Evidence map›Paper›PMID 40201129›Full record

ArticleiScience2025

A competition network connects Rab5 and Rab11 GTPases at the surface of endocytic structures.

Elsi Ferro, Simone Tealdi, Jean Piero Margaria, Maria Chiara De Santis, Luca Gozzelino, Marta Cunial, Chiara Enrico Bena, Irene Franco, Emilio Hirsch, Andrea Gamba and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

13 authors.

Elsi FerroDepartment of Applied Science and Technology, Politecnico di Torino, Corso Duca degli Abruzzi 24, 10129 Turin, Italy.
Simone TealdiItalian Institute for Genomic Medicine, SP142 km 3,95, 10060 Candiolo, Italy.
Jean Piero MargariaDepartment of Molecular Biotechnology and Health Sciences, Molecular Biotechnology Center, University of Turin, Via Nizza 52, 10126 Turin, Italy.
Maria Chiara De SantisDepartment of Molecular Biotechnology and Health Sciences, Molecular Biotechnology Center, University of Turin, Via Nizza 52, 10126 Turin, Italy.
Luca GozzelinoItalian Institute for Genomic Medicine, SP142 km 3,95, 10060 Candiolo, Italy.
Marta CunialItalian Institute for Genomic Medicine, SP142 km 3,95, 10060 Candiolo, Italy.
Chiara Enrico BenaDepartment of Applied Science and Technology, Politecnico di Torino, Corso Duca degli Abruzzi 24, 10129 Turin, Italy.
Irene FrancoSomatic Mutation Mechanisms Unit, Division of Genetics and Cell Biology, IRCCS Ospedale San Raffaele, Via Olgettina 58, 20132 Milan, Italy.
Emilio HirschDepartment of Molecular Biotechnology and Health Sciences, Molecular Biotechnology Center, University of Turin, Via Nizza 52, 10126 Turin, Italy.
Andrea GambaDepartment of Applied Science and Technology, Politecnico di Torino, Corso Duca degli Abruzzi 24, 10129 Turin, Italy.
Andrea PagnaniDepartment of Applied Science and Technology, Politecnico di Torino, Corso Duca degli Abruzzi 24, 10129 Turin, Italy.
Carla BosiaDepartment of Applied Science and Technology, Politecnico di Torino, Corso Duca degli Abruzzi 24, 10129 Turin, Italy.
Carlo Cosimo CampaItalian Institute for Genomic Medicine, SP142 km 3,95, 10060 Candiolo, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Specificity in membrane trafficking relies on the interaction between Rab small GTPase proteins and their molecular effectors. However, the evidence that different Rab proteins can bind to common effectors challenges this view. Here, we show that molecular competition between distinct Rab GTPases for a shared protein can link diverse membrane trafficking pathways. Theoretical analysis and experimental data support a role for Zfyve26 as a part of a competitive network that modulates changes in Rab5-Rab11 abundance, activation status, and correlation at the surface of single endocytic structures. By leveraging on the Loop index, a novel metric that couples the GTP-bound fraction and the total amount of Rab GTPase, we infer the saturation of Zfyve26 molecules at the endocytic surface from time-lapse imaging data. Our findings establish that transduction in the endocytic system is governed by stoichiometric constraints determining the trade-off between different trafficking pathways at the surface of a membrane-bound organelle.

Indexed as

Cell biologyFunctional aspects of cell biologyMolecular interactionOrganizational aspects of cell biology

Identifiers

PMID40201129
PMCPMC11978354

What Socratic holds

Textmetadata
LicenceCC BY-NC
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 Socratic graph.