Role of tissue transglutaminase-2 (TG2)-mediated aminylation in biological processes.
Post-translational modification (PTM) is an important mechanism in modulating a protein's structure and can lead to substantial diversity in biological function. Compared to other forms of PTMs such as phosphorylation, acetylation and glycosylation, the physiological significance of aminylation is limited. Aminylation refers to the covalent incorporation of biogenic/polyamines into target protein by calcium-dependent transglutaminases (TGs). The development of novel and more sensitive techniques has led to more proteins identified as tissue transglutaminase (TG2) substrates and potential targets for aminylation. Many of these substrate proteins play a role in cell signaling, cytoskeleton organization, muscle contraction, and inflammation. TG2 is well studied and widely expressed in a variety of tissues and will be the primary focus of this review on recent advance in transglutaminase-mediated aminylation.
Graduate Institute of Biomedical Science, Mackay Medical College, No. 46, Sec. 3, Jhong-Jheng Rd., Sanzhi Dist, New Taipei City, 25200, Taiwan, ROC. lai00002@mmc.edu.tw.
Thung-S
0000-0002-8791-9698
TS
Lai
Nephrology/Department of Internal Medicine, Mackay Memorial Hospital, Taipei, Taiwan, ROC.|Nursing and Management, Mackay Junior College of Medicine, Taipei, Taiwan, ROC.
Cheng-Jui
CJ
Lin
Department of Medicine, Medical University of South Carolina, Charleston, SC, 29425, USA.
Charles S
CS
Greenberg
D000586:Amination; D000818:Animals; D001679:Biogenic Amines / Q000737:chemistry / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000235:genetics / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) / Q000235:genetics / Q000378:metabolism; D006657:Histones / Q000235:genetics / Q000378:metabolism; D006801:Humans; D000071058:Huntingtin Protein / Q000235:genetics / Q000378:metabolism; D000072000:NF-KappaB Inhibitor alpha / Q000235:genetics / Q000378:metabolism; D066263:Protein Aggregation, Pathological / Q000235:genetics / Q000378:metabolism*; D000072417:Protein Domains; D000091345:Protein Glutamine gamma Glutamyltransferase 2; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction; D013379:Substrate Specificity; D011503:Transglutaminases / Q000235:genetics / Q000378:metabolism*
D001679:Biogenic Amines; D003598:Cytoskeletal Proteins; D016326:Extracellular Matrix Proteins; C086055:HTT protein, human; D006657:Histones; D000071058:Huntingtin Protein; C000717608:TGM2 protein, human; D000072000:NF-KappaB Inhibitor alpha; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); D000091345:Protein Glutamine gamma Glutamyltransferase 2; D011503:Transglutaminases; D019204:GTP-Binding Proteins
Aminylation; Histaminylation; Polyaminylation; Post-translational modification; Serotonylation; TG2; Tissue transglutaminase