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.