Evidence map›Paper›PMID 22545154›Full record

ArticlePloS one2012

Structure of an enzyme-derived phosphoprotein recognition domain.

Christopher A Johnston, Chris Q Doe, Kenneth E Prehoda

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Metamorphic protein folding as evolutionary adaptation.Trends in biochemical sciences · 2023
    Review
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  6. Review
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  12. Article
  13. Cell Fate Decision Making through Oriented Cell Division.Journal of developmental biology · 2015
    Article
  14. Epithelial homeostasis.Current biology : CB · 2014
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

3 authors at 1 institution in 1 country.

Christopher A JohnstonInstitute of Molecular Biology, University of Oregon, Eugene, Oregon, United States of America.
Chris Q Doe
Kenneth E Prehoda
University of Oregon · US

Funding

Regulated spindle orientation during asymmetric cell divisionR01GM087457 · NIGMS · UNIVERSITY OF OREGON · PI PREHODA, KENNETH E · 2010 to 2013
$1.3M
NIGMS NIH HHS GM087457NIGMS NIH HHS R01 GM087457
6 · The paper itself

Abstract

Membrane Associated Guanylate Kinases (MAGUKs) contain a protein interaction domain (GK(dom)) derived from the enzyme Guanylate Kinase (GK(enz)). Here we show that GK(dom) from the MAGUK Discs large (Dlg) is a phosphoprotein recognition domain, specifically recognizing the phosphorylated form of the mitotic spindle orientation protein Partner of Inscuteable (Pins). We determined the structure of the Dlg-Pins complex to understand the dramatic transition from nucleotide kinase to phosphoprotein recognition domain. The structure reveals that the region of the GK(dom) that once served as the GMP binding domain (GBD) has been co-opted for protein interaction. Pins makes significantly more contact with the GBD than does GMP, but primarily with residues that are conserved between enzyme and domain revealing the versatility of the GBD as a platform for nucleotide and protein interactions. Mutational analysis reveals that the GBD is also used to bind the GK ligand MAP1a, suggesting that this is a common mode of MAGUK complex assembly. The GK(enz) undergoes a dramatic closing reaction upon GMP binding but the protein-bound GK(dom) remains in the 'open' conformation indicating that the dramatic conformational change has been lost in the conversion from nucleotide kinase to phosphoprotein recognition domain.

Indexed as

Protein Interaction Domains and MotifsAmino Acid SequenceAnimalsCell LineGuanylate KinasesHumansModels, MolecularMolecular Sequence DataPhosphoproteinsProtein BindingGuanylate KinasesPhosphoproteins

Identifiers

PMID22545154
PMCPMC3335814
OpenAlexW2075023218

What OpenQuestion holds

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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.