Serine 62 is a phosphorylation site in folliculin, the Birt-Hogg-Dube gene product

被引:18
作者
Wang, Lu
Kobayashi, Toshiyuki
Piao, Xianghua
Shiono, Masatoshi
Takagi, Yumiko
Mineki, Reiko [2 ]
Taka, Hikari [2 ]
Zhang, Danqing
Abe, Masaaki
Sun, Guodong
Hagiwara, Yoshiaki [3 ]
Okimoto, Kazuo [4 ]
Matsumoto, Izumi [5 ]
Kouchi, Mami [5 ]
Hino, Okio [1 ]
机构
[1] Juntendo Univ, Sch Med, Dept Pathol & Oncol, Bunkyo Ku, Tokyo 1138421, Japan
[2] Juntendo Univ, Sch Med, Div Prote & Biomol Sci, Tokyo 1138421, Japan
[3] Immunobiol Labs Co Ltd, Res & Dev, Fujioka, Gunma 3750005, Japan
[4] Dainippon Sumitomo Pharma Co Ltd, Res Adm, Osaka 5640053, Japan
[5] Dainippon Sumitomo Pharma Co Ltd, Safety Res Labs, Osaka 5540022, Japan
关键词
Birt-Hogg-Dube syndrome; Folliculin; 5 '-AMP-activated protein kinase; Phosphorylation; FLCN-interacting protein; BHD GENE; PROTEIN; IDENTIFICATION;
D O I
10.1016/j.febslet.2009.11.033
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Recently, it was reported that the product of Birt-Hogg-Dube syndrome gene (folliculin, FLCN) is directly phosphorylated by 5'-AMP-activated protein kinase (AMPK). In this study, we identified serine 62 (Ser62) as a phosphorylation site in FLCN and generated an anti-phospho-Ser62-FLCN antibody. Our analysis suggests that Ser62 phosphorylation is indirectly up-regulated by AMPK and that another residue is directly phosphorylated by AMPK. By binding with FLCN-interacting proteins (FNIP1 and FNIP2/FNIPL), Ser62 phosphorylation is increased. A phospho-mimic mutation at Ser62 enhanced the formation of the FLCN-AMPK complex. These results suggest that function(s) of FLCN-AMPK-FNIP complex is regulated by Ser62 phosphorylation.
引用
收藏
页码:39 / 43
页数:5
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