alexa Localized LoxL3-dependent Fibronectin Oxidation Regulates Myofiber Stretch And Integrin-mediated Adhesion
ISSN: 2329-6577

Biological Systems: Open Access
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JOINT EVENT on 2nd International Conference on Bioscience and 5th International Conference on Integrative Biology
June 19-21, 2017 London, UK

Peleg Hasson
Technion - Israel Institute of Technology, Israel
ScientificTracks Abstracts: Biol Syst Open Access
DOI: 10.4172/2329-6577-C1-008
Abstract
For muscles to function, myofibers have to stretch and anchor at the myotendinous junction (MTJ), a region rich in extracellular matrix (ECM). Integrin signaling is required for MTJ formation, and mutations affecting the cascade lead to muscular dystrophies in mice and humans. Underlying mechanisms for integrin activation at the MTJ and ECM modifications regulating its signaling are unclear. We show that lysyl oxidase-like 3 (LoxL3) is a key regulator of integrin signaling that ensures localized control of the cascade. In LoxL3 mutants, myofibers anchor prematurely or overshoot to adjacent somites, and are loose and lack tension. We find that LoxL3 complexes with and directly oxidizes Fibronectin (FN), an ECM scaffold protein and integrin ligand enriched at the MTJ. We identify a mechanism whereby localized LoxL3 secretion from myofiber termini oxidizes FN, promoting FN polymerization thus priming it for integrin activation at the tips of myofibers and ensuring correct positioning and anchoring of myofibers along the MTJ.
Biography

Peleg Hasson has completed his PhD from the Hebrew University, Jerusalem and continued his Post-doctoral studies at the MRC-National Institute of Medical Research, London. Currently, he is working in his own lab at Technion - Israel Institute of Technology, Israel in 2010.

Email: [email protected]

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