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Rosa Barrio Lab researches ubiquitin proteins in development and rare diseases like Townes-Brocks Syndrome using innovative methods.

Our research focuses on

studying biomedically relevant genes and processes, with a particular interest in understanding the role of members of the ubiquitin family (UbLs) in the regulation of development and their association with diseases, especially rare diseases.

We study Townes-Brocks Syndrome, a ciliopathy caused by truncations in SALL1 transcription factor, as well as other rare diseases related to the UbL family.We study Townes-Brocks Syndrome, a ciliopathy caused by truncations in SALL1 transcription factor, as well as other rare diseases related to the UbL family.

We are also actively involved in the development of innovative strategies to investigate the influence of UbL modifications on protein regulation and disease. These strategies include bioUbLs (to identify proteins modified by UbLs), SUMO-ID (to identify interactors of proteins when modified by UbLs), and BioE3 (to identify bona-fide targets of E3 ligases).

To accomplish this, we use in vivo biotinylation and mass spectrometry of proteins from human and mouse cultured cells, as well as using Drosophila melanogaster and mouse models, all leading to valuable insights for physiological and disease processes.

Biomedicine research

Lab’s principal
lines of research

Sall & Rare Diseases

Spal-like (SALL) Family of Transcription Factors and rare diseases.

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Ubiquitin-like proteins

Ubiquitin-like proteins in development and disease.

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Tools to study ubiquitin

Tools to study ubiquitin-like modifications.

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Ubiquitin related networks

We collaborate with networks to advance science in proteostasis

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Selected publications

Polyamine-dependent metabolic shielding regulates alternative splicing.

Zabala-Letona A, Pujana-Vaquerizo M, Martinez-Laosa B, Ponce-Rodriguez M, Garcia-Longarte S, Mendizabal I, Gimeno A, Rogalska M, Tan J, Cabrera D, van Liempd S, Ximenez-Embun P, Espinosa S, Fagoaga-Eugui M, Peccati F, Zakrzewski M, Astobiza I, Arana-Castañares M, Cherkaoui S, Sendino M, Martín-Barros I, Ercilla A, Bozal-Basterra L, Carlevaris O, Arruabarrena-Aristorena A, Pérez-Andrés E, Santamaría-Zamorano T, Ferrer-Bonsoms JA, Carazo F, Cieśla M, Lobato C, Seoane J, Martín-Martín N, Barrio R, Sutherland JD, Aransay AM, Falcón-Pérez JM, Martínez-Pastor B, Rubio A, Blanco FJ, Hogarty MD, Morscher RJ, Berra E, Serwa RA, Jiménez-Barbero J, Jiménez-Osés G, Efeyan A, Finley L, Lizcano JM, Muñoz J, Valcarcel J, Carracedo A*.

Nature. 2026 Feb;650(8100):E4

doi: 10.1038/s41586-026-10140-3

PMID: 41565829

Loss of UFMylation supports prostate cancer metastasis and rewires cell metabolism towards hexosamine biosynthesis

Bozal-Basterra L, Salazar MC, Ferreira Campos AM, Demicco M, Schmidt DR, Sobczak K, Ereño-Orbea J, Altea-Manzano P, Miranda Villanueva A, Martínez La Osa B, Garcia-Longarte S, Ponce-Rodriguez M, Mendizabal I, Carlevaris O, Astobiza I, Martin-Martin N, Zabala-Letona A, Talamillo A, Fernández-García J, Azkargorta M, Iloro I, Barrio R, Elortza F, Fendt SM, Vander Heiden MG, Barbero JJ, Sutherland JD, Carracedo A.*

bioRxiv [Preprint]. 2025 Jun 4:2025.06.02.657324

doi: 10.1101/2025.06.02.657324.

PMID: 40502001

BioE3 identifies specific substrates of ubiquitin E3 ligases.

Barroso-Gomila O, Merino-Cacho L, Muratore V, Perez C, Taibi V, Maspero E, Azkargorta M, Iloro I, Trulsson F, Vertegaal ACO, Mayor U, Elortza F, Polo S, Barrio R*, Sutherland JD*

Nat Commun. 2023 Nov 23;14(1):7656

doi: 10.1038/s41467-023-43326-8

PMID: 37996419

Last news

2025/12/20
WINTER 2025
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2025/10/01
AUTUMN 2025
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2025/09/22
EMBO Workshop: SUMOylation: From discovery to translation.
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2025/09/02
47 Congreso de la SEBBM
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2025/07/01
SUMMER 2025
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2025/05/20
Fourth Annual Meeting of the ProteoCURE COST Action 2025
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Lab members

Funding

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