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hal.structure.identifierCentre de biophysique moléculaire [CBM]
dc.contributor.authorROBINET, Pauline
hal.structure.identifierCentre de biophysique moléculaire [CBM]
dc.contributor.authorMOLLET, Lucile
hal.structure.identifierCentre de biophysique moléculaire [CBM]
dc.contributor.authorGONZALEZ, Patrick
hal.structure.identifierCentre de biophysique moléculaire [CBM]
dc.contributor.authorNORMAND, Thierry
hal.structure.identifierInstitut de Mathématiques de Bordeaux [IMB]
dc.contributor.authorCHARPENTIER, Stephane
hal.structure.identifierCentre de biophysique moléculaire [CBM]
dc.contributor.authorBRULE, Fabienne
hal.structure.identifierCentre de biophysique moléculaire [CBM]
dc.contributor.authorDUBOIS, Martine
hal.structure.identifierCentre de biophysique moléculaire [CBM]
dc.contributor.authorLEGRAND, Alain
dc.date.accessioned2024-04-04T02:28:36Z
dc.date.available2024-04-04T02:28:36Z
dc.date.issued2010
dc.identifier.issn0006-291X
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/190109
dc.description.abstractEnMitogaligin, a protein encoded by galig, an internal cytotoxic gene of the galectin-3 locus, is mostly a mitochondrial protein. Mitochondrial targeting is due to an already identified mitochondrial localization signal. Interaction of mitogaligin with mitochondria leads to cytochrome c cytosolic leakage and ultimately to cell death. We have previously pointed out that mitogaligin can also be directed to the nucleus when the mitochondrial addressing signal is inactivated, indicating a possible dual intracellular localization of the protein. When expressed in the nucleus, mitogaligin exhibits also apoptotic properties leading to cell death. In this report, we show that nuclear addressing of mitogaligin depends on a sequence differing from classical signals containing basic, lysine or proline-tyrosine rich residues. The signal consists of a long sequence of amino acids residues based on a series of a short repetitive degenerated sequence.
dc.language.isoen
dc.publisherElsevier
dc.title.enThe mitogaligin protein is addressed to the nucleus via a non-classical localization signal
dc.typeArticle de revue
dc.identifier.doi10.1016/j.bbrc.2009.12.162
bordeaux.journalBiochemical and Biophysical Research Communications
bordeaux.page53-57
bordeaux.volume392
bordeaux.hal.laboratoriesInstitut de Mathématiques de Bordeaux (IMB) - UMR 5251*
bordeaux.issue1
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.institutionCNRS
bordeaux.peerReviewedoui
hal.identifierhal-00529397
hal.version1
hal.popularnon
hal.audienceInternationale
dc.subject.itUnconventional nuclear localization signal
dc.subject.itMitogaligin
dc.subject.itDual localization
dc.subject.itCELL-DEATH PROTEIN
dc.subject.itINTRACELLULAR-LOCALIZATION
dc.subject.itMOLECULAR-CLONING
dc.subject.itIDENTIFICATION
dc.subject.itSEQUENCE
dc.subject.itIMPORTIN
dc.subject.itVIRUS
dc.subject.itGENE
dc.subject.itTRANSLOCATION
dc.subject.itMITOCHONDRIA
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-00529397v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biochemical%20and%20Biophysical%20Research%20Communications&rft.date=2010&rft.volume=392&rft.issue=1&rft.spage=53-57&rft.epage=53-57&rft.eissn=0006-291X&rft.issn=0006-291X&rft.au=ROBINET,%20Pauline&MOLLET,%20Lucile&GONZALEZ,%20Patrick&NORMAND,%20Thierry&CHARPENTIER,%20Stephane&rft.genre=article


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