Evidence map›Paper›PMID 33674566›Full record

ArticleNature communications2021

De novo design of a reversible phosphorylation-dependent switch for membrane targeting.

Leon Harrington, Jordan M Fletcher, Tamara Heermann, Derek N Woolfson, Petra Schwille

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Chemically active wetting.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Review
  6. Review
  7. Article
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  18. DE-STRESS: a user-friendly web application for the evaluation of protein designs.Protein engineering, design & selection : PEDS · 2021
    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

5 authors.

Leon HarringtonDepartment of Molecular and Cellular Biophysics, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany.ORCID http://orcid.org/0000-0002-6781-2367
Jordan M FletcherSchool of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.
Tamara HeermannDepartment of Molecular and Cellular Biophysics, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany.ORCID http://orcid.org/0000-0003-1607-0727
Derek N WoolfsonSchool of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK. d.n.woolfson@bristol.ac.uk.ORCID http://orcid.org/0000-0002-0394-3202
Petra SchwilleDepartment of Molecular and Cellular Biophysics, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany. schwille@biochem.mpg.de.ORCID http://orcid.org/0000-0002-6106-4847

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X1
6 · The paper itself

Abstract

Modules that switch protein-protein interactions on and off are essential to develop synthetic biology; for example, to construct orthogonal signaling pathways, to control artificial protein structures dynamically, and for protein localization in cells or protocells. In nature, the E. coli MinCDE system couples nucleotide-dependent switching of MinD dimerization to membrane targeting to trigger spatiotemporal pattern formation. Here we present a de novo peptide-based molecular switch that toggles reversibly between monomer and dimer in response to phosphorylation and dephosphorylation. In combination with other modules, we construct fusion proteins that couple switching to lipid-membrane targeting by: (i) tethering a 'cargo' molecule reversibly to a permanent membrane 'anchor'; and (ii) creating a 'membrane-avidity switch' that mimics the MinD system but operates by reversible phosphorylation. These minimal, de novo molecular switches have potential applications for introducing dynamic processes into designed and engineered proteins to augment functions in living cells and add functionality to protocells.

Indexed as

Cell MembraneDimerizationEscherichia coliKineticsPeptidesPhosphorylationProtein EngineeringSignal TransductionSynthetic BiologyPeptides

Identifiers

PMID33674566
PMCPMC7935970

What OpenQuestion holds

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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.