p120 catenin associates with kinesin and facilitates the transport of cadherin-catenin complexes to intercellular junctions

Xinyu Chen, Shin Ichiro Kojima, Gary G. Borisy, Kathleen J. Green*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

203 Scopus citations

Abstract

p120 catenin (p120) is a component of adherens junctions and has been implicated in regulating cadherin-based cell adhesion as well as the activity of Rho small GTPases, but its exact roles in cell-cell adhesion are unclear. Using time-lapse imaging, we show that p120-GFP associates with vesicles and exhibits unidirectional movements along microtubules. Furthermore, p120 forms a complex with kinesin heavy chain through the p120 NH2-terminal head domain. Overexpression of p120, but not an NH2-terminal deletion mutant deficient in kinesin binding, recruits endogenous kinesin to N-cadherin. Disruption of the interaction between N-cadherin and p120, or the interaction between p120 and kinesin, leads to a delayed accumulation of N-cadherin at cell-cell contacts during calcium-initiated junction reassembly. Our analyses identify a novel role of p120 in promoting cell surface trafficking of cadherins via association and recruitment of kinesin.

Original languageEnglish (US)
Pages (from-to)547-557
Number of pages11
JournalJournal of Cell Biology
Volume163
Issue number3
DOIs
StatePublished - Nov 10 2003

Keywords

  • Adherens junction
  • Armadillo
  • Microtubule
  • N-cadherin
  • Trafficking

ASJC Scopus subject areas

  • Cell Biology

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