Evidence map›Paper›PMID 31266884›Full record

ArticleLife science alliance2019

Systematic identification of recognition motifs for the hub protein LC8.

Nathan Jespersen, Aidan Estelle, Nathan Waugh, Norman E Davey, Cecilia Blikstad, York-Christoph Ammon, Anna Akhmanova, Ylva Ivarsson, David A Hendrix, Elisar Barbar

Abstract read
In one paragraph

Article in Life science alliance, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

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  8. Journal of chemical theory and computation · 2025
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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

10 authors.

Nathan JespersenDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, USA.ORCID 0000-0001-6931-1526
Aidan EstelleDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, USA.
Nathan WaughDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, USA.ORCID 0000-0003-0533-9225
Norman E DaveyConway Institute of Biomolecular and Biomedical Sciences, University College Dublin, Ireland.
Cecilia BlikstadDepartment of Chemistry - Biomedical Centre, Uppsala University, Uppsala, Sweden.ORCID 0000-0001-5740-926X
York-Christoph AmmonDepartment of Biology, Utrecht University, Utrecht, The Netherlands.
Anna AkhmanovaDepartment of Biology, Utrecht University, Utrecht, The Netherlands.
Ylva IvarssonDepartment of Chemistry - Biomedical Centre, Uppsala University, Uppsala, Sweden.
David A HendrixDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, USA.
Elisar BarbarDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, USA barbare@oregonstate.edu.ORCID 0000-0003-4892-5259

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 R01 GM084276
6 · The paper itself

Abstract

Hub proteins participate in cellular regulation by dynamic binding of multiple proteins within interaction networks. The hub protein LC8 reversibly interacts with more than 100 partners through a flexible pocket at its dimer interface. To explore the diversity of the LC8 partner pool, we screened for LC8 binding partners using a proteomic phage display library composed of peptides from the human proteome, which had no bias toward a known LC8 motif. Of the identified hits, we validated binding of 29 peptides using isothermal titration calorimetry. Of the 29 peptides, 19 were entirely novel, and all had the canonical TQT motif anchor. A striking observation is that numerous peptides containing the TQT anchor do not bind LC8, indicating that residues outside of the anchor facilitate LC8 interactions. Using both LC8-binding and nonbinding peptides containing the motif anchor, we developed the "LC8Pred" algorithm that identifies critical residues flanking the anchor and parses random sequences to predict LC8-binding motifs with ∼78% accuracy. Our findings significantly expand the scope of the LC8 hub interactome.

Indexed as

Protein Interaction Domains and MotifsAlgorithmsCalorimetryCell Cycle ProteinsCytoplasmic DyneinsHeLa CellsHumansMicrotubule-Associated ProteinsModels, MolecularPeptidesProtein BindingProteomicsThermodynamicsCell Cycle ProteinsCytoplasmic DyneinsDYNLL1 protein, humanFAM83D protein, humanMicrotubule-Associated ProteinsPeptides

Identifiers

PMID31266884
PMCPMC6607443

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Registered trials

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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.