Evidence map›Paper›PMID 25036633›Full record

ArticleCell2014

APC is an RNA-binding protein, and its interactome provides a link to neural development and microtubule assembly.

Nicolas Preitner, Jie Quan, Dan W Nowakowski, Melissa L Hancock, Jianhua Shi, Joseph Tcherkezian, Tracy L Young-Pearse, John G Flanagan

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
8.5field-weighted citation impact, top 2% 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

114 citing papers in PubMed, 181 citations in OpenAlex.

  1. Article
  2. APC in the nervous system.Medical molecular morphology · 2026
    Review
  3. The KIF6-RBP Complex Orchestrates mRNA Transport Required for Sperm Flagellar Assembly.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
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54 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Nicolas PreitnerDepartment of Cell Biology and Program in Neuroscience, Harvard Medical School, Boston, MA 02115, USA.
Jie QuanDepartment of Cell Biology and Program in Neuroscience, Harvard Medical School, Boston, MA 02115, USA.
Dan W NowakowskiDepartment of Cell Biology and Program in Neuroscience, Harvard Medical School, Boston, MA 02115, USA.
Melissa L HancockDepartment of Cell Biology and Program in Neuroscience, Harvard Medical School, Boston, MA 02115, USA.
Jianhua ShiDepartment of Cell Biology and Program in Neuroscience, Harvard Medical School, Boston, MA 02115, USA.
Joseph TcherkezianLaboratory for Therapeutic Development, Rosalind and Morris Goodman Cancer Research Centre, McGill University, Montreal, QC H3G 1Y6, Canada.
Tracy L Young-PearseCenter for Neurologic Diseases, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.
John G FlanaganDepartment of Cell Biology and Program in Neuroscience, Harvard Medical School, Boston, MA 02115, USA. Electronic address: flanagan@hms.harvard.edu.
Harvard University · USMcGill University Health Centre · CA

Funding

CELL-CELL SIGNALING IN VISUAL DEVELOPMENTR01EY011559 · NEI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FLANAGAN, JOHN G · 1996 to 2016
$6.9M
Signal transduction in axon guidanceR01NS069913 · NINDS · HARVARD MEDICAL SCHOOL · PI John G Flanagan · 2011 to 2026
$4.5M
Identification and Function of Receptors and LigandsR37HD029417 · NICHD · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FLANAGAN, JOHN G · 2002 to 2011
$4.0M
NEI NIH HHS R01 EY011559NICHD NIH HHS R37 HD029417NINDS NIH HHS R01 NS069913
6 · The paper itself

Abstract

Adenomatous polyposis coli (APC) is a microtubule plus-end scaffolding protein important in biology and disease. APC is implicated in RNA localization, although the mechanisms and functional significance remain unclear. We show APC is an RNA-binding protein and identify an RNA interactome by HITS-CLIP. Targets were highly enriched for APC-related functions, including microtubule organization, cell motility, cancer, and neurologic disease. Among the targets is β2B-tubulin, known to be required in human neuron and axon migration. We show β2B-tubulin is synthesized in axons and localizes preferentially to dynamic microtubules in the growth cone periphery. APC binds the β2B-tubulin 3' UTR; experiments interfering with this interaction reduced β2B-tubulin mRNA axonal localization and expression, depleted dynamic microtubules and the growth cone periphery, and impaired neuron migration. These results identify APC as a platform binding functionally related protein and RNA networks, and suggest a self-organizing model for the microtubule to localize synthesis of its own subunits.

Indexed as

NeurogenesisAdenomatous Polyposis Coli ProteinAnimalsAxonsBase SequenceBrainCell LineCell MovementGanglia, SpinalGenome-Wide Association StudyGrowth ConesMiceMicrotubulesMolecular Sequence DataNeuronsProtein Interaction MapsAdenomatous Polyposis Coli ProteinRNA-Binding ProteinsRNA, MessengerTubulin

Identifiers

PMID25036633
PMCPMC4133101
OpenAlexW2066029285

What OpenQuestion holds

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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.