The dynamics of ubiquitination and its role within the proteome of extracellular vesicles
The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD067810. Any additional requests can be directed to the corresponding author.
| Autores: | , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2026 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/416828 |
| Acceso en línea: | http://hdl.handle.net/10261/416828 https://api.elsevier.com/content/abstract/scopus_id/105022118600 |
| Access Level: | acceso abierto |
| Palabra clave: | BEAS-2B Exosomes Extracellular vesicles Mass spectrometry Microvesicles Proteomics Ubiquitination |
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The dynamics of ubiquitination and its role within the proteome of extracellular vesiclesMorales-Tarré, OrlandoPopa-Navarro, XitlallyParadela, AlbertoHernández-Ortiz, MagdalenaArrieta, OscarCorrales, Fernando J.Encarnación-Guevara, SergioBEAS-2BExosomesExtracellular vesiclesMass spectrometryMicrovesiclesProteomicsUbiquitinationThe mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD067810. Any additional requests can be directed to the corresponding author.Ubiquitination is a multifaceted post-translational modification that plays a crucial role in regulating the degradation of unnecessary cellular proteins and is involved in various cellular processes, including protein export via extracellular vesicles. We investigate how alterations in the intracellular levels of ubiquitinated proteins affect vesicle protein content in BEAS-2B cells. We increased the intracellular levels of ubiquitinated proteins by inhibiting proteasomal degradation with MG-132 and by blocking deubiquitinating enzymes using PR-619. Using centrifugation and ultracentrifugation, were isolate various vesicle types, specifically the largest vesicles (enriched in plasma membrane-derived microvesicles) and the smallest vesicles (enriched in endosomal exosomes). High-resolution mass spectrometry-based proteomics was utilized to quantify their protein content. The content of extracellular vesicles changed in response to both treatments, reflecting cellular changes and the export of stress signals. The increase in intracellular levels of ubiquitinated proteins induced metabolic stress in the cells, generally leading to a reduction in protein translation, an enhanced response to oxidative stress, changes in membrane transport, and alterations in cell-microenvironment interactions. The modifications observed in the vesicular proteome suggest that ubiquitination plays a significant role in regulating protein export. This regulation can be mastered for diagnostic purposes and for describing cells and tissues through liquid biopsies. SIGNIFICANCE: Ubiquitination is one of the most abundant post-translational modifications in cells, and its role, beyond marking proteins for degradation, is not fully understood. Characterizing the effect of this modification on protein export to extracellular vesicles can shed light on how a cell selects its contents to influence its microenvironment, send signals to distant tissues, or interact with the immune system. This is particularly relevant in the context of pathologies such as cancer, which hijacks the cellular vesicle-producing machinery and adapts it to its needs to influence the remodeling of its surroundings. Understanding how a cell regulates the specific contents of its vesicles may point the way toward the development of treatments or superior diagnostic and classification tools.This manuscript was funded by the grant DGAPA-PAPIIT (IN213216) to Sergio Encarnación-Guevara.Peer reviewedElsevierParadela, Alberto [0000-0001-6837-7056]Corrales, Fernando J. [0000-0002-0231-5159]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202620262026info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/416828https://api.elsevier.com/content/abstract/scopus_id/105022118600reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésJournal of proteomicsapplication/pdfhttps://doi.org/10.1016/j.jprot.2025.105566Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/4168282026-05-22T06:33:51Z |
| dc.title.none.fl_str_mv |
The dynamics of ubiquitination and its role within the proteome of extracellular vesicles |
| title |
The dynamics of ubiquitination and its role within the proteome of extracellular vesicles |
| spellingShingle |
The dynamics of ubiquitination and its role within the proteome of extracellular vesicles Morales-Tarré, Orlando BEAS-2B Exosomes Extracellular vesicles Mass spectrometry Microvesicles Proteomics Ubiquitination |
| title_short |
The dynamics of ubiquitination and its role within the proteome of extracellular vesicles |
| title_full |
The dynamics of ubiquitination and its role within the proteome of extracellular vesicles |
| title_fullStr |
The dynamics of ubiquitination and its role within the proteome of extracellular vesicles |
| title_full_unstemmed |
The dynamics of ubiquitination and its role within the proteome of extracellular vesicles |
| title_sort |
The dynamics of ubiquitination and its role within the proteome of extracellular vesicles |
| dc.creator.none.fl_str_mv |
Morales-Tarré, Orlando Popa-Navarro, Xitlally Paradela, Alberto Hernández-Ortiz, Magdalena Arrieta, Oscar Corrales, Fernando J. Encarnación-Guevara, Sergio |
| author |
Morales-Tarré, Orlando |
| author_facet |
Morales-Tarré, Orlando Popa-Navarro, Xitlally Paradela, Alberto Hernández-Ortiz, Magdalena Arrieta, Oscar Corrales, Fernando J. Encarnación-Guevara, Sergio |
| author_role |
author |
| author2 |
Popa-Navarro, Xitlally Paradela, Alberto Hernández-Ortiz, Magdalena Arrieta, Oscar Corrales, Fernando J. Encarnación-Guevara, Sergio |
| author2_role |
author author author author author author |
| dc.contributor.none.fl_str_mv |
Paradela, Alberto [0000-0001-6837-7056] Corrales, Fernando J. [0000-0002-0231-5159] Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72] |
| dc.subject.none.fl_str_mv |
BEAS-2B Exosomes Extracellular vesicles Mass spectrometry Microvesicles Proteomics Ubiquitination |
| topic |
BEAS-2B Exosomes Extracellular vesicles Mass spectrometry Microvesicles Proteomics Ubiquitination |
| description |
The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD067810. Any additional requests can be directed to the corresponding author. |
| publishDate |
2026 |
| dc.date.none.fl_str_mv |
2026 2026 2026 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article http://purl.org/coar/resource_type/c_6501 Publisher's version info:eu-repo/semantics/publishedVersion |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
http://hdl.handle.net/10261/416828 https://api.elsevier.com/content/abstract/scopus_id/105022118600 |
| url |
http://hdl.handle.net/10261/416828 https://api.elsevier.com/content/abstract/scopus_id/105022118600 |
| dc.language.none.fl_str_mv |
Inglés |
| language_invalid_str_mv |
Inglés |
| dc.relation.none.fl_str_mv |
Journal of proteomics application/pdf https://doi.org/10.1016/j.jprot.2025.105566 Sí |
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info:eu-repo/semantics/openAccess |
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openAccess |
| dc.publisher.none.fl_str_mv |
Elsevier |
| publisher.none.fl_str_mv |
Elsevier |
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reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC instname:Consejo Superior de Investigaciones Científicas (CSIC) |
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Consejo Superior de Investigaciones Científicas (CSIC) |
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DIGITAL.CSIC. Repositorio Institucional del CSIC |
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DIGITAL.CSIC. Repositorio Institucional del CSIC |
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15,811543 |