Evidence map›Paper›PMID 25310241›Full record

ArticleeLife2014

Ancestral resurrection reveals evolutionary mechanisms of kinase plasticity.

Conor J Howard, Victor Hanson-Smith, Kristopher J Kennedy, Chad J Miller, Hua Jane Lou, Alexander D Johnson, Benjamin E Turk, Liam J Holt

Abstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
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

34 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Saturation mutagenesis of a predicted ancestral Syk-family kinase.Protein science : a publication of the Protein Society · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

8 authors.

Conor J HowardDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
Victor Hanson-SmithDepartment of Microbiology and Immunology, University of California, San Francisco, San Francisco, United States.
Kristopher J KennedyDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
Chad J MillerDepartment of Pharmacology, Yale University School of Medicine, New Haven, United States.
Hua Jane LouDepartment of Pharmacology, Yale University School of Medicine, New Haven, United States.
Alexander D JohnsonDepartment of Microbiology and Immunology, University of California, San Francisco, San Francisco, United States.
Benjamin E TurkDepartment of Pharmacology, Yale University School of Medicine, New Haven, United States.
Liam J HoltDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.ORCID http://orcid.org/0000-0002-4002-0861

Funding

MECHANISMS OF YEAST TRANSCRIPTIONAL REGULATORSR01GM037049 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JOHNSON, ALEXANDER D · 1986 to 2024
$9.4M
INSTITUTIONAL NATIONAL RESEARCH SERVICE AWARDT32GM007324 · NIGMS · YALE UNIVERSITY · PI BENNETT, ANTON M · 1987 to 2022
$6.2M
Modeling human phosphorylation networks through kinome-wide profilingR01GM104047 · NIGMS · YALE UNIVERSITY · PI TURK, BENJAMIN E, YAFFE, MICHAEL B · 2013 to 2017
$2.4M
Phosphorylation networks regulated by energy stress in yeastR01GM105947 · NIGMS · YALE UNIVERSITY · PI TURK, BENJAMIN E · 2013 to 2016
$1.3M
NIGMS NIH HHS GM037049NIGMS NIH HHS R01 GM037049NIGMS NIH HHS R01 GM104047NIGMS NIH HHS R01 GM105947NIGMS NIH HHS T32 GM007324
6 · The paper itself

Abstract

Protein kinases have evolved diverse specificities to enable cellular information processing. To gain insight into the mechanisms underlying kinase diversification, we studied the CMGC protein kinases using ancestral reconstruction. Within this group, the cyclin dependent kinases (CDKs) and mitogen activated protein kinases (MAPKs) require proline at the +1 position of their substrates, while Ime2 prefers arginine. The resurrected common ancestor of CDKs, MAPKs, and Ime2 could phosphorylate substrates with +1 proline or arginine, with preference for proline. This specificity changed to a strong preference for +1 arginine in the lineage leading to Ime2 via an intermediate with equal specificity for proline and arginine. Mutant analysis revealed that a variable residue within the kinase catalytic cleft, DFGx, modulates +1 specificity. Expansion of Ime2 kinase specificity by mutation of this residue did not cause dominant deleterious effects in vivo. Tolerance of cells to new specificities likely enabled the evolutionary divergence of kinases.

Indexed as

Evolution, MolecularPhylogenyAmino Acid SequenceAnimalsArginineCyclinsHumansKineticsMeiosisMolecular Sequence DataMutationPeptidesPhosphorylationProlineProtein KinasesSaccharomyces cerevisiaeArginineCyclinsPeptidesProlineProtein Kinasesancestral reconstructionbiochemistrycyclin-dependent kinaseevolutionevolutionary biologygenomicshumanIme2mouseneurosporaphosphoregulatory networksprotein kinaseS. cerevisiae

Identifiers

PMID25310241
PMCPMC4228266

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.