RPAP3 splicing variant isoform 1 interacts with PIH1D1 to compose R2TP complex for cell survival

Miki Yoshida; Makio Saeki; Hiroshi Egusa; Yasuyuki Irie; Yuya Kamano; Shinya Uraguchi; Maki Sotozono; Hitoshi Niwa; Yoshinori Kamisaki

doi:10.1016/j.bbrc.2012.11.017

RPAP3 splicing variant isoform 1 interacts with PIH1D1 to compose R2TP complex for cell survival

Miki Yoshida, Makio Saeki, Hiroshi Egusa, Yasuyuki Irie, Yuya Kamano, Shinya Uraguchi, Maki Sotozono, Hitoshi Niwa, Yoshinori Kamisaki

Research output: Contribution to journal › Article › peer-review

17 Citations (Scopus)

Abstract

We previously characterized RNA polymerase II-associated protein 3 (RPAP3) as a cell death enhancer. Here we report the identification and characterization of splicing isoform of RPAP3, isoform 1 and 2. We investigated the interaction between RPAP3 and PIH1 domain containing protein 1 (PIH1D1), and found that RPAP3 isoform 1, but not isoform 2, interacted with PIH1D1. Furthermore, knockdown of RPAP3 isoform 1 by small interfering RNA down-regulated PIH1D1 protein level without affecting PIH1D1 mRNA. RPAP3 isoform 2 potentiated doxorubicin-induced cell death in human breast cancer T-47 cells although isoform 1 showed no effect. These results suggest that R2TP complex is composed of RPAP3 isoform 1 for its stabilization, and that RPAP3 isoform 2 may have a dominant negative effect on the survival potency of R2TP complex.

Original language	English
Pages (from-to)	320-324
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	430
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2012.11.017
Publication status	Published - 2013 Jan 4

Keywords

Monad
PIH1D1
Pontin
R2TP
Reptin
RPAP3
WDR92

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.bbrc.2012.11.017

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title = "RPAP3 splicing variant isoform 1 interacts with PIH1D1 to compose R2TP complex for cell survival",

abstract = "We previously characterized RNA polymerase II-associated protein 3 (RPAP3) as a cell death enhancer. Here we report the identification and characterization of splicing isoform of RPAP3, isoform 1 and 2. We investigated the interaction between RPAP3 and PIH1 domain containing protein 1 (PIH1D1), and found that RPAP3 isoform 1, but not isoform 2, interacted with PIH1D1. Furthermore, knockdown of RPAP3 isoform 1 by small interfering RNA down-regulated PIH1D1 protein level without affecting PIH1D1 mRNA. RPAP3 isoform 2 potentiated doxorubicin-induced cell death in human breast cancer T-47 cells although isoform 1 showed no effect. These results suggest that R2TP complex is composed of RPAP3 isoform 1 for its stabilization, and that RPAP3 isoform 2 may have a dominant negative effect on the survival potency of R2TP complex.",

keywords = "Monad, PIH1D1, Pontin, R2TP, Reptin, RPAP3, WDR92",

author = "Miki Yoshida and Makio Saeki and Hiroshi Egusa and Yasuyuki Irie and Yuya Kamano and Shinya Uraguchi and Maki Sotozono and Hitoshi Niwa and Yoshinori Kamisaki",

note = "Funding Information: This study was supported in part by Japan Society for the Promotion of Science Grants C24592795 and the Osaka Medical Research Foundation for Incurable Diseases.",

year = "2013",

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doi = "10.1016/j.bbrc.2012.11.017",

language = "English",

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T1 - RPAP3 splicing variant isoform 1 interacts with PIH1D1 to compose R2TP complex for cell survival

AU - Yoshida, Miki

AU - Saeki, Makio

AU - Egusa, Hiroshi

AU - Irie, Yasuyuki

AU - Kamano, Yuya

AU - Uraguchi, Shinya

AU - Sotozono, Maki

AU - Niwa, Hitoshi

AU - Kamisaki, Yoshinori

N1 - Funding Information: This study was supported in part by Japan Society for the Promotion of Science Grants C24592795 and the Osaka Medical Research Foundation for Incurable Diseases.

PY - 2013/1/4

Y1 - 2013/1/4

N2 - We previously characterized RNA polymerase II-associated protein 3 (RPAP3) as a cell death enhancer. Here we report the identification and characterization of splicing isoform of RPAP3, isoform 1 and 2. We investigated the interaction between RPAP3 and PIH1 domain containing protein 1 (PIH1D1), and found that RPAP3 isoform 1, but not isoform 2, interacted with PIH1D1. Furthermore, knockdown of RPAP3 isoform 1 by small interfering RNA down-regulated PIH1D1 protein level without affecting PIH1D1 mRNA. RPAP3 isoform 2 potentiated doxorubicin-induced cell death in human breast cancer T-47 cells although isoform 1 showed no effect. These results suggest that R2TP complex is composed of RPAP3 isoform 1 for its stabilization, and that RPAP3 isoform 2 may have a dominant negative effect on the survival potency of R2TP complex.

AB - We previously characterized RNA polymerase II-associated protein 3 (RPAP3) as a cell death enhancer. Here we report the identification and characterization of splicing isoform of RPAP3, isoform 1 and 2. We investigated the interaction between RPAP3 and PIH1 domain containing protein 1 (PIH1D1), and found that RPAP3 isoform 1, but not isoform 2, interacted with PIH1D1. Furthermore, knockdown of RPAP3 isoform 1 by small interfering RNA down-regulated PIH1D1 protein level without affecting PIH1D1 mRNA. RPAP3 isoform 2 potentiated doxorubicin-induced cell death in human breast cancer T-47 cells although isoform 1 showed no effect. These results suggest that R2TP complex is composed of RPAP3 isoform 1 for its stabilization, and that RPAP3 isoform 2 may have a dominant negative effect on the survival potency of R2TP complex.

KW - Monad

KW - PIH1D1

KW - Pontin

KW - R2TP

KW - Reptin

KW - RPAP3

KW - WDR92

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JO - Biochemical and Biophysical Research Communications

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RPAP3 splicing variant isoform 1 interacts with PIH1D1 to compose R2TP complex for cell survival

Abstract

Keywords

UN SDGs

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