Beta-Actin is a Target for Transglutaminase Activity at Synaptic Endings in Chicken Telencephalic Cell Cultures

作     者：Dolge, Lars Aufenvenne, Karin Traupe, Heiko Baumgartner, Werner 

作者机构：Rhein Westfal TH Aachen Dept Cellular Neurobion Inst Biol 2 D-52070 Aachen Germany Univ Hosp Munster Dept Dermatol D-48149 Munster Germany 

出 版 物：《JOURNAL OF MOLECULAR NEUROSCIENCE》 (分子神经科学杂志)

年 卷 期：2012年第46卷第2期

页      面：410-419页

核心收录：

学科分类：0710[理学-生物学] 1001[医学-基础医学(可授医学、理学学位)] 07[理学] 071003[理学-生理学] 

基　　金：Deutsche Forschungsgemeinschaft [Ba2272/6-1] 

主　　题：Transglutaminase Actin Synapse Telencephalon Cadherin 

摘      要：Transglutaminases are Ca2+-dependent enzymes that catalyse the covalent cross-linking of protein-bound glutamine and lysine residues, which can stabilise proteins or protein aggregates. In the brain, elevated expression levels and activity of transglutaminases are known to be linked with several neurodegenerative diseases. However, little is known about the physiological functions of transglutaminases in the central nervous system. In this study, we examined the expression and activity of transglutaminase 1 in chicken telencephalic cell cultures. We observed a cytosolic expression of transglutaminase 1 in telencephalic neurons. However, transglutaminase 1 activity was restricted to synaptic endings. Transglutaminase targets in the cultured cells were characterised via a biotinylation assay and beta-actin was identified as a substrate. Furthermore, we were able to show that beta-actin is a target for the activity of recombinant human transglutaminase 1 in vitro. We propose a mechanism where neuronal transglutaminase 1 is activated by synaptic activity-dependent influx of calcium ions and thereupon catalyse the formation of an intramolecular cross-link in beta-actin, thereby stabilising the actin cytoskeleton against depolymerising effects. In this way, transglutaminase 1 could modulate actin-dependent plasticity events at synaptic endings.