TGM2/Transglutaminase 2 Protein, Mouse (His)

TGM2/Transglutaminase 2 protein, a calcium-dependent acyltransferase, catalyzes the formation of covalent bonds between peptide-bound glutamine and various primary amines, leading to the cross-linking or amination of proteins. Involved in diverse biological processes such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification, and apoptosis, TGM2 acts as a protein-glutamine gamma-glutamyltransferase. It mediates the cross-linking of proteins, including ACO2, HSPB6, FN1, HMGB1, RAP1GDS1, SLC25A4/ANT1, SPP1, and WDR54. The protein cross-linking activity is inhibited under physiological conditions by GTP, and this inhibition is relieved by Ca(2+) in response to various stresses. In addition to its role in apoptosis by promoting cytoskeletal protein cross-linking and mediating the formation of extracellular matrix scaffolds, TGM2 can use monoamine substrates to catalyze diverse protein post-translational modifications. It plays a crucial role in chromatin organization by mediating serotonylation and dopaminylation of histone H3, contributing to neurotransmission-independent functions in ventral tegmental area (VTA) neurons. Furthermore, TGM2 acts as a signal transducer in alpha-1 adrenergic receptor-mediated stimulation of phospholipase C-delta (PLCD) activity, highlighting its involvement in signaling pathways beyond its acyltransferase activity.