Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates

Autor: François-Xavier Cantrelle, Anne Loyens, Xavier Trivelli, Oliver Reimann, Clément Despres, Neha S. Gandhi, Christian P. R. Hackenberger, Isabelle Landrieu, Caroline Smet-Nocca

Publikováno v: Frontiers in Molecular Neuroscience, Vol 14 (2021)

Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer’s disease (AD) brains. In recent years, other posttrans

Externí odkaz: https://doaj.org/article/8d012c8e67d54abab12653fa56319bc6

Conformation and Affinity Modulations by Multiple Phosphorylation Occurring in the BIN1 SH3 Domain Binding Site of the Tau Protein Proline-Rich Region

Autor: Alessia Lasorsa, Krishnendu Bera, Idir Malki, Elian Dupré, François-Xavier Cantrelle, Hamida Merzougui, Davy Sinnaeve, Xavier Hanoulle, Jozef Hritz, Isabelle Landrieu

Publikováno v: Biochemistry
Biochemistry, 2023, 62 (11), pp.1631-1642. ⟨10.1021/acs.biochem.2c00717⟩

International audience; An increase in phosphorylation of the Tau protein is associated with Alzheimer's disease (AD) progression through unclear molecular mechanisms. In general, phosphorylation modifies the interaction of intrinsically disordered p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0eb065a46bb40bcd3eed5979b7677031
https://doi.org/10.1021/acs.biochem.2c00717

Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases

Autor: Rasheduzzaman Chowdhury, Ivanhoe K. H. Leung, Ya-Min Tian, Martine I. Abboud, Wei Ge, Carmen Domene, François-Xavier Cantrelle, Isabelle Landrieu, Adam P. Hardy, Christopher W. Pugh, Peter J. Ratcliffe, Timothy D. W. Claridge, Christopher J. Schofield

Publikováno v: Nature Communications, Vol 7, Iss 1, Pp 1-10 (2016)

The response to hypoxia involves multiple genes regulated by the hypoxia inducible transcription factors (HIFs), whose stability is regulated by prolyl hydroxylation. Here the authors provide a molecular basis for the substrate selectivity of the HIF

Externí odkaz: https://doaj.org/article/bcbb0397431d45b6a10192b43d152868

Direct Crosstalk Between O-GlcNAcylation and Phosphorylation of Tau Protein Investigated by NMR Spectroscopy

Autor: Gwendoline Bourré, François-Xavier Cantrelle, Amina Kamah, Béatrice Chambraud, Isabelle Landrieu, Caroline Smet-Nocca

Publikováno v: Frontiers in Endocrinology, Vol 9 (2018)

The formation of intraneuronal fibrillar inclusions of tau protein is associated with several neurodegenerative diseases referred to as tauopathies including Alzheimer's disease (AD). A common feature of these pathologies is hyperphosphorylation of t

Externí odkaz: https://doaj.org/article/19617cec1dbb41d18e42d13e6c4ca4d2

Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding

Autor: Urmi Sengupta, Guilherme G. Moreira, Ana P. Carapeto, Filipa S. Carvalho, Andrea Quezada, Mário Rodrigues, Isabel Cardoso, Guenter Fritz, Nicha Puangmalai, Isabelle Landrieu, Federico Herrera, Rakez Kayed, Cláudio M. Gomes, Joana S. Cristóvão, François Xavier Cantrelle

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Nature Communications
Nature Communications, 2021, 12 (1), pp.6292. ⟨10.1038/s41467-021-26584-2⟩
Nature Communications, Nature Publishing Group, 2021, 12 (1), pp.6292. ⟨10.1038/s41467-021-26584-2⟩

The microtubule-associated protein tau is implicated in the formation of oligomers and fibrillar aggregates that evade proteostasis control and spread from cell-to-cell. Tau pathology is accompanied by sustained neuroinflammation and, while the relea

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d23f2b68f2ad4ec8da568e2c26024fca
https://doaj.org/article/c84f299d39b043bfadec87ae6bbc7bf3