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    FEBS Lett. 2010 Jan 4;584(1):39-43. doi: 10.1016/j.febslet.2009.11.033.

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

    Wang L, Kobayashi T, Piao X, Shiono M, Takagi Y, Mineki R, Taka H, Zhang D, Abe M, Sun G, Hagiwara Y, Okimoto K, Matsumoto I, Kouchi M, Hino O.

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    Department of Pathology and Oncology, Juntendo University School of Medicine, Tokyo, Japan.

    Abstract

    Recently, it was reported that the product of Birt-Hogg-Dubé 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.

    PMID:
    19914239
    [PubMed - indexed for MEDLINE]

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