Serine 62 is a phosphorylation site in folliculin, the Birt-Hogg-Dube gene product.
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.
Mesh Terms:
Animals, Antibodies, Phospho-Specific, COS Cells, Carrier Proteins, Cercopithecus aethiops, Phosphorylation, Protein Kinases, Proteins, Rats, Serine
Animals, Antibodies, Phospho-Specific, COS Cells, Carrier Proteins, Cercopithecus aethiops, Phosphorylation, Protein Kinases, Proteins, Rats, Serine
FEBS Lett.
Date: Jan. 04, 2010
PubMed ID: 19914239
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