Serine 62 is a phosphorylation site in folliculin, the Birt-Hogg-Dube gene product
Serine 62 is a phosphorylation site in folliculin, the Birt-Hogg-Dube gene product
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DOI：
10.1016/j.febslet.2009.11.033
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发表时间：
2010-01-04
期刊：
影响因子：
3.5
通讯作者：
Hino, Okio
中科院分区：
文献类型：
--
作者：
Wang, Lu;Kobayashi, Toshiyuki;Hino, Okio
最近有报道称，Birt-Hogg-Dube综合征基因的产物（folliculin，FLCN）被5 ′-AMP-活化蛋白激酶（AMPK）直接磷酸化。在这项研究中，我们确定了丝氨酸62（Ser 62）作为FLCN的磷酸化位点，并产生了抗磷酸化Ser 62-FLCN抗体。我们的分析表明，Ser 62磷酸化是间接上调AMPK和另一个残基直接磷酸化AMPK。通过与FLCN相互作用蛋白（FNIP 1和FNIP 2/FNIPL）结合，Ser 62磷酸化增加。丝氨酸62位的磷酸化模拟突变增强了FLCN-AMPK复合物的形成。这些结果表明FLCN-AMPK-FNIP复合物的功能受Ser 62磷酸化的调节。
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.