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. 2019 Dec 6;9:1376. doi: 10.3389/fonc.2019.01376

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Copyright © 2019 Deville and Cordes.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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(A) The extracellular matrix (ECM) secretion depends mainly on cancer associated fibroblasts (CAFs). The dynamic reorganization of ECM is regulated by matrix metalloproteinase (MMP)-dependent matrix degradation and lysyl oxidase (LOX)-dependent ECM crosslinking. Changes in ECM and stiffening leads to: (a) epithelial-to-mesenchymal transition (EMT) enhancing cell migration and invasion, (b) limited drugs distribution, (c) genomic alterations resulting in clonogenicity and heterogeneity, and (d) the activation of key adhesion proteins, such as integrin. (B) Integrin-dependent outside-in signaling mechanisms regulated cell adhesion to ECM as part of their role in cancer radio- and drug-resistance. Many of these mechanisms involve the focal adhesion kinase (FAK). (C) The Linker of Nucleoskeleton and Cytoskeleton (LINC) complex is composed of two families: KASH located at the nuclear membrane exterior (NME) and SUN situated in the nuclear membrane interior (NMI). LINC regulates the physical transmission of forces generated by the ECM and cytoskeleton. Moreover, a low expression levels of lamin-A/C is correlated with a high cell migration and an increase of therapy resistance. Cells adjust to mechanical tensions by enhancing the expression level of lamin-A and phosphorylated emerin. LINC complex detaches from the nucleus and cytoskeleton to maintain DNA integrity when cells fail to manage the tension. Created with BioRender.