A
Anne Bertolotti
Researcher at Laboratory of Molecular Biology
Publications - 51
Citations - 14781
Anne Bertolotti is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Endoplasmic reticulum & Unfolded protein response. The author has an hindex of 30, co-authored 49 publications receiving 13457 citations. Previous affiliations of Anne Bertolotti include French Institute of Health and Medical Research & Medical Research Council.
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Journal ArticleDOI
Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.
Fumihiko Urano,Xiaozhong Wang,Anne Bertolotti,Yuhong Zhang,Peter Chung,Heather P. Harding,David Ron +6 more
TL;DR: Malfolded proteins in the endoplasmic reticulum induce cellular stress and activate c-Jun amino-terminal kinases (JNKs or SAPKs), and Mammalian homologs of yeast IRE1, which activate chaperone genes in response to ER stress, also activated JNK, and I RE1alpha-/- fibroblasts were impaired in JNK activation by ER stress.
Journal ArticleDOI
Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
Anne Bertolotti,Yuhong Zhang,Linda M. Hendershot,Linda M. Hendershot,Heather P. Harding,David Ron +5 more
TL;DR: In this article, the lumenal domains of transmembrane protein kinases (PERK and IRE1) were found to be functionally interchangeable in mediating an ER stress response and that in unstressed cells, both L1 and L2 domains formed a stable complex with the ER chaperone BiP.
Dynamic interaction of BiP and ER stress transducers in the unfolded
TL;DR: It is shown that the lumenal domains of these two proteins are functionally interchangeable in mediating an ER stress response and that, in unstressed cells, both lumenAL domains form a stable complex with the ER chaperone BiP.
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Perk Is Essential for Translational Regulation and Cell Survival during the Unfolded Protein Response
TL;DR: In this paper, the authors report that mutating the gene encoding the ER stress-activated eIF2alpha kinase PERK abolishes the phosphorylation of eIF 2 alpha in response to accumulation of malfolded proteins in the ER resulting in abnormally elevated protein synthesis and higher levels of ER stress.
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Sustained translational repression by eIF2α-P mediates prion neurodegeneration
Julie A. Moreno,Helois Radford,Diego Peretti,Joern R. Steinert,Nicholas Verity,Maria Guerra Martin,Mark Halliday,Jason Morgan,David Dinsdale,Catherine A. Ortori,David A. Barrett,Pavel Tsaytler,Anne Bertolotti,Anne E. Willis,Martin Bushell,Giovanna R. Mallucci +15 more
TL;DR: It is shown that accumulation of prion protein during prion replication causes persistent translational repression of global protein synthesis by eIF2α-P, associated with synaptic failure and neuronal loss in prion-diseased mice, and that promoting translational recovery in hippocampi of prionsinfected mice is neuroprotective.