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TRPV4-dependent induction of a novel mammalian cold-inducible protein SRSF5 as well as CIRP and RBM3

Cold-inducible RNA-binding protein (CIRP) and RNA-binding motif protein 3 (RBM3) are two evolutionarily conserved RNA-binding proteins that are structurally related to hnRNPs and upregulated in response to moderately low temperatures in mammalian cells. Although contributions of splicing efficiency,...

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Autores principales: Fujita, Takanori, Higashitsuji, Hiroaki, Higashitsuji, Hisako, Liu, Yu, Itoh, Katsuhiko, Sakurai, Toshiharu, Kojima, Takahiro, Kandori, Shuya, Nishiyama, Hiroyuki, Fukumoto, Motoi, Fukumoto, Manabu, Shibasaki, Koji, Fujita, Jun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5442135/
https://www.ncbi.nlm.nih.gov/pubmed/28536481
http://dx.doi.org/10.1038/s41598-017-02473-x
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author Fujita, Takanori
Higashitsuji, Hiroaki
Higashitsuji, Hisako
Liu, Yu
Itoh, Katsuhiko
Sakurai, Toshiharu
Kojima, Takahiro
Kandori, Shuya
Nishiyama, Hiroyuki
Fukumoto, Motoi
Fukumoto, Manabu
Shibasaki, Koji
Fujita, Jun
author_facet Fujita, Takanori
Higashitsuji, Hiroaki
Higashitsuji, Hisako
Liu, Yu
Itoh, Katsuhiko
Sakurai, Toshiharu
Kojima, Takahiro
Kandori, Shuya
Nishiyama, Hiroyuki
Fukumoto, Motoi
Fukumoto, Manabu
Shibasaki, Koji
Fujita, Jun
author_sort Fujita, Takanori
collection PubMed
description Cold-inducible RNA-binding protein (CIRP) and RNA-binding motif protein 3 (RBM3) are two evolutionarily conserved RNA-binding proteins that are structurally related to hnRNPs and upregulated in response to moderately low temperatures in mammalian cells. Although contributions of splicing efficiency, the gene promoters activated upon mild hypothermia and the transcription factor Sp1 to induction of CIRP have been reported, precise mechanisms by which hypothermia and other stresses induce the expression of mammalian cold-inducible proteins (CIPs) are poorly understood. By screening the serine/arginine-rich splicing factors (SRSFs), we report that the transcript and protein levels of SRSF5 were increased in mammalian cells cultured at 32 °C. Expression of SRSF5 as well as CIRP and RBM3 were also induced by DNA damage, hypoxia, cycloheximide and hypotonicity. Immunohistochemical studies demonstrated that SRSF5 was constitutively expressed in male germ cells and the level was decreased in human testicular germ cell tumors. SRSF5 facilitated production of p19 H-RAS, and increased sensitivity to doxorubicin in human U-2 OS cells. Induction of CIPs was dependent on transient receptor potential vanilloid 4 (TRPV4) channel protein, but seemed independent of its ion channel activity. These findings indicate a previously unappreciated role for the TRP protein in linking environmental stress to splicing.
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spelling pubmed-54421352017-05-25 TRPV4-dependent induction of a novel mammalian cold-inducible protein SRSF5 as well as CIRP and RBM3 Fujita, Takanori Higashitsuji, Hiroaki Higashitsuji, Hisako Liu, Yu Itoh, Katsuhiko Sakurai, Toshiharu Kojima, Takahiro Kandori, Shuya Nishiyama, Hiroyuki Fukumoto, Motoi Fukumoto, Manabu Shibasaki, Koji Fujita, Jun Sci Rep Article Cold-inducible RNA-binding protein (CIRP) and RNA-binding motif protein 3 (RBM3) are two evolutionarily conserved RNA-binding proteins that are structurally related to hnRNPs and upregulated in response to moderately low temperatures in mammalian cells. Although contributions of splicing efficiency, the gene promoters activated upon mild hypothermia and the transcription factor Sp1 to induction of CIRP have been reported, precise mechanisms by which hypothermia and other stresses induce the expression of mammalian cold-inducible proteins (CIPs) are poorly understood. By screening the serine/arginine-rich splicing factors (SRSFs), we report that the transcript and protein levels of SRSF5 were increased in mammalian cells cultured at 32 °C. Expression of SRSF5 as well as CIRP and RBM3 were also induced by DNA damage, hypoxia, cycloheximide and hypotonicity. Immunohistochemical studies demonstrated that SRSF5 was constitutively expressed in male germ cells and the level was decreased in human testicular germ cell tumors. SRSF5 facilitated production of p19 H-RAS, and increased sensitivity to doxorubicin in human U-2 OS cells. Induction of CIPs was dependent on transient receptor potential vanilloid 4 (TRPV4) channel protein, but seemed independent of its ion channel activity. These findings indicate a previously unappreciated role for the TRP protein in linking environmental stress to splicing. Nature Publishing Group UK 2017-05-23 /pmc/articles/PMC5442135/ /pubmed/28536481 http://dx.doi.org/10.1038/s41598-017-02473-x Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Fujita, Takanori
Higashitsuji, Hiroaki
Higashitsuji, Hisako
Liu, Yu
Itoh, Katsuhiko
Sakurai, Toshiharu
Kojima, Takahiro
Kandori, Shuya
Nishiyama, Hiroyuki
Fukumoto, Motoi
Fukumoto, Manabu
Shibasaki, Koji
Fujita, Jun
TRPV4-dependent induction of a novel mammalian cold-inducible protein SRSF5 as well as CIRP and RBM3
title TRPV4-dependent induction of a novel mammalian cold-inducible protein SRSF5 as well as CIRP and RBM3
title_full TRPV4-dependent induction of a novel mammalian cold-inducible protein SRSF5 as well as CIRP and RBM3
title_fullStr TRPV4-dependent induction of a novel mammalian cold-inducible protein SRSF5 as well as CIRP and RBM3
title_full_unstemmed TRPV4-dependent induction of a novel mammalian cold-inducible protein SRSF5 as well as CIRP and RBM3
title_short TRPV4-dependent induction of a novel mammalian cold-inducible protein SRSF5 as well as CIRP and RBM3
title_sort trpv4-dependent induction of a novel mammalian cold-inducible protein srsf5 as well as cirp and rbm3
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5442135/
https://www.ncbi.nlm.nih.gov/pubmed/28536481
http://dx.doi.org/10.1038/s41598-017-02473-x
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