Evidence map›Paper›PMID 18042456›Full record

ArticleMolecular cell2007

Structure of the Pho85-Pho80 CDK-cyclin complex of the phosphate-responsive signal transduction pathway.

Kexin Huang, Ian Ferrin-O'Connell, Wei Zhang, Gordon A Leonard, Erin K O'Shea, Florante A Quiocho

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

30 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. TheFrontiers in microbiology · 2022
    Article
  5. A transcriptional activator fromFrontiers in microbiology · 2022
    Article
  6. Structural basis for CDK7 activation by MAT1 and Cyclin H.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. IPmBio · 2020
    Article
  8. A precisely positioned MED12 activation helix stimulates CDK8 kinase activity.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Review
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  12. Review
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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

6 authors at 3 institutions in 2 countries.

Kexin HuangVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Ian Ferrin-O'Connell
Wei Zhang
Gordon A Leonard
Erin K O'Shea
Florante A Quiocho
Baylor College of Medicine · USCenter for Systems Biology · USEuropean Synchrotron Radiation Facility · FR

Funding

REGULATION OF YEAST PHO5 GENER01GM051377 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI O'SHEA, ERIN K. · 1994 to 2011
$3.7M
FATTY ACID SYNTHASE: STRUCTURE, DYNAMICS AND FUNCTIONR01GM068826 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI QUIOCHO, FLORANTE A · 2004 to 2007
$1.9M
NIGMS NIH HHS GM051377NIGMS NIH HHS GM068826NIGMS NIH HHS R01 GM051377NIGMS NIH HHS R01 GM068826
6 · The paper itself

Abstract

The ability to sense and respond appropriately to environmental changes is a primary requirement of all living organisms. In response to phosphate limitation, Saccharomyces cerevisiae induces transcription of a set of genes involved in the regulation of phosphate acquisition from the ambient environment. A signal transduction pathway (the PHO pathway) mediates this response, with Pho85-Pho80 playing a vital role. Here we report the X-ray structure of Pho85-Pho80, a prototypic structure of a CDK-cyclin complex functioning in transcriptional regulation in response to environmental changes. The structure revealed a specific salt link between a Pho85 arginine and a Pho80 aspartate that makes phosphorylation of the Pho85 activation loop dispensable and that maintains a Pho80 loop conformation for possible substrate recognition. It further showed two sites on the Pho80 cyclin for high-affinity binding of the transcription factor substrate (Pho4) and the CDK inhibitor (Pho81) that are markedly distant to each other and the active site.

Indexed as

Binding SitesCrystallography, X-RayCyclin-Dependent KinasesCyclinsDNA-Binding ProteinsEnzyme ActivationEnzyme InhibitorsModels, MolecularMutant ProteinsPhenylalaninePhosphatesPhosphorylationProtein BindingProtein Structure, SecondaryRepressor ProteinsSaccharomyces cerevisiaeCyclin-Dependent KinasesCyclinsDNA-Binding ProteinsEnzyme InhibitorsMutant ProteinsPhenylalaninePHO4 protein, S cerevisiaePHO80 protein, S cerevisiaePHO81 protein, S cerevisiaePHO85 protein, S cerevisiaePhosphatesRepressor ProteinsSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID18042456
PMCPMC2175173
OpenAlexW1974814118

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.