Category: Blog

Quick Read. SUMOylation is a reversible post-translational modification in which Small Ubiquitin-like Modifier proteins are covalently attached to lysines on target proteins. The core human pathway uses the SAE1–UBA2 E1 activating enzyme, the UBC9/UBE2I E2 conjugating enzyme, E3 ligases that sharpen substrate selection, and SENP proteases that mature SUMO precursors and remove SUMO from substrates.…

Quick Read. ER-phagy is selective autophagic turnover of the endoplasmic reticulum. Cells use receptor proteins such as FAM134B, RTN3L, CCPG1, SEC62, ATL3 and TEX264 to identify ER regions for capture by autophagic membranes and delivery to lysosomes. The process helps control ER size, remove damaged or protein-loaded ER subdomains, and restore proteostasis after stress. One-sentence…

Quick Read. Protein tyrosine sulfation is a post-translational modification that adds sulfate to selected tyrosine residues of secreted and membrane proteins as they pass through the trans-Golgi network. The sulfate donor is PAPS, the Golgi transporter SLC35B2 supplies luminal PAPS, and the enzymes TPST1 and TPST2 install the modification. Sulfotyrosine can strengthen extracellular protein–protein recognition…

Quick Read. N-myristoylation is a lipid modification that attaches a 14-carbon myristoyl group to selected proteins, usually at an exposed N-terminal glycine. The modification is installed by N-myristoyltransferases NMT1 and NMT2 using myristoyl-CoA. It often helps proteins associate with membranes, but the important idea is not “fat makes proteins sticky.” Myristate is one part of…

Learn protein prenylation from FPP/GGPP and CaaX recognition through FTase/GGTase, RCE1–ICMT processing, Rab escort, dynamic membrane targeting, evidence, misconceptions and model limits.

Learn O-GlcNAc cycling from hexosamine-pathway flux and UDP-GlcNAc to OGT/OGA substrate selection, signalling, stress adaptation, proteomic measurement, misconceptions and model limits.