RT Journal Article SR Electronic T1 N-cadherin engagement limits the recruitment of microtubules at cell-cell contacts through organization of acto-myosin JF Journal of Cell Science JO J. Cell Sci. FD The Company of Biologists Ltd DO 10.1242/jcs.131284 A1 Plestant, Charlotte A1 Strale, Pierre-Olivier A1 Seddiki, Rima A1 Nguyen, Emmanuelle A1 Ladoux, Benoit A1 Mège, René-Marc YR 2014 UL http://jcs.biologists.org/content/early/2014/02/12/jcs.131284.abstract AB Engagement of cadherins induces a cross-talk between adhesion complexes and the actin cytoskeleton allowing cadherin adhesion strengthening and cell's cytoskeleton organization. The underlying mechanisms are not fully understood and microtubules (MTs) may be involved as it is the case for integrin-mediated cell-extracellular matrix adhesions. Therefore, we investigated the relationship between N-cadherin and MTs by analyzing the influence of N-cadherin engagement on MT distribution and dynamics using substrates mimicking the formation of cadherin adhesions. MTs progressed significantly less towards cadherin adhesions than towards focal adhesions and presented a significantly lower mean elongation rate. The increased actin treadmilling and the presence of an acto-myosin contractile belt at the rear of the cadherin adhesion zone that MTs did not pass through suggested that actin might relay the inhibitory actions on MTs. The reduction of MT elongation rate, associated with destabilization in EB protein recruitment at plus ends, was alleviated by the expression of a truncated N-cadherin, but only moderately affected by acto-myosin perturbations. In contrast, the destabilization of acto-myosin fibers allowed the penetration of MTs in the adhesion area, suggesting an obstructive effect of tangential actin bundles on MT penetration independently of MT dynamics. In turn, blockade of MT penetration induced a strengthening of cadherin adhesions. Altogether, these results establish a functional cross-talk between N-cadherin, F-actin and MTs. The opposite effect of cadherin and integrin engagement on actin organization and MT distribution may be of primary importance to bias MT network during cell polarization.