A New STAT3-binding Partner, ARL3, Enhances the Phosphorylation and Nuclear Accumulation of STAT3
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.
Journal
-
- Journal of Biological Chemistry (JBC)
-
Journal of Biological Chemistry (JBC) 291 (21), 11161-11171, 2016-05-20
American Society for Biochemistry and Molecular Biology (ASBMB)
- Tweet
Details 詳細情報について
-
- CRID
- 1050564288973989632
-
- NII Article ID
- 120006219975
-
- HANDLE
- 2115/65506
-
- ISSN
- 00219258
-
- Text Lang
- en
-
- Article Type
- journal article
-
- Data Source
-
- IRDB
- CiNii Articles