Journal
JOURNAL OF CELL BIOLOGY
Volume 163, Issue 3, Pages 547-557Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200305137
Keywords
armadillo; adherens junction; N-cadherin; microtubule; trafficking
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Funding
- NIAMS NIH HHS [R01AR41836, R01 AR041836] Funding Source: Medline
- NIDCR NIH HHS [P01DE12328, P01 DE012328] Funding Source: Medline
- NIGMS NIH HHS [R01GM25062, R01 GM025062] Funding Source: Medline
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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.
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