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

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


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinase Kinases
  • Animals
  • Antibodies, Phospho-Specific / biosynthesis
  • COS Cells
  • Carrier Proteins / metabolism
  • Chlorocebus aethiops
  • Phosphorylation
  • Protein Kinases / metabolism
  • Proteins / genetics
  • Proteins / immunology
  • Proteins / metabolism*
  • Rats
  • Serine / genetics
  • Serine / immunology
  • Serine / metabolism*


  • Antibodies, Phospho-Specific
  • Carrier Proteins
  • FNIP1 protein, human
  • Flcn protein, rat
  • Proteins
  • Serine
  • Protein Kinases
  • AMP-Activated Protein Kinase Kinases