Evidence map›Paper›PMID 25263009›Full record

ReviewSeminars in cell & developmental biology2015

Polybivalency and disordered proteins in ordering macromolecular assemblies.

Elisar Barbar, Afua Nyarko

Open access · greenAbstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2015. 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
1.6field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
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  8. Review
  9. Article
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  11. Article
  12. Intrinsic protein disorder in oncogenic KRAS signaling.Cellular and molecular life sciences : CMLS · 2017
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Dynein and intraflagellar transport.Experimental cell research · 2015
    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

2 authors at 1 institution in 1 country.

Elisar BarbarDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, United States. Electronic address: barbare@science.oregonstate.edu.
Afua NyarkoDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, United States.
Oregon State University · US

Funding

Dynein light chain as a dimerization hub for natively disordered proteinsR01GM084276 · NIGMS · OREGON STATE UNIVERSITY · PI BARBAR, ELISAR J · 2009 to 2013
$1.5M
NIGMS NIH HHS GM 084276NIGMS NIH HHS R01 GM084276
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) are prevalent in macromolecular assemblies and are thought to mediate protein recognition in complex regulatory processes and signaling pathways. The formation of a polybivalent scaffold is a key process by which IDPs drive early steps in macromolecular assemblies. Three intrinsically disordered proteins, IC, Swallow and Nup159, are core components, respectively, of cytoplasmic dynein, bicoid mRNA localization apparatus, and nuclear pore complexes. In all three systems, the hub protein LC8 recognizes on the IDP, short linear motifs that are fully disordered in the apo form, but adopt a β-strand when bound to LC8. The IDP/LC8 complex forms a bivalent scaffold primed to bind additional bivalent ligands. Scaffold formation also promotes self-association and/or higher order organization of the IDP components at a site distant from LC8 binding. Rigorous thermodynamic analyses imply that association of additional bivalent ligands is driven by entropic effects where the first binding event is weak but subsequent binding of additional ligands occurs with higher affinity. Here, we review specific examples of macromolecular assemblies in which polybivalency of aligned IDP duplexes not only enhances binding affinity and results in formation of a stable complex but also compensates unfavorable steric and enthalpic interactions. We propose that polybivalent scaffold assembly involving IDPs and LC8-like proteins is a general process in the cell biology of a class of multi-protein structures that are stable yet fine-tuned for diverse cellular requirements.

Indexed as

AnimalsCell Physiological PhenomenaCytoplasmic DyneinsIntrinsically Disordered ProteinsMultiprotein ComplexesSignal TransductionThermodynamicsCytoplasmic DyneinsIntrinsically Disordered ProteinsMultiprotein ComplexesBivalencyEnthalpy–entropy compensationIntrinsically disordered proteinsLC8Macromolecular assemblyPoly-bivalent scaffold

Identifiers

PMID25263009
PMCPMC4339520
OpenAlexW2041721668

What OpenQuestion holds

Textmetadata
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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.