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

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. MINT- 7298145, MINT- 7298166: Flcn (uniprotkb: Q76JQ2) physically interacts (MI: 0915) with AMPK alpha 1 (uniprotkb: P54645) by anti tag coimmunoprecipitation (MI: 0007) MINT- 7298267: AMPK alpha 1 (uniprotkb: Q13131) phosphorylates (MI: 0217) tsc2 (uniprotkb: P49816) by protein kinase assay (MI: 0424) MINT- 7298182: FNIP1 (uniprotkb: Q8TF40) physically interacts (MI: 0915) with Flcn (uniprotkb: Q76JQ2) by anti tag coimmunoprecipitation (MI: 0007) MINT- 7298132: AMPK alpha 1 (uniprotkb: Q13131) phosphorylates (MI: 0217) Flcn (uniprotkb: Q76JQ2) by protein kinase assay (MI: 0424) MINT- 7298229: FNIPL (uniprotkb: Q9P278) physically interacts (MI: 0915) with Flcn (uniprotkb: Q76JQ2) by anti tag coimmunoprecipitation (MI: 0007)