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| Content Provider | Springer Nature Link |
|---|---|
| Author | Kanchan, Kajal Fuxreiter, Mónika Fésüs, László |
| Copyright Year | 2015 |
| Abstract | Transglutaminase 2 (TG2) is a ubiquitously expressed member of an enzyme family catalyzing Ca2+-dependent transamidation of proteins. It is a multifunctional protein having several well-defined enzymatic (GTP binding and hydrolysis, protein disulfide isomerase, and protein kinase activities) and non-enzymatic (multiple interactions in protein scaffolds) functions. Unlike its enzymatic interactions, the significance of TG2’s non-enzymatic regulation of its activities has recently gained importance. In this review, we summarize all the partners that directly interact with TG2 in a non-enzymatic manner and analyze how these interactions could modulate the crosslinking activity and cellular functions of TG2 in different cell compartments. We have found that TG2 mostly acts as a scaffold to bridge various proteins, leading to different functional outcomes. We have also studied how specific structural features, such as intrinsically disordered regions and embedded short linear motifs contribute to multifunctionality of TG2. Conformational diversity of intrinsically disordered regions enables them to interact with multiple partners, which can result in different biological outcomes. Indeed, ID regions in TG2 were identified in functionally relevant locations, indicating that they could facilitate conformational transitions towards the catalytically competent form. We reason that these structural features contribute to modulating the physiological and pathological functions of TG2 and could provide a new direction for detecting unique regulatory partners. Additionally, we have assembled all known anti-TG2 antibodies and have discussed their significance as a toolbox for identifying and confirming novel TG2 regulatory functions. |
| Starting Page | 3009 |
| Ending Page | 3035 |
| Page Count | 27 |
| File Format | |
| ISSN | 1420682X |
| Journal | Cellular and Molecular Life Sciences |
| Volume Number | 72 |
| Issue Number | 16 |
| e-ISSN | 14209071 |
| Language | English |
| Publisher | Springer Basel |
| Publisher Date | 2015-05-06 |
| Publisher Place | Basel |
| Access Restriction | Subscribed |
| Subject Keyword | Transglutaminase 2 Non-enzymatic interactions Intrinsically disordered regions TRANSDAB database Scaffolding Anti-TG2 antibodies Cell Biology Biomedicine general Life Sciences Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience |
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