Evidence map›Paper›PMID 42493509›Full record

ArticleNature communications2026

Activity-dependent ribosome profiling reveals the landscape of canonical and non-canonical translation in brain tissue.

Nayan Suryawanshi, Hitoshi Uchida, Ryo Endo, Kai Sato, Daisuke Satoh, Kazuya Tsumagari, Koshi Imami, Takayasu Mikuni, Motomasa Tanaka

Erratum issuedAbstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Nayan Suryawanshi *Laboratory for Protein Conformation Diseases, RIKEN Center for Brain Science, Wako, Saitama, Japan.
Hitoshi Uchida *Department of Cellular Neuropathology, Brain Research Institute, Niigata University, Niigata, Japan.ORCID http://orcid.org/0000-0002-8952-2061
Ryo EndoLaboratory for Protein Conformation Diseases, RIKEN Center for Brain Science, Wako, Saitama, Japan.
Kai SatoLaboratory for Protein Conformation Diseases, RIKEN Center for Brain Science, Wako, Saitama, Japan.ORCID http://orcid.org/0000-0001-8018-5671
Daisuke SatohDepartment of Cellular Neuropathology, Brain Research Institute, Niigata University, Niigata, Japan.
Kazuya TsumagariProteome Homeostasis Research Unit, RIKEN Center for Integrative Medical Sciences, Yokohama, Japan.ORCID http://orcid.org/0000-0001-8464-7829
Koshi ImamiProteome Homeostasis Research Unit, RIKEN Center for Integrative Medical Sciences, Yokohama, Japan.ORCID http://orcid.org/0000-0002-7451-4982
Takayasu MikuniDepartment of Cellular Neuropathology, Brain Research Institute, Niigata University, Niigata, Japan. tmikuni@bri.niigata-u.ac.jp.ORCID http://orcid.org/0000-0002-9769-9369
Motomasa TanakaLaboratory for Protein Conformation Diseases, RIKEN Center for Brain Science, Wako, Saitama, Japan. motomasa.tanaka@riken.jp.ORCID http://orcid.org/0000-0002-2994-7703

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neural activity-dependent translation is essential for synaptic plasticity and diverse brain functions. Translation involves not only canonical main open reading frames (mORFs) but also upstream ORFs (uORFs), which may regulate mORF expression. However, due to technical limitations, systematic investigation of activity-dependent uORFs and mORFs in brain tissues remains challenging. Here, we developed a ribosome tagging and purification strategy that bypasses the prolonged turnover of ribosomal proteins, enabling ribosome profiling with one-hour temporal resolution after neural stimulation. Applying this strategy to mouse hippocampal slices undergoing long-term potentiation, we identify hundreds of activity-induced mORFs and uORFs, including a previously unknown uORF from Egr1. We demonstrate that this Egr1-uORF translation is tightly regulated by neuronal activity, and its encoded peptide interacts with peroxisomal machinery, suggesting a potential link between synaptic stimulus and peroxisome biology. This study provides a useful technique and resources for deciphering molecular mechanisms underlying activity- and translation-dependent brain functions in health and disease.

Indexed as

HippocampusLong-Term PotentiationNeuronsProtein BiosynthesisRibosome ProfilingAnimalsEarly Growth Response Protein 1FemaleMaleMiceMice, Inbred C57BLPeroxisomesRibosomesEarly Growth Response Protein 1Egr1 protein, mouse

Identifiers

PMID42493509
PMCPMC13396407

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.