Evidence map›Paper›PMID 41840126›Full record

ArticleNature cell biology2026

Fructose-1,6-bisphosphate couples glycolytic activity to cell adhesion.

Lennart Hoffmann, Marlen Duchmann, Katina Lazarow, Yun-Hsuan Huang, Fabian Lukas, Wen-Ting Lo, Regina Feil, Christopher Schmied, Martin Lehmann, John E Lunn and 4 more

Abstract read
In one paragraph

Article in Nature cell biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

14 authors.

Lennart HoffmannDepartment for Nanophysiology, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany.ORCID http://orcid.org/0009-0005-3511-6892
Marlen DuchmannDepartment for Nanophysiology, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany.
Katina LazarowScreening Unit, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.
Yun-Hsuan HuangMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany.
Fabian LukasDepartment for Nanophysiology, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany.
Wen-Ting LoDepartment for Molecular Pharmacology and Cell Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.ORCID http://orcid.org/0000-0001-7904-6834
Regina FeilMetabolic Networks, Max Planck Institute of Molecular Plant Physiology, Potsdam-Golm, Germany.
Christopher SchmiedCellular Imaging Facility, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.ORCID http://orcid.org/0000-0003-2058-1124
Martin LehmannCellular Imaging Facility, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.ORCID http://orcid.org/0000-0002-8370-6353
John E LunnMetabolic Networks, Max Planck Institute of Molecular Plant Physiology, Potsdam-Golm, Germany.ORCID http://orcid.org/0000-0001-8533-3004
Ilaria PiazzaMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany.ORCID http://orcid.org/0000-0001-5895-6134
Jens P von KriesScreening Unit, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.
Volker HauckeDepartment for Molecular Pharmacology and Cell Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.ORCID http://orcid.org/0000-0003-3119-6993
Tanja MaritzenDepartment for Nanophysiology, RPTU University Kaiserslautern-Landau, Kaiserslautern, Germany. maritzen@rptu.de.ORCID http://orcid.org/0000-0003-4993-0340

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) INST248/342-1 FUGGDeutsche Forschungsgemeinschaft (German Research Foundation) MA4735/4-1
6 · The paper itself

Abstract

Cellular adhesion to the extracellular matrix is essential for morphogenesis, tissue integrity and survival signalling. The best understood adhesion structures are focal adhesions (FAs). In spite of their importance, our knowledge of upstream factors that integrate FA dynamics with other cellular processes, such as metabolism, remains fragmentary. Using a genome-wide screen, we identify aldolase A, a key glycolytic enzyme that converts fructose-1,6-bisphosphate (FBP), as a regulatory switch that links metabolic flux to FA assembly and cell morphogenesis. We show that cellular FBP serves as a signalling metabolite, which transmits information about the metabolic cell state to the actin-based machinery for cell adhesion and protrusion. This mechanism involves FBP binding to the Rac1 inhibitor RCC2 and a concomitant elevation of Rac1 activity resulting in actin reorganization, increased FA assembly and elevated protrusive activity. Here we predict this mechanism to be crucial for processes ranging from development to cancer.

Indexed as

Cell AdhesionFructose-Bisphosphate AldolaseFructosediphosphatesGlycolysisActinsAnimalsFocal AdhesionsGuanine Nucleotide Exchange FactorsHumansrac1 GTP-Binding ProteinSignal TransductionActinsfructose-1,6-diphosphateFructose-Bisphosphate AldolaseFructosediphosphatesGuanine Nucleotide Exchange Factorsrac1 GTP-Binding Protein

Identifiers

PMID41840126
PMCPMC13086585

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.