The BHD Literature Database has been updated with 6 articles.
Dephoure et al. used stable isotope labelling and mass spectrometry to find proteins whose phosphorylation is cell cycle dependent. They found that FLCN is phosphorylated at S62 and S73 during mitosis, and phosphorylated at S302 (mislabelled as S304 in the paper) during G1. This finding is discussed in a previous blog post.
Yu et al. used large-scale quantitative phospho-proteomics to define signalling networks downstream of mTORC1 and mTORC2. They found that mTORC1 phosphorylates FLCN at S62 and S302.
Peña-Llopis et al. used a gene expression microarray to screen for targets of mTORC1 and saw that it activates FLCN expression.
Wagner et al. used mass spectrometry to investigate endogenous ubiquitylation sites. They found that FLCN is ubiquitylated at K206 and K559 and that FNIP1 was ubiquitylated at K161. This paper is discussed in a previous blog post.
Danielsen et al. used higher-energy collisional dissociation to find ubiquitylated lysines and found that FLCN is ubiquitylated.
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All of these papers are freely available to download in the BHD Article Library: Basic section.