Evidence map›Paper›PMID 24948787›Full record

ArticleG3 (Bethesda, Md.)2014

Proteomic analysis reveals CACN-1 is a component of the spliceosome in Caenorhabditis elegans.

Michael F Doherty, Guillaume Adelmant, Alyssa D Cecchetelli, Jarrod A Marto, Erin J Cram

Open access · goldAbstract read
In one paragraph

Article in G3 (Bethesda, Md.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

11 citing papers in PubMed, 13 citations in OpenAlex.

  1. microPublication biology · 2024
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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

5 authors at 3 institutions in 1 country.

Michael F DohertyBiology Department, Northeastern University, Boston, Massachusetts 02115.
Guillaume AdelmantDepartment of Cancer Biology and Blais Proteomics Center, Dana-Farber Cancer Institute, Boston, Massachusetts 02215 Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Alyssa D CecchetelliBiology Department, Northeastern University, Boston, Massachusetts 02115.
Jarrod A MartoDepartment of Cancer Biology and Blais Proteomics Center, Dana-Farber Cancer Institute, Boston, Massachusetts 02215 Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Erin J CramBiology Department, Northeastern University, Boston, Massachusetts 02115 e.cram@neu.edu.
Northeastern University · USDana-Farber Cancer Institute · USHarvard University · US

Funding

Transcriptional control of inhibitory synapse formationP01NS047572 · NINDS · DANA-FARBER CANCER INSTITUTE · PI STILES, CHARLES D · 2004 to 2013
$13.5M
Characterization of a novel regulator of cell migrationR01GM085077 · NIGMS · NORTHEASTERN UNIVERSITY · PI CRAM, ERIN JEAN · 2008 to 2012
$1.4M
NIGMS NIH HHS GM085077NIGMS NIH HHS R01 GM085077NINDS NIH HHS P01 NS047572NINDS NIH HHS P01NS047572
6 · The paper itself

Abstract

Cell migration is essential for embryonic development and tissue formation in all animals. cacn-1 is a conserved gene of unknown molecular function identified in a genome-wide screen for genes that regulate distal tip cell migration in the nematode worm Caenorhabditis elegans. In this study we take a proteomics approach to understand CACN-1 function. To isolate CACN-1-interacting proteins, we used an in vivo tandem-affinity purification strategy. Tandem-affinity purification-tagged CACN-1 complexes were isolated from C. elegans lysate, analyzed by mass spectrometry, and characterized bioinformatically. Results suggest significant interaction of CACN-1 with the C. elegans spliceosome. All of the identified interactors were screened for distal tip cell migration phenotypes using RNAi. Depletion of many of these factors led to distal tip cell migration defects, particularly a failure to stop migrating, a phenotype commonly seen in cacn-1 deficient animals. The results of this screen identify eight novel regulators of cell migration and suggest CACN-1 may participate in a protein network dedicated to high-fidelity gonad development. The composition of proteins comprising the CACN-1 network suggests that this critical developmental module may exert its influence through alternative splicing or other post-transcriptional gene regulation.

Indexed as

AnimalsAnimals, Genetically ModifiedCaenorhabditis elegansCaenorhabditis elegans ProteinsCell MovementNuclear ProteinsProtein Interaction MapsProteomicsRNA InterferenceSpliceosomesCACN-1 protein, C elegansCaenorhabditis elegans ProteinsNuclear ProteinsC. eleganscell migrationproteomicsspliceosome

Identifiers

PMID24948787
PMCPMC4132184
OpenAlexW2171327064

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.