A recent paper published by Wang et al (2009) has shown that serine 62 (Ser62) is the major phosphorylation site in FLCN. Their analysis suggests that Ser62 phosphorylation is indirectly up-regulated by AMPK and that another residue is directly phosphorylated by AMPK. Also, by binding with FLCN-interacting proteins (FNIP1 and FNIP2/FNIPL), Ser62 phosphorylation was increased.
Importantly the authors generated a rabbit polyclonal antibody able to detect phosphorylation at this specific residue. More details regarding the anti-phospho-Ser62-FLCN antibody is available in our ‘Laboratory Essentials‘ section.