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Regulation of autophagy by nucleoporin Tpr

The nuclear pore complex (NPC) consists of a conserved set of ~30 different proteins, termed nucleoporins, and serves as a gateway for the exchange of materials between the cytoplasm and nucleus. Tpr (translocated promoter region) is a component of NPC that presumably localizes at intranuclear filam...

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Autores principales: Funasaka, Tatsuyoshi, Tsuka, Eriko, Wong, Richard W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3501823/
https://www.ncbi.nlm.nih.gov/pubmed/23170199
http://dx.doi.org/10.1038/srep00878
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author Funasaka, Tatsuyoshi
Tsuka, Eriko
Wong, Richard W.
author_facet Funasaka, Tatsuyoshi
Tsuka, Eriko
Wong, Richard W.
author_sort Funasaka, Tatsuyoshi
collection PubMed
description The nuclear pore complex (NPC) consists of a conserved set of ~30 different proteins, termed nucleoporins, and serves as a gateway for the exchange of materials between the cytoplasm and nucleus. Tpr (translocated promoter region) is a component of NPC that presumably localizes at intranuclear filaments. Here, we show that Tpr knockdown caused a severe reduction in the number of nuclear pores. Furthermore, our electron microscopy studies indicated a significant reduction in the number of inner nuclear filaments. In addition, Tpr siRNA treatment impaired cell growth and proliferation compared to control siRNA-treated cells. In Tpr-depleted cells, the levels of p53 and p21 proteins were enhanced. Surprisingly, Tpr depletion increased p53 nuclear accumulation and facilitated autophagy. Our study demonstrates for the first time that Tpr plays a role in autophagy through controlling HSP70 and HSF1 mRNA export, p53 trafficking with karyopherin CRM1, and potentially through direct transcriptional regulation of autophagy factors.
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spelling pubmed-35018232012-11-20 Regulation of autophagy by nucleoporin Tpr Funasaka, Tatsuyoshi Tsuka, Eriko Wong, Richard W. Sci Rep Article The nuclear pore complex (NPC) consists of a conserved set of ~30 different proteins, termed nucleoporins, and serves as a gateway for the exchange of materials between the cytoplasm and nucleus. Tpr (translocated promoter region) is a component of NPC that presumably localizes at intranuclear filaments. Here, we show that Tpr knockdown caused a severe reduction in the number of nuclear pores. Furthermore, our electron microscopy studies indicated a significant reduction in the number of inner nuclear filaments. In addition, Tpr siRNA treatment impaired cell growth and proliferation compared to control siRNA-treated cells. In Tpr-depleted cells, the levels of p53 and p21 proteins were enhanced. Surprisingly, Tpr depletion increased p53 nuclear accumulation and facilitated autophagy. Our study demonstrates for the first time that Tpr plays a role in autophagy through controlling HSP70 and HSF1 mRNA export, p53 trafficking with karyopherin CRM1, and potentially through direct transcriptional regulation of autophagy factors. Nature Publishing Group 2012-11-20 /pmc/articles/PMC3501823/ /pubmed/23170199 http://dx.doi.org/10.1038/srep00878 Text en Copyright © 2012, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-sa/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-ShareALike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/
spellingShingle Article
Funasaka, Tatsuyoshi
Tsuka, Eriko
Wong, Richard W.
Regulation of autophagy by nucleoporin Tpr
title Regulation of autophagy by nucleoporin Tpr
title_full Regulation of autophagy by nucleoporin Tpr
title_fullStr Regulation of autophagy by nucleoporin Tpr
title_full_unstemmed Regulation of autophagy by nucleoporin Tpr
title_short Regulation of autophagy by nucleoporin Tpr
title_sort regulation of autophagy by nucleoporin tpr
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3501823/
https://www.ncbi.nlm.nih.gov/pubmed/23170199
http://dx.doi.org/10.1038/srep00878
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