Abstract
Transglutaminase 2 (TG2) is an inducible transamidating acyltransferase that catalyzes Ca2+-dependent protein modifications. It acts as a G protein in transmembrane signaling and as a cell surface adhesion mediator, this distinguishes it from other members of the transglutaminase family. The sequence motifs and domains revealed in the TG2 structure, can each be assigned distinct cellular functions, including the regulation of cytoskeleton, cell adhesion, and cell death. Though many biological functions of the enzyme have already been described or proposed previously, studies of TG2 null mice by our laboratory during the past years revealed several novel in vivo roles of the protein. In this review we will discuss these novel roles in their biological context.
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Acknowledgments
These studies were supported by Hungarian grants from the National Research Fund (OTKA T049445 and NI67877), Ministry of Welfare T (115/2006) and the EU HRTN-CT-2006-036032.
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Sarang, Z., Tóth, B., Balajthy, Z. et al. Some lessons from the tissue transglutaminase knockout mouse. Amino Acids 36, 625–631 (2009). https://doi.org/10.1007/s00726-008-0130-x
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DOI: https://doi.org/10.1007/s00726-008-0130-x