ArticleBiochemistry2007
GTP-binding-defective forms of tissue transglutaminase trigger cell death.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 39 citations in OpenAlex.
- Beyond neurotransmission: the roles of serotonylation in physiological and pathological processes.Cellular & molecular biology letters · 2026Review
- Distinct conformational states enable transglutaminase 2 to promote cancer cell survival versus cell death.Communications biology · 2024Article
- Pathogenetic Contributions and Therapeutic Implications of Transglutaminase 2 in Neurodegenerative Diseases.International journal of molecular sciences · 2024Review
- Article
- Evolving Experimental Techniques for Structure-Based Drug Design.The journal of physical chemistry. B · 2022Review
- Sulfated glycosaminoglycans inhibit transglutaminase 2 by stabilizing its closed conformation.Scientific reports · 2022Article
- Exploring the Role of Transglutaminase in Patients with Glioblastoma: Current Perspectives.OncoTargets and therapy · 2022Review
- Transglutaminase 2 Has Metabolic and Vascular Regulatory Functions Revealed by In Vivo Activation of Alpha1-Adrenergic Receptor.International journal of molecular sciences · 2020Article
- A small molecule regulator of tissue transglutaminase conformation inhibits the malignant phenotype of cancer cells.Oncotarget · 2018Article
- The diamond anniversary of tissue transglutaminase: a protein of many talents.Drug discovery today · 2018Review
- Opening up about Tissue Transglutaminase: When Conformation Matters More than Enzymatic Activity.Med one · 2018Article
- The Different Conformational States of Tissue Transglutaminase Have Opposing Affects on Cell Viability.The Journal of biological chemistry · 2016Article
- Role of hypoxia-induced transglutaminase 2 in pulmonary artery smooth muscle cell proliferation.American journal of physiology. Lung cellular and molecular physiology · 2014Article
- Aberrant calcium signaling by transglutaminase-mediated posttranslational modification of inositol 1,4,5-trisphosphate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Transglutaminase regulation of cell function.Physiological reviews · 2014Review
- Transglutaminse 2 and EGGL, the protein cross-link formed by transglutaminse 2, as therapeutic targets for disabilities of old age.Rejuvenation research · 2013Review
- A mechanism for the upregulation of EGF receptor levels in glioblastomas.Cell reports · 2013Article
- Transglutaminase 2 facilitates or ameliorates HIF signaling and ischemic cell death depending on its conformation and localization.Biochimica et biophysica acta · 2013Article
- Regulation of the activities of the mammalian transglutaminase family of enzymes.Protein science : a publication of the Protein Society · 2012Review
- Transglutaminase 2: a molecular Swiss army knife.Biochimica et biophysica acta · 2012Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Tissue transglutaminase (TGase-2), which binds GTP and catalyzes the cross-linking of proteins (transamidation), has been implicated both in the promotion of cell death and in the protection of cells against apoptotic insults. However, a novel transcript originally identified from the brains of Alzheimer's patients, encoding a truncated form of TGase-2 (called TGase-S), shows strong apoptotic activity. TGase-S exhibits no detectable GTP-binding capability, suggesting that its ability to induce cell death might be due to its inability to bind GTP. Thus, we have examined whether eliminating the GTP-binding capability of full-length human TGase-2 would prevent it from conferring protection against apoptotic challenges and instead convert it into a protein that causes cell death. A number of point mutants of human TGase-2 defective for binding GTP, as well as a mutant that shows impaired GTP-hydrolytic activity, were generated. Similar to what we had found for TGase-S, there was a time-dependent decrease in the expression of the GTP-binding-defective TGase-2 mutants in different cell lines, whereas the expression of wild-type TGase-2 and the GTP hydrolysis-defective mutant was sustained. Moreover, the GTP-binding-defective TGase-2 mutants induced cell death. The cell death responses triggered by these mutants were not due to their transdamidation activity, because double-mutants that were both GTP-binding- and transamidation-defective also stimulated cell death. Therefore, these results point to the inability to bind GTP as being sufficient for the apoptotic activity exhibited by the TGase-S protein. They also highlight a novel example of how the loss of GTP-binding activity can convert a protein that provides protection against apoptotic stimuli into a cell death-promoting factor.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.