3, SH2, and catalytic domains seen in mammalian Src kinases. In Capsaspora cells, CoSrc1 and CoSrc2 localize to punctate structures in filopodia that may represent primordial focal adhesions. We have cloned, expressed, and purified both enzymes. CoSrc1 and CoSrc2 are active tyrosine kinases. Mammalian Src kinases are normally regulated in a reciprocal fashion by autophosphorylation in the activation loop (which increases activity) and by Csk-mediated phosphorylation of the C-terminal tail (which inhibits activity). Similar to mammalian Src kinases, the enzymatic activities of CoSrc1 and CoSrc2 are increased by autophosphorylation in the activation loop. We have identified a Csk-like kinase (CoCsk) in the genome of C. owczarzaki. We cloned, expressed, and purified CoCsk and found that it has no measurable tyrosine kinase activity. Furthermore, CoCsk does not phosphorylate or regulate CoSrc1 or CoSrc2 in cells or in vitro, and CoSrc1 and CoSrc2 are active in Capsaspora cell lysates. Thus, the function of Csk as a negative regulator of Src family kinases appears to have arisen with the emergence of metazoans.

Indexed as

Amino Acid SequenceAnimalsBlotting, WesternCloning, MolecularCSK Tyrosine-Protein KinaseDNA, ComplementaryMolecular Sequence DataSequence Homology, Amino AcidSf9 Cellssrc-Family KinasesCSK Tyrosine-Protein KinaseDNA, Complementarysrc-Family Kinases

Identifiers

PMID22998693
PMCPMC3567254
OpenAlexW2048000913

What OpenQuestion holds

Textmetadata
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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.