Evidence map›Paper›PMID 40209344›Full record

ArticleEuropean journal of cell biology2025

Galectin-8 drives ERK-dependent mitochondrial fragmentation, perinuclear relocation and mitophagy, with metabolic adaptations for cell proliferation.

Adely de la Peña, Claudio Retamal, Francisca Pérez-Molina, Nicole Díaz-Valdivia, Francisco Veloso-Bahamondes, Diego Tapia, Jorge Cancino, Felix Randow, Alfonso González, Claudia Oyanadel and 1 more

Abstract read
In one paragraph

Article in European journal of cell biology, 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. Review
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

11 authors.

Adely de la PeñaCentro de Biología Celular y Biomedicina, CEBICEM, Facultad de Ciencias, Universidad San Sebastián, Santiago, Chile; Escuela de Medicina, Facultad de Medicina, Universidad San Sebastián, Santiago, Chile.
Claudio RetamalCentro de Biología Celular y Biomedicina, CEBICEM, Facultad de Ciencias, Universidad San Sebastián, Santiago, Chile; Departamento de Ciencias Biológicas y Químicas, Facultad de Ciencias, Universidad San Sebastián, Santiago, Chile.
Francisca Pérez-MolinaCentro de Biología Celular y Biomedicina, CEBICEM, Facultad de Ciencias, Universidad San Sebastián, Santiago, Chile; Escuela de Medicina, Facultad de Medicina, Universidad San Sebastián, Santiago, Chile.
Nicole Díaz-ValdiviaCentro de Biología Celular y Biomedicina, CEBICEM, Facultad de Ciencias, Universidad San Sebastián, Santiago, Chile; Escuela de Medicina, Facultad de Medicina, Universidad San Sebastián, Santiago, Chile.
Francisco Veloso-BahamondesCentro de Biología Celular y Biomedicina, CEBICEM, Facultad de Ciencias, Universidad San Sebastián, Santiago, Chile; Escuela de Medicina, Facultad de Medicina, Universidad San Sebastián, Santiago, Chile.
Diego TapiaCentro de Biología Celular y Biomedicina, CEBICEM, Facultad de Ciencias, Universidad San Sebastián, Santiago, Chile.
Jorge CancinoCentro de Biología Celular y Biomedicina, CEBICEM, Facultad de Ciencias, Universidad San Sebastián, Santiago, Chile; Escuela de Medicina, Facultad de Medicina, Universidad San Sebastián, Santiago, Chile.
Felix RandowDivision of Protein and Nucleic Acid Chemistry, MRC Laboratory of Molecular Biology, Cambridge, UK; Department of Medicine, University of Cambridge, UK.
Alfonso GonzálezCentro de Biología Celular y Biomedicina, CEBICEM, Facultad de Ciencias, Universidad San Sebastián, Santiago, Chile; Escuela de Medicina, Facultad de Medicina, Universidad San Sebastián, Santiago, Chile; Centro Científico Tecnológico de Excelencia Ciencia y Vida, Fundación Ciencia y Vida, Santiago, Chile. Electronic address: alfonso.gonzalez@uss.cl.
Claudia OyanadelCentro de Biología Celular y Biomedicina, CEBICEM, Facultad de Ciencias, Universidad San Sebastián, Santiago, Chile; Departamento de Ciencias Biológicas y Químicas, Facultad de Ciencias, Universidad San Sebastián, Santiago, Chile. Electronic address: claudia.oyanadel@uss.cl.
Andrea SozaCentro de Biología Celular y Biomedicina, CEBICEM, Facultad de Ciencias, Universidad San Sebastián, Santiago, Chile; Centro Científico Tecnológico de Excelencia Ciencia y Vida, Fundación Ciencia y Vida, Santiago, Chile. Electronic address: andrea.soza@uss.cl.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria adapt to the cell proliferative demands induced by growth factors through dynamic changes in morphology, distribution, and metabolic activity. Galectin-8 (Gal-8), a carbohydrate-binding protein that promotes cell proliferation by transactivating the EGFR-ERK signaling pathway, is overexpressed in several cancers. However, its impact on mitochondrial dynamics during cell proliferation remains unknown. Using MDCK and RPTEC kidney epithelial cells, we demonstrate that Gal-8 induces mitochondrial fragmentation and perinuclear redistribution. Additionally, mitochondria adopt donut-shaped morphologies, and live-cell imaging with two Keima-based reporters demonstrates Gal-8-induced mitophagy. ERK signaling inhibition abrogates all these Gal-8-induced mitochondrial changes and cell proliferation. Studies with established mutant versions of Gal-8 and CHO cells reveal that mitochondrial changes and proliferative response require interactions between the N-terminal carbohydrate recognition domain of Gal-8 and α-2,3-sialylated N-glycans at the cell surface. DRP1, a key regulator of mitochondrial fission, becomes phosphorylated in MDCK cells or overexpressed in RPTEC cells in an ERK-dependent manner, mediating mitochondrial fragmentation and perinuclear redistribution. Bafilomycin A abrogates Gal-8-induced cell proliferation, suggesting that mitophagy serves as an adaptation to cell proliferation demands. Functional analysis under Gal-8 stimulation shows that mitochondria maintain an active electron transport chain, partially uncoupled from ATP synthesis, and an increased membrane potential, indicative of healthy mitochondria. Meanwhile, the cells exhibit increased extracellular acidification rate and lactate production via aerobic glycolysis, a hallmark of an active proliferative state. Our findings integrate mitochondrial dynamics with metabolic adaptations during Gal-8-induced cell proliferation, with potential implications for physiology, disease, and therapeutic strategies.

Indexed as

Cell ProliferationExtracellular Signal-Regulated MAP KinasesGalectinsMAP Kinase Signaling SystemMitochondriaMitophagyAnimalsCHO CellsCricetulusDogsHumansMadin Darby Canine Kidney CellsMitochondrial DynamicsExtracellular Signal-Regulated MAP KinasesGalectinsGalectin-8GlycosylationMitochondrial dynamicsMitophagyProliferation

Identifiers

PMID40209344
PMCPMC12162348

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Registered trials

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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.