TY - JOUR
T1 - α-Catenin-mediated cadherin clustering couples cadherin and actin dynamics
AU - Chen, Chi Shuo
AU - Hong, Soonjin
AU - Indra, Indrajyoti
AU - Sergeeva, Alina P.
AU - Troyanovsky, Regina B.
AU - Shapiro, Lawrence
AU - Honig, Barry
AU - Troyanovsky, Sergey M.
N1 - Publisher Copyright:
© 2015 Chen et al.
PY - 2015
Y1 - 2015
N2 - The function of the actin-binding domain of α-catenin, αABD, including its possible role in the direct anchorage of the cadherin-catenin complex to the actin cytoskeleton, has remained uncertain. We identified two point mutations on the αABD surface that interfere with αABD binding to actin and used them to probe the role of α-catenin-actin interactions in adherens junctions. We found that the junctions directly bound to actin via αABD were more dynamic than the junctions bound to actin indirectly through vinculin and that recombinant αABD interacted with cortical actin but not with actin bundles. This interaction resulted in the formation of numerous short-lived cortex-bound αABD clusters. Our data suggest that αABD clustering drives the continuous assembly of transient, actin-associated cadherin-catenin clusters whose disassembly is maintained by actin depolymerization. It appears then that such actin-dependent αABD clustering is a unique molecular mechanism mediating both integrity and reassembly of the cell-cell adhesive interface formed through weak cis- and trans-intercadherin interactions.
AB - The function of the actin-binding domain of α-catenin, αABD, including its possible role in the direct anchorage of the cadherin-catenin complex to the actin cytoskeleton, has remained uncertain. We identified two point mutations on the αABD surface that interfere with αABD binding to actin and used them to probe the role of α-catenin-actin interactions in adherens junctions. We found that the junctions directly bound to actin via αABD were more dynamic than the junctions bound to actin indirectly through vinculin and that recombinant αABD interacted with cortical actin but not with actin bundles. This interaction resulted in the formation of numerous short-lived cortex-bound αABD clusters. Our data suggest that αABD clustering drives the continuous assembly of transient, actin-associated cadherin-catenin clusters whose disassembly is maintained by actin depolymerization. It appears then that such actin-dependent αABD clustering is a unique molecular mechanism mediating both integrity and reassembly of the cell-cell adhesive interface formed through weak cis- and trans-intercadherin interactions.
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U2 - 10.1083/jcb.201412064
DO - 10.1083/jcb.201412064
M3 - Article
C2 - 26261181
AN - SCOPUS:84959551575
SN - 0021-9525
VL - 210
SP - 647
EP - 661
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 4
ER -