Published 10 November 2003. doi:10.1083/jcb.200305137
© The Rockefeller University Press,
0021-9525/2003/11/547 $8.00
The Journal of Cell Biology, Volume 163, Number 3, 547-557
p120 catenin associates with kinesin and facilitates the transport of cadherincatenin complexes to intercellular junctions
Xinyu Chen1,
Shin-ichiro Kojima2,
Gary G. Borisy2 and
Kathleen J. Green1
1 Departments of Pathology and Dermatology, R.H. Lurie Cancer Center, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611
2 Department of Cell and Molecular Biology, R.H. Lurie Cancer Center, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611
Address correspondence to Kathleen J. Green, Dept. of Pathology, Feinberg School of Medicine, Northwestern University, 303 E. Chicago Ave., Chicago, IL 60611. Tel.: (312) 503-5300. Fax: (312) 503-8240. email: kgreen{at}northwestern.edu
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 cellcell 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 cellcell 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.
Key Words: Armadillo; adherens junction; N-cadherin; microtubule; trafficking
The online version of this article includes supplemental material.
Abbreviations used in this paper: Arm, armadillo; JMD, juxtamembrane domain; KHC, kinesin heavy chain; KLC, kinesin light chain; MT, microtubule; p120, p120 catenin.

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