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• W2300250957 abstract "// Florian Beaumatin 1, 2 , Mohamad El Dhaybi 1, 2, 4 , Jean-Paul Lasserre 1, 2 , Bénédicte Salin 1, 2 , Mary Pat Moyer 3 , Mireille Verdier 4 , Stéphen Manon 1, 2 , Muriel Priault 1, 2 1 CNRS, Institut de Biochimie et de Génétique Cellulaires, UMR5095, 33077 Bordeaux, France 2 Université Bordeaux Ségalen, Institut de Biochimie et de Génétique Cellulaires, UMR5095, 33077 Bordeaux, France 3 INCELL Corporation, San Antonio, TX 78249, USA 4 EA 3842, Homéostasie Cellulaire et Pathologies, Université de Limoges, 87025 Limoges cedex, France Correspondence to: Muriel Priault, e-mail: muriel.priault@ibgc.cnrs.fr Keywords: Bcl-x L , autophagy, apoptosis, cancer, post-translational modification Received: September 29, 2015      Accepted: January 31, 2016      Published: March 06, 2016 ABSTRACT Bcl-x L is a member of the Bcl-2 family, playing a critical role in the survival of tumor cells. Here, we show that Bcl-x L oncogenic function can be uncoupled from its anti-apoptotic activity when it is regulated by the post-translational deamidation of its Asn52. Bcl-x L activity can be regulated by post-translational modifications: deamidation of Asn52 and 66 into Asp residues was reported to occur exclusively in response to DNA damage, and to cripple its anti-apoptotic activity. Our work reports for the first time the spontaneous occurrence of monodeamidated Asp 52 Bcl-x L in control conditions, in vivo and in vitro . In the normal and cancer cell lines tested, no less than 30% and up to 56% of Bcl-x L was singly deamidated on Asn 52 . Functional analyses revealed that singly deamidated Bcl-x L retains anti-apoptotic functions, and exhibits enhanced autophagic activity while harboring impaired clonogenic and tumorigenic properties compared to native Bcl-x L . Additionally, Asp 52 Bcl-x L remains phosphorylatable, and thus is still an eligible target of anti-neoplasic agents. Altogether our results complement the existing data on Bcl-x L deamidation: they challenge the common acceptance that Asn52 and Asn66 are equally eligible for deamidation, and provide a valuable improvement of our knowledge on the regulation of Bcl-x L oncogenic functions by deamidation." @default.
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• W2300250957 date "2016-03-06" @default.
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• W2300250957 title "N52 monodeamidated Bcl-xL shows impaired oncogenic properties<i>in vivo</i>and<i>in vitro</i>" @default.
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• W2300250957 doi "https://doi.org/10.18632/oncotarget.7938" @default.
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