HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Faculty of Pharmaceutical Sciences >
Peer-reviewed Journal Articles, etc >

A New STAT3-binding Partner, ARL3, Enhances the Phosphorylation and Nuclear Accumulation of STAT3

Files in This Item:
manuscript.pdf2.04 MBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/65506

Title: A New STAT3-binding Partner, ARL3, Enhances the Phosphorylation and Nuclear Accumulation of STAT3
Authors: Togi, Sumihito Browse this author
Muromoto, Ryuta Browse this author →KAKEN DB
Hirashima, Koki Browse this author
Kitai, Yuichi Browse this author →KAKEN DB
Okayama, Taichiro Browse this author
Ikeda, Osamu Browse this author
Matsumoto, Naoki Browse this author
Kon, Shigeyuki Browse this author →KAKEN DB
Sekine, Yuichi Browse this author →KAKEN DB
Oritani, Kenji Browse this author →KAKEN DB
Matsuda, Tadashi Browse this author →KAKEN DB
Keywords: gene transcription
nuclear translocation
protein phosphorylation
signal transduction
STAT3
Issue Date: 20-May-2016
Publisher: American Society for Biochemistry and Molecular Biology (ASBMB)
Journal Title: Journal of Biological Chemistry (JBC)
Volume: 291
Issue: 21
Start Page: 11161
End Page: 11171
Publisher DOI: 10.1074/jbc.M116.724849
Abstract: Signal transducer and activator of transcription 3 (STAT3) is involved in cell proliferation, differentiation, and cell survival during immune responses, hematopoiesis, neurogenesis, and other biological processes. STAT3 activity is regulated by a variety of mechanisms, including phosphorylation and nuclear translocation. To clarify the molecular mechanisms underlying the regulation of STAT3 activity, we performed yeast two-hybrid screening. We identified ARL3 (ADP-ribosylation factor-like 3) as a novel STAT3-binding partner. ARL3 recognizes the DNA-binding domain as well as the C-terminal region of STAT3 in vivo, and their binding was the strongest when both proteins were activated. Importantly, small interfering RNA-mediated reduction of endogenous ARL3 expression decreased IL-6-induced tyrosine phosphorylation, nuclear accumulation, and transcriptional activity of STAT3. These results indicate that ARL3 interacts with STAT3 and regulates the transcriptional activation of STAT3 by influencing its nuclear accumulation of STAT3.
Rights: This research was originally published in Journal of Biological Chemistry. Sumihito Togi, Ryuta Muromoto, Koki Hirashima, Yuichi Kitai, Taichiro Okayama, Osamu Ikeda, Naoki Matsumoto, Shigeyuki Kon, Yuichi Sekine, Kenji Oritani and Tadashi Matsuda. A New STAT3-binding Partner, ARL3, Enhances the Phosphorylation and Nuclear Accumulation of STAT3. Journal of Biological Chemistry. 2016; Vol.291:11161-11171. ©the American Society for Biochemistry and Molecular Biology.
Type: article
URI: http://hdl.handle.net/2115/65506
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 松田 正

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 

 - Hokkaido University