Evidence map›Paper›PMID 34081539›Full record

ArticleMolecular biology of the cell2021

The dynein light chain protein Tda2 functions as a dimerization engine to regulate actin capping protein during endocytosis.

Andrew K Lamb, Andres N Fernandez, Olve B Peersen, Santiago M Di Pietro

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 31% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Andrew K LambDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870.
Andres N FernandezDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870.
Olve B PeersenDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870.
Santiago M Di PietroDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870.
Colorado State University · US

Funding

Molecular Mechanisms of Pigmentation in Health and DiseaseR01GM125619 · NIGMS · COLORADO STATE UNIVERSITY · PI DI PIETRO, SANTIAGO MAURO · 2018 to 2021
$1.4M
NIGMS NIH HHS R01 GM125619
6 · The paper itself

Abstract

Clathrin- and actin-mediated endocytosis is a fundamental process in eukaryotic cells. Previously, we discovered Tda2 as a new yeast dynein light chain (DLC) that works with Aim21 to regulate actin assembly during endocytosis. Here we show Tda2 functions as a dimerization engine bringing two Aim21 molecules together using a novel binding surface different than the canonical DLC ligand binding groove. Point mutations on either protein that diminish the Tda2-Aim21 interaction in vitro cause the same in vivo phenotype as

Indexed as

EndocytosisActin Capping ProteinsActin CytoskeletonCytoskeletal ProteinsProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActin Capping ProteinsAIM21 protein, S cerevisiaeCytoskeletal ProteinsSaccharomyces cerevisiae ProteinsTDA2 protein, S cerevisiae

Identifiers

PMID34081539
PMCPMC8351736
OpenAlexW3164574308

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.