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

Author

Napoletano F, Ferrari Bravo G, Voto IAP, Santin A, Celora L, Campaner E, Dezi C, Bertossi A, Valentino E, Santorsola M, Rustighi A, Fajner V, Maspero E, Ansaloni F, Cancila V, Valenti CF, Santo M, Artimagnella OB, Finaurini S, Gioia U, Polo S, Sanges R, Tripodo C, Mallamaci A, Gustincich S, d'Adda di Fagagna F, Mantovani F, Specchia V, and Del Sal G

Subjects
Alzheimer Disease metabolism, Alzheimer Disease pathology, Animals, Cells, Cultured, Chromobox Protein Homolog 5 genetics, Chromobox Protein Homolog 5 metabolism, DNA Transposable Elements genetics, Drosophila metabolism, Drosophila Proteins antagonists & inhibitors, Drosophila Proteins genetics, Humans, Lamin Type B chemistry, Mice, Mice, Inbred C57BL, NIMA-Interacting Peptidylprolyl Isomerase antagonists & inhibitors, NIMA-Interacting Peptidylprolyl Isomerase genetics, Neocortex cytology, Neocortex metabolism, Neurons cytology, Neurons metabolism, Nuclear Envelope chemistry, Peptidylprolyl Isomerase antagonists & inhibitors, Peptidylprolyl Isomerase genetics, Phosphorylation, RNA Interference, RNA, Small Interfering metabolism, Drosophila Proteins metabolism, Heterochromatin metabolism, Lamin Type B metabolism, NIMA-Interacting Peptidylprolyl Isomerase metabolism, Peptidylprolyl Isomerase metabolism, Stress, Mechanical
Abstract

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., Competing Interests: Declaration of interests The authors declare no competing interests., (Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved.)

Published
2021
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2. The prolyl-isomerase PIN1 is essential for nuclear Lamin-B structure and function and protects heterochromatin under mechanical stress

Author

Valentina Fajner, Alessandra Rustighi, Ilaria Anna Pia Voto, Valeria Specchia, Stefano Gustincich, Clara Dezi, Elena Valentino, Valeria Cancila, Fabrizio d'Adda di Fagagna, Elena Maspero, Remo Sanges, Francesco Napoletano, Elena Campaner, Claudio Tripodo, Sara Finaurini, Antonello Mallamaci, Federico Ansaloni, Gloria Ferrari Bravo, Arianna Bertossi, Fiamma Mantovani, Lucia Celora, Mariangela Santorsola, Manuela Santo, Giannino Del Sal, Ubaldo Gioia, Osvaldo Basilio Artimagnella, Simona Polo, Aurora Santin, Cesare Valenti, Napoletano, F., Ferrari Bravo, G., Voto, I. A. P., Santin, A., Celora, L., Campaner, E., Dezi, C., Bertossi, A., Valentino, E., Santorsola, M., Rustighi, A., Fajner, V., Maspero, E., Ansaloni, F., Cancila, V., Valenti, C. F., Santo, M., Artimagnella, O. B., Finaurini, S., Gioia, U., Polo, S., Sanges, R., Tripodo, C., Mallamaci, A., Gustincich, S., d'Adda di Fagagna, F., Mantovani, F., Specchia, V., Del Sal, G., Napoletano F., Ferrari Bravo G., Voto I.A.P., Santin A., Celora L., Campaner E., Dezi C., Bertossi A., Valentino E., Santorsola M., Rustighi A., Fajner V., Maspero E., Ansaloni F., Cancila V., Valenti C.F., Santo M., Artimagnella O.B., Finaurini S., Gioia U., Polo S., Sanges R., Tripodo C., Mallamaci A., Gustincich S., d'Adda di Fagagna F., Mantovani F., Specchia V., and Del Sal G.

Subjects
transposons, Neocortex, Mice, Heterochromatin, Prolyl isomerase, Drosophila Proteins, Biology (General), Phosphorylation, RNA, Small Interfering, Tissue homeostasis, Cells, Cultured, Settore ING-INF/05 - Sistemi Di Elaborazione Delle Informazioni, Neurons, Lamin Type B, Chemistry, HP1, phosphorylation, neurodegeneration, nuclear envelope, Peptidylprolyl Isomerase, Cell biology, Drosophila, heterochromatin, HP1, Lamin, mechanical stress, neurodegeneration, nuclear envelope, phosphorylation, PIN1, transposons, Nuclear lamina, Drosophila, RNA Interference, Premature aging, QH301-705.5, Nuclear Envelope, heterochromatin, Lamin, mechanical stress, PIN1, Settore BIO/11 - Biologia Molecolare, Settore MED/08 - Anatomia Patologica, General Biochemistry, Genetics and Molecular Biology, Alzheimer Disease, Settore MED/05 - Patologia Clinica, Animals, Humans, Heterochromatin maintenance, mechanical stre, Mice, Inbred C57BL, NIMA-Interacting Peptidylprolyl Isomerase, Chromobox Protein Homolog 5, DNA Transposable Elements, Heterochromatin protein 1, Stress, Mechanical
Abstract

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.

Published
2021

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