ID 106361
Author
Kano, Shizuka Department of Stress Science, Institute of Health Biosciences, the University of Tokushima Graduate School|Student Lab, the University of Tokushima Faculty of Medicine
Nishida, Kensei Department of Stress Science, Institute of Health Biosciences, the University of Tokushima Graduate School Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Nishiyama, Chihiro Student Lab, the University of Tokushima Faculty of Medicine
Akaike, Yoko Department of Stress Science, Institute of Health Biosciences, the University of Tokushima Graduate School
Kajita, Keisuke Department of Stress Science, Institute of Health Biosciences, the University of Tokushima Graduate School
Kurokawa, Ken Department of Stress Science, Institute of Health Biosciences, the University of Tokushima Graduate School
Masuda, Kiyoshi Department of Stress Science, Institute of Health Biosciences, the University of Tokushima Graduate School KAKEN Search Researchers
Kuwano, Yuki Department of Stress Science, Institute of Health Biosciences, the University of Tokushima Graduate School Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Tanahashi, Toshihito Department of Stress Science, Institute of Health Biosciences, the University of Tokushima Graduate School
Rokutan, Kazuhito Department of Stress Science, Institute of Health Biosciences, the University of Tokushima Graduate School Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Keywords
truncated SRSF3 protein
oxidative stress
cell growth
c-Jun
Content Type
Journal Article
Description
Serine/arginine-rich splicing factor 3 (SRSF3), a member of the SRSF family, plays a wide-ranging role in gene expression. The human SRSF3 gene generates a major mRNA isoform encoding a functional, full-length protein and a PTC-containing isoform (SRSF3-PTC). The latter is expected to be degraded through the nonsense-mediated mRNA decay system. However, it was reported that SRSF3-PTC mRNA was produced under stressful conditions and translated into a truncated SRSF3 protein (SRSF3-TR). To disclose unknown functions of SRSF3-TR, we established Flp-In-293 cells stably expressing SRSF3-TR. The SRSF3-TR-expressing cells increased mRNA and protein levels of positive regulators for G1 to S phase transition (cyclin D1, cyclin D3, CDC25A, and E2F1) and accelerated their growth. c-Jun is required for progression through the G1 phase, the mechanism by which involves transcriptional control of the cyclin D1 gene. We also found that the JUN promoter activity was significantly increased in the Flp-In-293 cells stably expressing SRSF3-TR, compared with mock-transfected control cells. The SRSF3-TR-expressing cells increased c-Jun and Sp-1 levels, which are important for the positive autoregulation and basal transcription of JUN, respectively. Our results suggest that stress-inducible SRSF3-TR may participate in the acceleration of cell growth through facilitating c-Jun-mediated G1 progression under stressful conditions.
Journal Title
The journal of medical investigation : JMI
ISSN
13431420
NCID
AA11166929
Volume
60
Issue
3-4
Start Page
228
End Page
235
Sort Key
228
Published Date
2013-08
EDB ID
FullText File
language
eng
TextVersion
Publisher
departments
Medical Sciences