Evidence map›Paper›PMID 36856076›Full record

ArticleThe FEBS journal2023

Functional molecular evolution of a GTP sensing kinase: PI5P4Kβ.

Koh Takeuchi, Miki Senda, Yoshiki Ikeda, Koji Okuwaki, Kaori Fukuzawa, So Nakagawa, Mika Sasaki, Atsuo T Sasaki, Toshiya Senda

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. Article
  3. Multimodal action of KRP203 on phosphoinositide kinases in vitro and in cells.Biochemical and biophysical research communications · 2023
    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

9 authors at 7 institutions in 2 countries.

Koh TakeuchiGraduate School of Pharmacological Sciences, The University of Tokyo, Japan.ORCID 0000-0002-6227-4627
Miki SendaStructural Biology Research Center, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Ibaraki, Japan.
Yoshiki IkedaDivision of Hematology and Oncology, Department of Internal Medicine, University of Cincinnati College of Medicine, OH, USA.
Koji OkuwakiGraduate School of Pharmaceutical Sciences, Osaka University, Japan.
Kaori FukuzawaGraduate School of Pharmaceutical Sciences, Osaka University, Japan.
So NakagawaDepartment of Molecular Life Science, Tokai University School of Medicine, Isehara, Japan.ORCID 0000-0003-1760-3839
Mika SasakiDivision of Hematology and Oncology, Department of Internal Medicine, University of Cincinnati College of Medicine, OH, USA.
Atsuo T SasakiDivision of Hematology and Oncology, Department of Internal Medicine, University of Cincinnati College of Medicine, OH, USA.ORCID 0000-0003-2963-4501
Toshiya SendaStructural Biology Research Center, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Ibaraki, Japan.ORCID 0000-0002-5153-928X
High Energy Accelerator Research Organization · JPOsaka University of Pharmaceutical Sciences · JPKansai Medical University · JPKeio University · JPThe University of Tokyo · JPTokai University · JPUniversity of Cincinnati Medical Center · US

Funding

Therapeutic resistance and aggressive malignancy in glioblastomas: the contribution of GTP metabolism through regulation by IMPDH2R01CA255331 · NCI · UNIVERSITY OF CINCINNATI · PI SASAKI, ATSUO · 2021 to 2025
$2.0M
Targeting the Novel PI5P4K Pathway to Induce Glioblastoma SenescenceR01NS089815 · NINDS · UNIVERSITY OF CINCINNATI · PI SASAKI, ATSUO · 2014 to 2018
$1.7M
Mechanistic role of phosphatidylinositol 5-phosphate 4-kinase beta in GTP-dependent lysosomal acidification for stress-resilient cell growth and metabolismR01GM144426 · NIGMS · UNIVERSITY OF CINCINNATI · PI Atsuo Sasaki · 2023 to 2026
$1.7M
NCI NIH HHS R01 CA255331NIGMS NIH HHS R01 GM144426NINDS NIH HHS R01 NS089815
6 · The paper itself

Abstract

Over 4 billion years of evolution, multiple mutations, including nucleotide substitutions, gene and genome duplications and recombination, have established de novo genes that translate into proteins with novel properties essential for high-order cellular functions. However, molecular processes through which a protein evolutionarily acquires a novel function are mostly speculative. Recently, we have provided evidence for a potential evolutionary mechanism underlying how, in mammalian cells, phosphatidylinositol 5-phosphate 4-kinase β (PI5P4Kβ) evolved into a GTP sensor from ATP-utilizing kinase. Mechanistically, PI5P4Kβ has acquired the guanine efficient association (GEA) motif by mutating its nucleotide base recognition sequence, enabling the evolutionary transition from an ATP-dependent kinase to a distinct GTP/ATP dual kinase with its K

Indexed as

Adenosine TriphosphateEvolution, MolecularAnimalsGuanosine TriphosphateMammalsAdenosine TriphosphateGuanosine Triphosphateenergy metabolismGTPGTP sensing kinasemolecular evolutionPI5P4Kβ

Identifiers

PMID36856076
PMCPMC10471773
OpenAlexW4322720394

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.