TY - JOUR
T1 - Serum response factor is modulated by the SUMO-1 conjugation system
AU - Matsuzaki, Kazuhito
AU - Minami, Takeshi
AU - Tojo, Masahide
AU - Honda, Yoshiomi
AU - Uchimura, Yasuhiro
AU - Saitoh, Hisato
AU - Yasuda, Hideyo
AU - Nagahiro, Shinji
AU - Saya, Hideyuki
AU - Nakao, Mitsuyoshi
N1 - Funding Information:
This work was supported by a Grant-in-Aid for Scientific Research on Priority Areas, by Special Coordination Funds for Promoting Science and Technology, by Grant-in-Aid for 21st Century COE Research from the Ministry of Education, Culture, Sports, Science and Technology, the Japanese Government, and by The Grant of the Princess Takamatsu Cancer Research Fund (M.N.).
PY - 2003/6/20
Y1 - 2003/6/20
N2 - Serum stimulation leads to activation of the serum response factor (SRF)-mediated transcription of immediate-early genes such as c-fos via various signal transduction pathways. We have previously reported that promyelocytic leukemia protein (PML) is involved in the transcriptional regulation by SRF. PML is one of the well-known substrates for modification by small ubiquitin-related modifier-1 (SUMO-1) and several SUMO-1-modified proteins associate with PML. Here, we report that SRF is modified by SUMO-1 chiefly at lysine147 within the DNA-binding domain. Substitution of this target lysine for alanine did not affect the translocation of SRF to PML-nuclear bodies. The SRF mutant augmented the transcriptional activity under Rho A-stimulated condition but not under serum-starved condition, suggesting that activated SRF is suppressed by its sumoylation. These data support the transcriptional role of SUMO-1 conjugating system in cellular serum response.
AB - Serum stimulation leads to activation of the serum response factor (SRF)-mediated transcription of immediate-early genes such as c-fos via various signal transduction pathways. We have previously reported that promyelocytic leukemia protein (PML) is involved in the transcriptional regulation by SRF. PML is one of the well-known substrates for modification by small ubiquitin-related modifier-1 (SUMO-1) and several SUMO-1-modified proteins associate with PML. Here, we report that SRF is modified by SUMO-1 chiefly at lysine147 within the DNA-binding domain. Substitution of this target lysine for alanine did not affect the translocation of SRF to PML-nuclear bodies. The SRF mutant augmented the transcriptional activity under Rho A-stimulated condition but not under serum-starved condition, suggesting that activated SRF is suppressed by its sumoylation. These data support the transcriptional role of SUMO-1 conjugating system in cellular serum response.
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U2 - 10.1016/S0006-291X(03)00910-0
DO - 10.1016/S0006-291X(03)00910-0
M3 - Article
C2 - 12788062
AN - SCOPUS:0037716544
SN - 0006-291X
VL - 306
SP - 32
EP - 38
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -