<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-05-23T16:43:26Z</responseDate><request verb="GetRecord" identifier="oai:repisalud.isciii.es:20.500.12105/16418" metadataPrefix="marc">https://repisalud.isciii.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:repisalud.isciii.es:20.500.12105/16418</identifier><datestamp>2025-04-01T09:58:31Z</datestamp><setSpec>com_20.500.12105_19604</setSpec><setSpec>com_20.500.12105_2051</setSpec><setSpec>col_20.500.12105_19605</setSpec></header><metadata><record xmlns="http://www.loc.gov/MARC21/slim" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:doc="http://www.lyncode.com/xoai" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.loc.gov/MARC21/slim http://www.loc.gov/standards/marcxml/schema/MARC21slim.xsd">
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      <subfield code="a">Rojas-Gómez, Amelia</subfield>
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      <subfield code="a">Dosil, Sara G</subfield>
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      <subfield code="a">Chichón, Francisco Javier</subfield>
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      <subfield code="a">Fernández-Gallego, Nieves</subfield>
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      <subfield code="a">Calvo, Enrique</subfield>
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      <subfield code="a">Requena, Silvia</subfield>
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      <subfield code="a">Otón, Joaquin</subfield>
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      <subfield code="a">Serrano, Alvaro</subfield>
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      <subfield code="a">Arroyo, Montserrat</subfield>
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      <subfield code="a">Valpuesta, José M</subfield>
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      <subfield code="a">Sánchez-Madrid, Francisco</subfield>
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      <subfield code="a">Martín-Cófreces, Noa B</subfield>
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      <subfield code="c">2023-06</subfield>
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      <subfield code="a">Cell proteostasis includes gene transcription, protein translation, folding of de novo proteins, post-translational modifications, secretion, degradation and recycling. By profiling the proteome of extracellular vesicles (EVs) from T cells, we have found the chaperonin complex CCT, involved in the correct folding of particular proteins. By limiting CCT cell-content by siRNA, cells undergo altered lipid composition and metabolic rewiring towards a lipid-dependent metabolism, with increased activity of peroxisomes and mitochondria. This is due to dysregulation of the dynamics of interorganelle contacts between lipid droplets, mitochondria, peroxisomes and the endolysosomal system. This process accelerates the biogenesis of multivesicular bodies leading to higher EV production through the dynamic regulation of microtubule-based kinesin motors. These findings connect proteostasis with lipid metabolism through an unexpected role of CCT.</subfield>
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      <subfield code="a">J Extracell Vesicles. 2023 Jun;12(6):e12333.</subfield>
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      <subfield code="a">10.1002/jev2.12333</subfield>
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      <subfield code="a">37328936</subfield>
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      <subfield code="a">http://hdl.handle.net/20.500.12105/16418</subfield>
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      <subfield code="a">Chaperonin CCT controls extracellular vesicle production and cell metabolism through kinesin dynamics.</subfield>
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