Protein transamidation by transglutaminase 2 in cells: a disputed Ca2+-dependent action of a multifunctional protein |
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Authors: | Király Róbert Demény Mátéá Fésüs László |
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Institution: | Department of Biochemistry and Molecular Biology, Apoptosis and Genomics Group of the Hungarian Academy of Sciences, University of Debrecen, Debrecen, Hungary. |
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Abstract: | 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. |
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