Please use this identifier to cite or link to this item: https://doi.org/10.4161/cam.26344
Title: Transglutaminase-2 in cell adhesion: All roads lead to paxillin?
Authors: Png, E.
Tong, L. 
Keywords: Adhesion
Adhesome
Cell culture
Migration
Paxillin
Review
Signaling
Transglutaminase
Issue Date: Sep-2013
Citation: Png, E., Tong, L. (2013-09). Transglutaminase-2 in cell adhesion: All roads lead to paxillin?. Cell Adhesion and Migration 7 (5) : 412-417. ScholarBank@NUS Repository. https://doi.org/10.4161/cam.26344
Abstract: Cell-matrix adhesion is a fundamental biological process that governs survival, migration, and proliferation of living eukaryotic cells. Paxillin is an important central player in a network of adhesome proteins that form focal adhesion complexes. Phosphorylation of tyrosine and serine residues in paxillin is critical for the coordinated sequential recruitment of other adaptor and kinase proteins to adhesion complexes. Recently, the phosphorylation of serine178 in paxillin has been shown to be vital for epithelial cell adhesion and migration. In vivo and in vitro evidence have shown that transglutaminase (TG)-2 positively regulates this phosphorylation. Here, we propose three possible mechanisms that may explain these observations. First, TG-2 itself may be an adhesome member directly interacting with paxillin in a non-covalent way. Second, TG-2 may cross link a mitogen-activated protein kinase kinase kinase (MAP3K), which eventually activates c-Jun N-terminal kinase (JNK), and the latter phosphorylates paxillin. Lastly, TG-2 may have intrinsic kinase activity that phosphorylates paxillin. Future studies investigating these hypotheses on TG-2-paxillin relationships are necessary in order to address this fundamental process in cell matrix adhesion signaling. © 2013 Landes Bioscience.
Source Title: Cell Adhesion and Migration
URI: http://scholarbank.nus.edu.sg/handle/10635/110688
ISSN: 19336918
DOI: 10.4161/cam.26344
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