Evidence map›Paper›PMID 24927537›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Mycobacterium tuberculosis supports protein tyrosine phosphorylation.

Ulrike Kusebauch, Corrie Ortega, Anja Ollodart, Richard S Rogers, David R Sherman, Robert L Moritz, Christoph Grundner

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 104 citations in OpenAlex.

  1. Structural insights into multitargetingMicrobiology spectrum · 2026
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  18. The domain architecture of PtkA, the first tyrosine kinase fromThe Journal of biological chemistry · 2018
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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

7 authors at 3 institutions in 1 country.

Ulrike KusebauchInstitute for Systems Biology, Seattle, WA 98109;
Corrie OrtegaSeattle Biomedical Research Institute, Seattle, WA 98109; andDepartment of Global Health, University of Washington, Seattle, WA, 98195.
Anja OllodartSeattle Biomedical Research Institute, Seattle, WA 98109; and.
Richard S RogersInstitute for Systems Biology, Seattle, WA 98109;
David R ShermanSeattle Biomedical Research Institute, Seattle, WA 98109; andDepartment of Global Health, University of Washington, Seattle, WA, 98195.
Robert L MoritzInstitute for Systems Biology, Seattle, WA 98109; robert.moritz@sytemsbiology.org christoph.grundner@seattlebiomed.org.
Christoph GrundnerSeattle Biomedical Research Institute, Seattle, WA 98109; andDepartment of Global Health, University of Washington, Seattle, WA, 98195 robert.moritz@sytemsbiology.org christoph.grundner@seattlebiomed.org.
Institute for Systems Biology · USCenter for Infectious Disease Research · USUniversity of Washington · US

Funding

Quantitative Systems BiologyP50GM076547 · NIGMS · INSTITUTE FOR SYSTEMS BIOLOGY · PI BALIGA, NITIN S · 2006 to 2016
$30.6M
Complete Human Peptide- and MRM-AtlasRC2HG005805 · NHGRI · INSTITUTE FOR SYSTEMS BIOLOGY · PI HOOD, LEROY E, MORITZ, ROBERT L · 2009 to 2010
$4.6M
FAIMS-Selected Reaction Monitoring to Quantitative Protein Networks in DiseaseS10RR027584 · NCRR · INSTITUTE FOR SYSTEMS BIOLOGY · PI MORITZ, ROBERT L · 2011 to 2011
$576k
NCRR NIH HHS S10 RR027584NHGRI NIH HHS R01 HG005805NHGRI NIH HHS RC2 HG005805NIGMS NIH HHS 2P50 GM076547NIGMS NIH HHS P50 GM076547PHS HHS 10802993
6 · The paper itself

Abstract

Reversible protein phosphorylation determines growth and adaptive decisions in Mycobacterium tuberculosis (Mtb). At least 11 two-component systems and 11 Ser/Thr protein kinases (STPKs) mediate phosphorylation on Asp, His, Ser, and Thr. In contrast, protein phosphorylation on Tyr has not been described previously in Mtb. Here, using a combination of phospho-enrichment and highly sensitive mass spectrometry, we show extensive protein Tyr phosphorylation of diverse Mtb proteins, including STPKs. Several STPKs function as dual-specificity kinases that phosphorylate Tyr in cis and in trans, suggesting that dual-specificity kinases have a major role in bacterial phospho-signaling. Mutation of a phosphotyrosine site of the essential STPK PknB reduces its activity in vitro and in live Mtb, indicating that Tyr phosphorylation has a functional role in bacterial growth. These data identify a previously unrecognized phosphorylation system in a human pathogen that claims ∼ 1.4 million lives every year.

Indexed as

Bacterial ProteinsHumansMutationMycobacterium tuberculosisPhosphorylationProtein Serine-Threonine KinasesSignal TransductionBacterial ProteinsPknB protein, Mycobacterium tuberculosisProtein Serine-Threonine Kinases

Identifiers

PMID24927537
PMCPMC4078798
OpenAlexW2117238181

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.