💡 Online now - the Spotlight "Cryptic phosphorylation sites provide new structural and functional insights into the human phosphoproteome" from Jesse Rinehart.

#ProteinPhosphorylation #Phosphoproteome #CrypticPhosphorylation

Read it here 👉 authors.elsevier.com/a/1mTsH3S6Gf...

Florigen activation complex forms via multifaceted assembly in Arabidopsis Nature - In flowering plants, DNA–FD–14-3-3 recruits FT to the florigen activation complex both through DNA–FT interactions and by reducing liquid phase condensation of FD...

Honoured to have participated in this amazing story uncovering novel #florigen roles in #Arabidopsis Congrats to @HeGao @NaDing and collaborators!!
Check it out @nature.com
🌱 🌸 🧬 🔬

#bZIP #proteinphosphorylation @mpipz.bsky.social
rdcu.be/ePPjS

Available online - the Spotlight "FN3K: the (un)sweetest kinase" from Viraj Sanghvi @oncolab.bsky.social and colleagues.

#ProteinPhosphorylation #ProteinGlycation #AdvancedGlycationEndProducts #AGE #SBDD

Read it here: authors.elsevier.com/a/1ktQO3S6Gf...

Complex structure and activation mechanism of arginine kinase McsB by McsA | Nature Chemical Biology Protein phosphorylation is a pivotal post-translational modification modulating various cellular processes. In Gram-positive bacteria, the protein arginine kinase McsB, along with its activator McsA, has a key role in labeling misfolded and damaged proteins during stress. However, the activation mechanism of McsB by McsA remains elusive. Here we report the cryo-electron microscopy structure of a tetrameric McsA–McsB complex at 3.41 Å resolution. Biochemical analysis indicates that the homotetrameric assembly is essential for McsB’s kinase activity. The conserved C-terminal zinc finger of McsA interacts with an extended loop in McsB, optimally orienting a critical catalytic cysteine residue. In addition, McsA binding decreases the CtsR’s affinity for McsB, enhancing McsB’s kinase activity and accelerating the turnover rate of CtsR phosphorylation. Furthermore, McsA binding also increases McsB’s thermostability, ensuring its activity under heat stress. These findings elucidate the struct

Unlocking the mystery: Cryo-EM structure of tetrameric McsA-McsB reveals activation at 3.41 Å, crucial for stress response. #ProteinPhosphorylation PMID:39232187, Nat Chem Biol 2025, @nchembio https://doi.org/10.1038/s41589-024-01720-3 #Medsky 🧪