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During the last two decades its additional enzymatic (GTP binding and hydrolysis, protein disulfide isomerase, protein kinase) and non\u2010enzymatic (multiple interactions in protein scaffolds) activities, which do not require Ca\n                    <jats:sup>2+<\/jats:sup>\n                    , 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\n                    <jats:sup>2+<\/jats:sup>\n                    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\u2010canonical Ca\n                    <jats:sup>2+<\/jats:sup>\n                    binding sites, mechanisms making it sensitive to low Ca\n                    <jats:sup>2+<\/jats:sup>\n                    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\u2010translational protein modification.\n                  <\/jats:p>","DOI":"10.1111\/j.1742-4658.2011.08345.x","type":"journal-article","created":{"date-parts":[[2011,9,8]],"date-time":"2011-09-08T17:40:09Z","timestamp":1315503609000},"page":"4717-4739","source":"Crossref","is-referenced-by-count":93,"title":["Protein transamidation by transglutaminase 2 in cells: a disputed Ca\n                    <sup>2+<\/sup>\n                    \u2010dependent action of a multifunctional 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