[HTML][HTML] Serine 62 is a phosphorylation site in folliculin, the Birt–Hogg–Dubé gene product
L Wang, T Kobayashi, X Piao, M Shiono, Y Takagi… - FEBS letters, 2010 - Elsevier
L Wang, T Kobayashi, X Piao, M Shiono, Y Takagi, R Mineki, H Taka, D Zhang, M Abe…
FEBS letters, 2010•ElsevierRecently, 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 the major 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 …
FLCN) is directly phosphorylated by 5′-AMP-activated protein kinase (AMPK). In this study,
we identified serine 62 (Ser62) as the major 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 …
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 the major 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. STRUCTURED SUMMARY: 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)
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