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<title lang=en>Hsp90 Oligomerization Process: How Can p23 Drive the Chaperone Machineries?</title>
<creator>Lepvrier, Eléonore</creator>
<creator>Nigen, Michaël</creator>
<creator>Moullintraffort, Laura</creator>
<creator>Chat, Sophie</creator>
<creator>Allegro, Diane</creator>
<creator>Barbier, Pascale</creator>
<creator>Thomas, Daniel</creator>
<creator>Nazabal, Alexis</creator>
<creator>Garnier, Cyrille</creator>
<contributor>Laboratoire de Pharmacie Galenique, Biopharmacie et Pharmacie Clinique ; Université de Rennes 1 (UR1)</contributor>
<contributor>Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Science et Technologie du Lait et de l'Oeuf (STLO) ; Institut National de la Recherche Agronomique (INRA) - AGROCAMPUS OUEST</contributor>
<contributor>Institut de Génétique et Développement de Rennes (IGDR) ; Université de Rennes 1 (UR1) - Centre National de la Recherche Scientifique (CNRS) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Génétique Animale et Biologie Intégrative (GABI) ; Institut National de la Recherche Agronomique (INRA) - AgroParisTech</contributor>
<contributor>Centre de Recherches en Oncologie biologique et Oncopharmacologie (CRO2) ; Aix Marseille Université (AMU) - Hôpital de la Timone [CHU - APHM] (TIMONE) - Institut National de la Santé et de la Recherche Médicale (INSERM)</contributor>
<contributor>Cova IX AG ; CovaIXAG</contributor>
<description>International audience</description>
<source>ISSN: 1570-9639</source>
<source>BBA - Proteins and Proteomics</source>
<publisher>Elsevier</publisher>
<identifier>hal-01174219</identifier>
<identifier>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01174219</identifier>
<source>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01174219</source>
<source>BBA - Proteins and Proteomics, Elsevier, 2015, 1854, pp.1412-1424. 〈10.1016/j.bbapap.2015.07.003〉</source>
<identifier>DOI : 10.1016/j.bbapap.2015.07.003</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbapap.2015.07.003</relation>
<identifier>PUBMED : 26151834</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/26151834</relation>
<language>en</language>
<subject lang=en>high mass spectrometry</subject>
<subject lang=en>Hsp90</subject>
<subject lang=en>oligomers</subject>
<subject lang=en>p23</subject>
<subject lang=en>protein complexes</subject>
<subject>[SDV] Life Sciences [q-bio]</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>The 90-kDa heat shock protein (Hsp90) is a highly flexible dimer able to self-associate in the presence of divalent cations or under heat shock. In a previous work, we focused on the Mg2 +-induced oligomerization process of Hsp90, and characterized the oligomers. Combining analytical ultracentrifugation, size-exclusion chromatography coupled to multi-angle laser light scattering and high-mass matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, we studied the interaction of p23 with both Hsp90 dimer and oligomers. Even if p23 predominantly binds the Hsp90 dimer, we demonstrated, for the first time, that p23 is also able to interact with Hsp90 oligomers, shifting the Hsp90 dimer-oligomers equilibrium toward dimer. Our results showed that the Hsp90:p23 binding stoichiometry decreases with the Hsp90 oligomerization degree. Therefore, we propose a model in which p23 would act as a “protein wedge” regarding the Hsp90 dimer closure and the Hsp90 oligomerization process</description>
<date>2015</date>
</dc>
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