Evidence map›Paper›PMID 42660790›Full record

ReviewTrends in cell biology2026

Remaking an exit: dynamic regulation of ER exit sites by post-translational modifications.

Tetsuya Hirata, Michael Boyce

Abstract readReview
In one paragraph

Review in Trends in cell biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. 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

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

2 authors.

Tetsuya HirataDepartment of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA. Electronic address: tetsuya.hirata@duke.edu.
Michael BoyceDepartment of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA. Electronic address: michael.boyce@duke.edu.

Funding

Control of COPII vesicle trafficking by intracellular protein glycosylationR01GM117473 · NIGMS · DUKE UNIVERSITY · PI BOYCE, MICHAEL S · 2017 to 2025
$2.6M
Cell signaling through O-linked glycosylationR35GM161290 · NIGMS · DUKE UNIVERSITY · PI MICHAEL S BOYCE · 2026 to 2026
$475k
NIGMS NIH HHS R01 GM117473NIGMS NIH HHS R35 GM161290
6 · The paper itself

Abstract

Endoplasmic reticulum exit sites (ERES) are dynamic platforms that coordinate not only protein trafficking but also protein quality control and signaling functions. ERES size, composition, architecture, interactions, and activity must be precisely remodeled in response to myriad pathophysiological cues to finely tune cellular homeostasis. However, the molecular mechanisms underlying this regulation remain incompletely understood. Coat protein complex II (COPII) mediates many ERES functions, and its subunits and client cargos are subject to spatiotemporal regulation by post-translational modifications (PTMs) that modulate ERES assembly, cargo selection, and inter-organelle communication. In this article, we review recent advances in understanding how PTMs control the organization and functional versatility of ERES and the COPII system.

Indexed as

Endoplasmic ReticulumProtein Processing, Post-TranslationalAnimalsCOP-Coated VesiclesHumansProtein TransportSignal TransductionCOPIIER exit siteER-phagypost-translational modificationsprotein traffickingsignaling

Identifiers

PMID42660790
PMCPMC13544067

What OpenQuestion holds

Textmetadata
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.