Evidence map›Paper›PMID 29244021›Full record

ArticleeLife2017

Diverse functions of homologous actin isoforms are defined by their nucleotide, rather than their amino acid sequence.

Pavan Vedula, Satoshi Kurosaka, Nicolae Adrian Leu, Yuri I Wolf, Svetlana A Shabalina, Junling Wang, Stephanie Sterling, Dawei W Dong, Anna Kashina

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

43 citing papers in PubMed, 65 citations in OpenAlex.

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  11. IL-2 delivery to CD8Nature communications · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Pavan Vedula *Department of Biomedical Sciences, University of Pennsylvania, Philadelphia, United States.ORCID https://orcid.org/0000-0002-9914-0008
Satoshi Kurosaka *Department of Biomedical Sciences, University of Pennsylvania, Philadelphia, United States.ORCID http://orcid.org/0000-0002-4365-9003
Nicolae Adrian LeuDepartment of Biomedical Sciences, University of Pennsylvania, Philadelphia, United States.
Yuri I WolfNational Center for Biotechnology Information, National Institutes of Health, Bethesda, United States.
Svetlana A ShabalinaNational Center for Biotechnology Information, National Institutes of Health, Bethesda, United States.
Junling WangDepartment of Biomedical Sciences, University of Pennsylvania, Philadelphia, United States.
Stephanie SterlingDepartment of Biomedical Sciences, University of Pennsylvania, Philadelphia, United States.
Dawei W DongDepartment of Biomedical Sciences, University of Pennsylvania, Philadelphia, United States.
Anna KashinaDepartment of Biomedical Sciences, University of Pennsylvania, Philadelphia, United States.ORCID http://orcid.org/0000-0002-0243-6866
University of Pennsylvania · USNational Institutes of Health · US

Funding

Regulation of cell migration by nucleotide coding sequence and arginylationR35GM122505 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Anna S Kashina · 2017 to 2026
$6.2M
Molecular Mechanisms of Protein ArginylationR01GM104003 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KASHINA, ANNA S · 2013 to 2016
$1.3M
NIGMS NIH HHS R01 GM104003NIGMS NIH HHS R35 GM122505NIH HHS GM104003NIH HHS GM117984
6 · The paper itself

Abstract

β- and γ-cytoplasmic actin are nearly indistinguishable in their amino acid sequence, but are encoded by different genes that play non-redundant biological roles. The key determinants that drive their functional distinction are unknown. Here, we tested the hypothesis that β- and γ-actin functions are defined by their nucleotide, rather than their amino acid sequence, using targeted editing of the mouse genome. Although previous studies have shown that disruption of β-actin gene critically impacts cell migration and mouse embryogenesis, we demonstrate here that generation of a mouse lacking β-actin protein by editing β-actin gene to encode γ-actin protein, and vice versa, does not affect cell migration and/or organism survival. Our data suggest that the essential in vivo function of β-actin is provided by the gene sequence independent of the encoded protein isoform. We propose that this regulation constitutes a global 'silent code' mechanism that controls the functional diversity of protein isoforms.

Indexed as

ActinsAmino Acid SequenceAnimalsBase SequenceGene EditingMiceProtein IsoformsActinsProtein Isoformsactinbiochemistrycell biologycoding sequenceisoformsmouse

Identifiers

PMID29244021
PMCPMC5794254
OpenAlexW2775774022

What OpenQuestion holds

Textmetadata
LicenceCC0
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.