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Protein transamidation by transglutaminase 2 in cells: a disputed Ca 2+ ‐dependent action of a multifunctional protein
Author(s) -
Király Róbert,
Demény MátéÁ.,
Fésüs László
Publication year - 2011
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2011.08345.x
Subject(s) - tissue transglutaminase , enzyme , gtp' , biochemistry , chemistry , intracellular , protein disulfide isomerase , protein kinase a , microbiology and biotechnology , biophysics , biology
Transglutaminase 2 (TG2) is the first described cellular member of an enzyme family catalyzing Ca 2+ ‐dependent transamidation of proteins. During the last two decades its additional enzymatic (GTP binding and hydrolysis, protein disulfide isomerase, protein kinase) and non‐enzymatic (multiple interactions in protein scaffolds) activities, which do not require Ca 2+ , have been recognized. It became a prevailing view that TG2 is silent as a transamidase, except in extreme stress conditions, in the intracellular environment characterized by low Ca 2+ and high GTP concentrations. To counter this presumption a critical review of the experimental evidence supporting the role of this enzymatic activity in cellular processes is provided. It includes the structural basis of TG2 regulation through non‐canonical Ca 2+ binding sites, mechanisms making it sensitive to low Ca 2+ concentrations, techniques developed for the detection of protein transamidation in cells and examples of basic cellular phenomena as well as pathological conditions influenced by this irreversible post‐translational protein modification.