Evidence map›Paper›PMID 25565106›Full record

ArticleStructure (London, England : 1993)2015

Single-molecule FRET reveals hidden complexity in a protein energy landscape.

Maksym Tsytlonok, Shehu M Ibrahim, Pamela J E Rowling, Wenshu Xu, Maria J Ruedas-Rama, Angel Orte, David Klenerman, Laura S Itzhaki

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Structure (London, England : 1993), 2015. 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
–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

3 citing papers in PubMed.

  1. Fluorescent Probes for STED Optical Nanoscopy.Nanomaterials (Basel, Switzerland) · 2021
    Review
  2. Article
  3. 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

8 authors.

Maksym TsytlonokMRC Cancer Cell Unit, Hutchison/MRC Research Centre, Hills Road, Cambridge CB2 0XZ, UK; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Shehu M IbrahimDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Pamela J E RowlingDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK; Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, UK.
Wenshu XuDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK; Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, UK.
Maria J Ruedas-RamaDepartment of Physical Chemistry, Faculty of Pharmacy, Campus Cartuja, University of Granada, 18071 Granada, Spain.
Angel OrteDepartment of Physical Chemistry, Faculty of Pharmacy, Campus Cartuja, University of Granada, 18071 Granada, Spain.
David KlenermanDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK. Electronic address: dk10012@cam.ac.uk.
Laura S ItzhakiDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK; Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, UK. Electronic address: lsi10@cam.ac.uk.

Funding

Medical Research Council G1002329MRF_ C0385
6 · The paper itself

Abstract

Here, using single-molecule FRET, we reveal previously hidden conformations of the ankyrin-repeat domain of AnkyrinR, a giant adaptor molecule that anchors integral membrane proteins to the spectrin-actin cytoskeleton through simultaneous binding of multiple partner proteins. We show that the ankyrin repeats switch between high-FRET and low-FRET states, controlled by an unstructured "safety pin" or "staple" from the adjacent domain of AnkyrinR. Opening of the safety pin leads to unravelling of the ankyrin repeat stack, a process that will dramatically affect the relative orientations of AnkyrinR binding partners and, hence, the anchoring of the spectrin-actin cytoskeleton to the membrane. Ankyrin repeats are one of the most ubiquitous molecular recognition platforms in nature, and it is therefore important to understand how their structures are adapted for function. Our results point to a striking mechanism by which the order-disorder transition and, thereby, the activity of repeat proteins can be regulated.

Indexed as

Fluorescence Resonance Energy TransferAnkyrin RepeatAnkyrinsCrystallography, X-RayHumansModels, MolecularMutant ProteinsMutationProtein Structure, TertiaryANK1 protein, humanAnkyrinsMutant Proteins

Identifiers

PMID25565106
PMCPMC4291146

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.