Nuclear Envelope Budding is a Response to Cellular Stress

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2021 Jul 22

PMID 34290138

Citations 19

Authors

Dimitra Panagaki

Jacob T Croft

Katharina Keuenhof

Lisa Larsson Berglund

Stefanie Andersson

Verena Kohler

Sabrina Buttner

Markus J Tamas

Thomas Nystrom

Richard Neutze

Johanna L Hoog

Affiliations

Soon will be listed here.

Abstract

Nuclear envelope budding (NEB) is a recently discovered alternative pathway for nucleocytoplasmic communication distinct from the movement of material through the nuclear pore complex. Through quantitative electron microscopy and tomography, we demonstrate how NEB is evolutionarily conserved from early protists to human cells. In the yeast , NEB events occur with higher frequency during heat shock, upon exposure to arsenite or hydrogen peroxide, and when the proteasome is inhibited. Yeast cells treated with azetidine-2-carboxylic acid, a proline analog that induces protein misfolding, display the most dramatic increase in NEB, suggesting a causal link to protein quality control. This link was further supported by both localization of ubiquitin and Hsp104 to protein aggregates and NEB events, and the evolution of these structures during heat shock. We hypothesize that NEB is part of normal cellular physiology in a vast range of species and that in NEB comprises a stress response aiding the transport of protein aggregates across the nuclear envelope.

Citing Articles

Direct binding of arsenicals to nuclear transport factors disrupts nucleocytoplasmic transport.

Lorentzon E, Lee J, Masaryk J, Keuenhof K, Karlsson N, Galipaud C bioRxiv. 2025; .

PMID: 39868121 PMC: 11761705. DOI: 10.1101/2025.01.13.632748.

CLCC1 promotes membrane fusion during herpesvirus nuclear egress.

Dai B, Polack L, Sperl A, Dame H, Huynh T, Deveney C bioRxiv. 2024; .

PMID: 39386602 PMC: 11463520. DOI: 10.1101/2024.09.23.614151.

Vesicular translocation of PARP-1 to cytoplasm causes ADP-ribosylation and disassembly of vimentin filaments during microglia activation induced by LPS.

Chen R, Xie L, Fan Y, Hua X, Chung C Front Cell Neurosci. 2024; 18:1363154.

PMID: 38590714 PMC: 10999663. DOI: 10.3389/fncel.2024.1363154.

Nuclear pore dysfunction and disease: a complex opportunity.

Fare C, Rothstein J Nucleus. 2024; 15(1):2314297.

PMID: 38383349 PMC: 10883112. DOI: 10.1080/19491034.2024.2314297.

Nuclear envelope budding: Getting large macromolecular complexes out of the nucleus.

Sule K, Nakamura M, Parkhurst S Bioessays. 2023; 46(2):e2300182.

PMID: 38044581 PMC: 10843589. DOI: 10.1002/bies.202300182.

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