2. Academic Validation
  3. Role of tissue transglutaminase-2 (TG2)-mediated aminylation in biological processes

Role of tissue transglutaminase-2 (TG2)-mediated aminylation in biological processes

  • Amino Acids. 2017 Mar;49(3):501-515. doi: 10.1007/s00726-016-2270-8.
Thung-S Lai 1,  Cheng-Jui Lin 2 3,  Charles S Greenberg 4
Affiliations

Affiliations

  • 1 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.
  • 2 Nephrology/Department of Internal Medicine, Mackay Memorial Hospital, Taipei, Taiwan, ROC.
  • 3 Nursing and Management, Mackay Junior College of Medicine, Taipei, Taiwan, ROC.
  • 4 Department of Medicine, Medical University of South Carolina, Charleston, SC, 29425, USA.
PMID: 27270573 DOI: 10.1007/s00726-016-2270-8
Abstract

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.

Keywords

Aminylation; Histaminylation; Polyaminylation; Post-translational modification; Serotonylation; TG2; Tissue transglutaminase.

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