Evidence map›Paper›PMID 34014523›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Dynamic Control of Signaling by Phosphorylation of PDZ Binding Motifs.

Márton A Simon, László Nyitray

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

2 authors at 1 institution in 1 country.

Márton A SimonDepartment of Biochemistry, ELTE Eötvös Loránd University, Budapest, Hungary.
László NyitrayDepartment of Biochemistry, ELTE Eötvös Loránd University, Budapest, Hungary. nyitray@elte.hu.
Eötvös Loránd University · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dynamic regulation of protein-protein interactions (PPIs) involves phosphorylation of short liner motifs in disordered protein regions modulating binding affinities. The ribosomal-S6-kinase 1 is capable of binding to scaffold proteins containing PDZ domains through a PDZ-binding motif (PBM) located at the disordered C-terminus of the kinase. Phosphorylation of the PBM dramatically changes the interactome of RSK1 with PDZ domains exerting a fine-tuning mechanism to regulate PPIs. Here we present in detail highly effective biophysical (fluorescence polarization, isothermal calorimetry) and cellular (protein-fragment complementation) methods to study the effect of phosphorylation on RSK1-PDZ interactions that can be also applied to investigate phosphoregulation of other PPIs in signaling pathways.

Indexed as

PDZ DomainsProtein Interaction Domains and MotifsBinding SitesFluorescence PolarizationHumansMicrotubule-Associated ProteinsPhosphorylationProtein BindingProtein Serine-Threonine KinasesRibosomal Protein S6 Kinases, 90-kDaSignal TransductionMAST2 protein, humanMicrotubule-Associated ProteinsProtein Serine-Threonine KinasesRibosomal Protein S6 Kinases, 90-kDaRPS6KA1 protein, humanBimolecular fragment complementation assayFluorescence polarizationIsothermal titration calorimetryNanoBiTPDZ domainProtein–protein interaction

Identifiers

PMID34014523
OpenAlexW3162970763

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.