Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2023.01.26.525744v1?rss=1

Authors: Baade, T., Michaelis, M., Prestel, A., Paone, C., Klishin, N., Scheinost, L., Nedielkov, R., Hauck, C. R., Moller, H. M.

Abstract:
Integrins are fundamental for cell adhesion and the formation of focal adhesions (FA). Accordingly, these receptors guide embryonic development, tissue maintenance and haemostasis, but are also involved in cancer invasion and metastasis. A detailed understanding of the molecular interactions that drive integrin activation, focal adhesion assembly, and downstream signalling cascades is critical. Here, we reveal a direct association of paxillin, a marker protein of focal adhesion sites, with the cytoplasmic tails of the integrin {beta}1 and {beta}3 subunits. The binding interface resides in paxillin's LIM3 domain, where based on the NMR structure and functional analyses a flexible, seven amino acid loop engages the unstructured part of the integrin cytoplasmic tail. Genetic manipulation of the involved residues in either paxillin or integrin {beta}3 compromises cell adhesion and motility. This direct interaction between paxillin and the integrin cytoplasmic domain identifies an alternative, kindlin-independent mode of integrin outside-in signalling particularly important for integrin {beta}3 function.

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