Evidence map›Paper›PMID 29599515›Full record

ArticleScientific reports2018

Src signaling in a low-complexity unicellular kinome.

Hiroshi Suga, W Todd Miller

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Structure, Function, and Regulation of the SRMS Tyrosine Kinase.International journal of molecular sciences · 2020
    Review
  6. Review
  7. The Src module: an ancient scaffold in the evolution of cytoplasmic tyrosine kinases.Critical reviews in biochemistry and molecular biology · 2018
    Review
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

2 authors at 2 institutions in 2 countries.

Hiroshi SugaFaculty of Life and Environmental Sciences, Prefectural University of Hiroshima, 727-0023, Shobara, Hiroshima, Japan. hsuga@pu-hiroshima.ac.ap.
W Todd MillerDepartment of Physiology and Biophysics, Stony Brook University, Stony Brook, NY, 11794, USA. todd.miller@stonybrook.edu.
Prefectural University of Hiroshima · JPStony Brook University · US

Funding

SUSTRATE SPECIFICITY OF NONRECEPTOR TYROSINE KINASER01CA058530 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI MILLER, W TODD · 1999 to 2018
$3.7M
NCI NIH HHS R01 CA058530
6 · The paper itself

Abstract

Creolimax fragrantissima is a member of the ichthyosporean clade, the earliest branching holozoan lineage. The kinome of Creolimax is markedly reduced as compared to those of metazoans. In particular, Creolimax possesses a single non-receptor tyrosine kinase: CfrSrc, the homolog of c-Src kinase. CfrSrc is an active tyrosine kinase, and it is expressed throughout the lifecycle of Creolimax. In animal cells, the regulatory mechanism for Src involves tyrosine phosphorylation at a C-terminal site by Csk kinase. The lack of Csk in Creolimax suggests that a different mode of negative regulation must exist for CfrSrc. We demonstrate that CfrPTP-3, one of the 7 tyrosine-specific phosphatases (PTPs) in Creolimax, suppresses CfrSrc activity in vitro and in vivo. Transcript levels of CfrPTP-3 and two other PTPs are significantly higher than that of CfrSrc in the motile amoeboid and sessile multinucleate stages of the Creolimax life cycle. Thus, in the context of a highly reduced kinome, a pre-existing PTP may have been co-opted for the role of Src regulation. Creolimax represents a unique model system to study the adaptation of tyrosine kinase signaling and regulatory mechanisms.

Indexed as

AnimalsBinding SitesCSK Tyrosine-Protein KinaseMesomycetozoeaPhosphorylationProtein Tyrosine PhosphatasesSignal Transductionsrc-Family KinasesTyrosineCSK Tyrosine-Protein KinaseProtein Tyrosine Phosphatasessrc-Family KinasesTyrosine

Identifiers

PMID29599515
PMCPMC5876402
OpenAlexW2795285576

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.