Academic Journal

The prolyl-isomerase PIN1 is essential for nuclear Lamin-B structure and function and protects heterochromatin under mechanical stress

التفاصيل البيبلوغرافية
العنوان: The prolyl-isomerase PIN1 is essential for nuclear Lamin-B structure and function and protects heterochromatin under mechanical stress
المؤلفون: Francesco Napoletano, Gloria Ferrari Bravo, Ilaria Anna Pia Voto, Aurora Santin, Lucia Celora, Elena Campaner, Clara Dezi, Arianna Bertossi, Elena Valentino, Mariangela Santorsola, Alessandra Rustighi, Valentina Fajner, Elena Maspero, Federico Ansaloni, Valeria Cancila, Cesare Fabio Valenti, Manuela Santo, Osvaldo Basilio Artimagnella, Sara Finaurini, Ubaldo Gioia, Simona Polo, Remo Sanges, Claudio Tripodo, Antonello Mallamaci, Stefano Gustincich, Fabrizio d’Adda di Fagagna, Fiamma Mantovani, Valeria Specchia, Giannino Del Sal
المصدر: Cell Reports, Vol 36, Iss 11, Pp 109694- (2021)
بيانات النشر: Elsevier, 2021.
سنة النشر: 2021
المجموعة: LCC:Biology (General)
مصطلحات موضوعية: Drosophila, PIN1, transposons, neurodegeneration, heterochromatin, HP1, Biology (General), QH301-705.5
الوصف: Summary: Chromatin organization plays a crucial role in tissue homeostasis. Heterochromatin relaxation and consequent unscheduled mobilization of transposable elements (TEs) are emerging as key contributors of aging and aging-related pathologies, including Alzheimer’s disease (AD) and cancer. However, the mechanisms governing heterochromatin maintenance or its relaxation in pathological conditions remain poorly understood. Here we show that PIN1, the only phosphorylation-specific cis/trans prolyl isomerase, whose loss is associated with premature aging and AD, is essential to preserve heterochromatin. We demonstrate that this PIN1 function is conserved from Drosophila to humans and prevents TE mobilization-dependent neurodegeneration and cognitive defects. Mechanistically, PIN1 maintains nuclear type-B Lamin structure and anchoring function for heterochromatin protein 1α (HP1α). This mechanism prevents nuclear envelope alterations and heterochromatin relaxation under mechanical stress, which is a key contributor to aging-related pathologies.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2211-1247
Relation: http://www.sciencedirect.com/science/article/pii/S2211124721011414; https://doaj.org/toc/2211-1247
DOI: 10.1016/j.celrep.2021.109694
URL الوصول: https://doaj.org/article/e42ceae700674016b2bc9029cf16e18c
رقم الانضمام: edsdoj.42ceae700674016b2bc9029cf16e18c
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:22111247
DOI:10.1016/j.celrep.2021.109694