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<title lang=en>Precise mapping of the CD95 pre-ligand assembly domain.</title>
<creator>Edmond, Valérie</creator>
<creator>Ghali, Benoist</creator>
<creator>Penna, Aubin</creator>
<creator>Taupin, Jean-Luc</creator>
<creator>Daburon, Sophie</creator>
<creator>Moreau, Jean-François</creator>
<creator>Legembre, Patrick</creator>
<contributor>Récepteur de mort et échappement tumoral ; 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 ) - 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>Composantes innées de la réponse immunitaire et différenciation (CIRID) ; Université Bordeaux Segalen - Bordeaux 2 - Centre National de la Recherche Scientifique (CNRS)</contributor>
<description>International audience</description>
<source>ISSN: 1932-6203</source>
<source>PLoS ONE</source>
<publisher>Public Library of Science</publisher>
<identifier>hal-00873708</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00873708</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00873708/document</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00873708/file/Precise_Mappingsur the_CD95-accepted.pdf</identifier>
<source>https://hal.archives-ouvertes.fr/hal-00873708</source>
<source>PLoS ONE, Public Library of Science, 2012, 7 (9), pp.e46236. 〈10.1371/journal.pone.0046236〉</source>
<identifier>DOI : 10.1371/journal.pone.0046236</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0046236</relation>
<identifier>PUBMED : 23049989</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/23049989</relation>
<language>en</language>
<subject>[SDV.BC] Life Sciences [q-bio]/Cellular Biology</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>Pre-association of CD95 at the plasma membrane is mandatory for efficient death receptor signaling. This homotrimerization occurs through self-association of an extracellular domain called the pre-ligand assembly domain (PLAD). Using novel molecular and cellular tools, we confirmed that CD95-PLAD is necessary to promote CD95 multimerization and plays a pivotal role in the transmission of apoptotic signals. However, while a human CD95 mutant deleted of the previously described PLAD domain (amino acids 1 to 66) fails to interact with its wild-type counterpart and trigger autonomous cell death, deletion of amino acids 1 to 42 does not prevent homo- or hetero (human/mouse)-oligomerization of CD95, and thus does not alter transmission of the apoptotic signal. Overall, these findings indicate that the region between amino acids 43 to 66 corresponds to the minimal motif involved in CD95 homotypic interaction and is necessary to convey an efficient apoptotic signal. Interfering with this PLAD may represent a new therapeutic strategy for altering CD95-induced apoptotic and non-apoptotic signals.</description>
<date>2012</date>
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