Phosphorylation of threonine-265 in Zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines

Noriko Sato; Nobuyuki Kamada; Ryuta Muromoto; Taro Kawai; Kenji Sugiyama; Tadashi Watanabe; Seiyu Imoto; Yuichi Sekine; Norihiko Ohbayashi; Masato Ishida; Shizuo Akira; Tadashi Matsuda

doi:10.1016/j.imlet.2005.10.015

Phosphorylation of threonine-265 in Zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines

Noriko Sato, Nobuyuki Kamada, Ryuta Muromoto, Taro Kawai, Kenji Sugiyama, Tadashi Watanabe, Seiyu Imoto, Yuichi Sekine, Norihiko Ohbayashi, Masato Ishida, Shizuo Akira, Tadashi Matsuda

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18 Citations (Scopus)

Abstract

Zipper-interacting protein kinase (ZIPK) is a widely expressed serine/threonine kinase that has been implicated in cell death and transcriptional regulation, but its mechanism of regulation remains unknown. Here, we identified threonine-265 (Thr265) in ZIPK as a major autophosphorylation site. Mutational analyses revealed that autophosphorylation of Thr265 were essential for its full catalytic activity toward an exogenous substrate as well as for cell death induction. Furthermore, leukemia inhibitory factor (LIF) stimulated Thr265 phosphorylation of ZIPK, thereby leading to phosphorylation and activation of signal transducer and activator of transcription (STAT3). Taken together, our findings demonstrate that ZIPK is positively regulated through Thr265 phosphorylation and that this phosphorylation is essential for its function.

Original language	English
Pages (from-to)	127-134
Number of pages	8
Journal	Immunology Letters
Volume	103
Issue number	2
DOIs	https://doi.org/10.1016/j.imlet.2005.10.015
Publication status	Published - 2006 Mar 15
Externally published	Yes

Keywords

Apoptosis
IL-6
LIF
Phosphorylation
ZIPK

ASJC Scopus subject areas

Immunology and Allergy
Immunology

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10.1016/j.imlet.2005.10.015

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Sato, N., Kamada, N., Muromoto, R., Kawai, T., Sugiyama, K., Watanabe, T., Imoto, S., Sekine, Y., Ohbayashi, N., Ishida, M., Akira, S., & Matsuda, T. (2006). Phosphorylation of threonine-265 in Zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines. Immunology Letters, 103(2), 127-134. https://doi.org/10.1016/j.imlet.2005.10.015

Sato, N, Kamada, N, Muromoto, R, Kawai, T, Sugiyama, K, Watanabe, T, Imoto, S, Sekine, Y, Ohbayashi, N, Ishida, M, Akira, S & Matsuda, T 2006, 'Phosphorylation of threonine-265 in Zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines', Immunology Letters, vol. 103, no. 2, pp. 127-134. https://doi.org/10.1016/j.imlet.2005.10.015

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title = "Phosphorylation of threonine-265 in Zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines",

abstract = "Zipper-interacting protein kinase (ZIPK) is a widely expressed serine/threonine kinase that has been implicated in cell death and transcriptional regulation, but its mechanism of regulation remains unknown. Here, we identified threonine-265 (Thr265) in ZIPK as a major autophosphorylation site. Mutational analyses revealed that autophosphorylation of Thr265 were essential for its full catalytic activity toward an exogenous substrate as well as for cell death induction. Furthermore, leukemia inhibitory factor (LIF) stimulated Thr265 phosphorylation of ZIPK, thereby leading to phosphorylation and activation of signal transducer and activator of transcription (STAT3). Taken together, our findings demonstrate that ZIPK is positively regulated through Thr265 phosphorylation and that this phosphorylation is essential for its function.",

keywords = "Apoptosis, IL-6, LIF, Phosphorylation, ZIPK",

author = "Noriko Sato and Nobuyuki Kamada and Ryuta Muromoto and Taro Kawai and Kenji Sugiyama and Tadashi Watanabe and Seiyu Imoto and Yuichi Sekine and Norihiko Ohbayashi and Masato Ishida and Shizuo Akira and Tadashi Matsuda",

note = "Funding Information: This work was supported in part by grants from Ministry of Education, Culture, Sports, Science and Technology of the Japanese Government, AstraZeneca Research Grant 2003, the Naito Foundation, the Akiyama Foundation and the Sasakawa Scientific Research Grant from the Japan Science Society.",

year = "2006",

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doi = "10.1016/j.imlet.2005.10.015",

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AU - Sato, Noriko

AU - Kamada, Nobuyuki

AU - Muromoto, Ryuta

AU - Kawai, Taro

AU - Sugiyama, Kenji

AU - Watanabe, Tadashi

AU - Imoto, Seiyu

AU - Sekine, Yuichi

AU - Ohbayashi, Norihiko

AU - Ishida, Masato

AU - Akira, Shizuo

AU - Matsuda, Tadashi

N1 - Funding Information: This work was supported in part by grants from Ministry of Education, Culture, Sports, Science and Technology of the Japanese Government, AstraZeneca Research Grant 2003, the Naito Foundation, the Akiyama Foundation and the Sasakawa Scientific Research Grant from the Japan Science Society.

PY - 2006/3/15

Y1 - 2006/3/15

N2 - Zipper-interacting protein kinase (ZIPK) is a widely expressed serine/threonine kinase that has been implicated in cell death and transcriptional regulation, but its mechanism of regulation remains unknown. Here, we identified threonine-265 (Thr265) in ZIPK as a major autophosphorylation site. Mutational analyses revealed that autophosphorylation of Thr265 were essential for its full catalytic activity toward an exogenous substrate as well as for cell death induction. Furthermore, leukemia inhibitory factor (LIF) stimulated Thr265 phosphorylation of ZIPK, thereby leading to phosphorylation and activation of signal transducer and activator of transcription (STAT3). Taken together, our findings demonstrate that ZIPK is positively regulated through Thr265 phosphorylation and that this phosphorylation is essential for its function.

AB - Zipper-interacting protein kinase (ZIPK) is a widely expressed serine/threonine kinase that has been implicated in cell death and transcriptional regulation, but its mechanism of regulation remains unknown. Here, we identified threonine-265 (Thr265) in ZIPK as a major autophosphorylation site. Mutational analyses revealed that autophosphorylation of Thr265 were essential for its full catalytic activity toward an exogenous substrate as well as for cell death induction. Furthermore, leukemia inhibitory factor (LIF) stimulated Thr265 phosphorylation of ZIPK, thereby leading to phosphorylation and activation of signal transducer and activator of transcription (STAT3). Taken together, our findings demonstrate that ZIPK is positively regulated through Thr265 phosphorylation and that this phosphorylation is essential for its function.

KW - Apoptosis

KW - IL-6

KW - LIF

KW - Phosphorylation

KW - ZIPK

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ER -

Phosphorylation of threonine-265 in Zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines

Abstract

Keywords

ASJC Scopus subject areas

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