期刊
JOURNAL OF CELL SCIENCE
卷 123, 期 5, 页码 671-681出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.058198
关键词
Axon branching; Glycoprotein; Heparan sulphate; L1-ezrin-moesin-radixin-actin; Lectin; Plasma membrane
类别
资金
- EC Marie Curie Research Training Network [2005019561]
- Carlos III Health Institute
- Castilla-La-Mancha Health Service (SESCAM)
- Spanish National Health System [EMER07/026]
Serine phosphorylation of the beta-galactoside-binding protein galectin-3 (Gal-3) impacts nuclear localization but has unknown consequences for extracellular activities. Herein, we reveal that the phosphorylated form of galectin-3 (pGal-3), adsorbed to substratum surfaces or to heparan sulphate proteoglycans, is instrumental in promoting axon branching in cultured hippocampal neurons by local actin destabilization. pGal-3 interacts with neural cell adhesion molecule L1, and enhances L1 association with Thy-1-rich membrane microdomains. Concomitantly, membrane-actin linker proteins ezrin-radixin-moesin (ERM) are recruited to the same membrane site via interaction with the intracellular domain of L1. We propose that the local regulation of the L1-ERM-actin pathway, at the level of the plasma membrane, underlies pGal-3-induced axon branching, and that galectin phosphorylation in situ could act as a molecular switch for the axon response to Gal-3.
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