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<identifier>oai:HAL:inserm-00284621v1</identifier>
<datestamp>2017-12-21</datestamp>
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<publisher>HAL CCSD</publisher>
<title lang=en>A mutant alphaII-spectrin designed to resist calpain and caspase cleavage questions the functional importance of this process in vivo.</title>
<creator>Meary, Fleur</creator>
<creator>Metral, Sylvain</creator>
<creator>Ferreira, Chrystophe</creator>
<creator>Eladari, Dominique</creator>
<creator>Colin, Yves</creator>
<creator>Lecomte, Marie-Christine</creator>
<creator>Nicolas, Gaël</creator>
<contributor>Protéines de la membrane érythrocytaire et homologues non-érythroides ; Université des Antilles et de la Guyane (UAG) - Institut National de la Transfusion Sanguine [Paris] (INTS) - Université Paris Diderot - Paris 7 (UPD7) - Université de la Réunion (UR) - Institut National de la Santé et de la Recherche Médicale (INSERM)</contributor>
<contributor>Institut Claude Bernard - Physiologie et Pathologie ; Assistance publique - Hôpitaux de Paris (AP-HP) - Université Paris Diderot - Paris 7 (UPD7) - Institut National de la Santé et de la Recherche Médicale (INSERM)</contributor>
<contributor>Physiologie et pharmacologie vasculaire et rénale ; IFR58 - Université Paris Descartes - Paris 5 (UPD5) - Institut National de la Santé et de la Recherche Médicale (INSERM)</contributor>
<description>International audience</description>
<source>ISSN: 0021-9258</source>
<source>EISSN: 1083-351X</source>
<source>Journal of Biological Chemistry</source>
<publisher>American Society for Biochemistry and Molecular Biology</publisher>
<identifier>inserm-00284621</identifier>
<identifier>http://www.hal.inserm.fr/inserm-00284621</identifier>
<identifier>http://www.hal.inserm.fr/inserm-00284621/document</identifier>
<identifier>http://www.hal.inserm.fr/inserm-00284621/file/Meary_-_JBC_2007.pdf</identifier>
<source>http://www.hal.inserm.fr/inserm-00284621</source>
<source>Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, 282 (19), pp.14226-14237</source>
<identifier>PUBMED : 17374614</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/17374614</relation>
<language>en</language>
<subject lang=en>spectrin</subject>
<subject lang=en>fodrin</subject>
<subject lang=en>knockout</subject>
<subject lang=en>calpain</subject>
<subject lang=en>caspase</subject>
<subject lang=en>calmodulin</subject>
<subject>[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology</subject>
<subject>[SDV.BC] Life Sciences [q-bio]/Cellular Biology</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>alpha- and beta-spectrins are components of molecular scaffolds located under the lipid bilayer and named membrane skeletons. Disruption of these scaffolds through mutations in spectrins demonstrated that they are involved in the membrane localization or the maintenance of proteins associated with them. The ubiquitous alphaII-spectrin chain bears in its central region a unique domain that is sensitive to several proteases such as calpains or caspases. The conservation of this region in vertebrates suggests that the proteolysis of alphaII-spectrin by these enzymes could be involved in important functions. To assess the role of alphaII-spectrin cleavage in vivo, we generated a murine model in which the exons encoding the region defining this cleavage sensitivity were disrupted by gene targeting. Surprisingly, homozygous mice expressing this mutant alphaII-spectrin appeared healthy, bred normally, and had no histological anomaly. Remarkably, the mutant alphaII-spectrin assembles correctly into the membrane skeleton, thus challenging the notion that this region is required for the stable biogenesis of the membrane skeleton in nonerythroid cells. Our finding also argues against a critical role of this particular alphaII-spectrin cleavage in either major cellular functions or in normal development.</description>
<date>2007-05-11</date>
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