Work

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

Year: 2003

Type: article

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.

Source: The Journal of Cell Biology

DOI: 10.1083/jcb.200305137

Authors: Xinyu Chen, Shin-ichiro Kojima, Gary G. Borisy, Kathleen J. Green

Institutions: Northwestern University, Robert H. Lurie Comprehensive Cancer Center of Northwestern University

Language: English

Topic: Cell Adhesion Molecules Research

Subfield: Immunology and Allergy

Field: Medicine

Domain: Health Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institute of Dental and Craniofacial Research

Awards: MECHANISM AND CONTROL OF MICROTUBULE ASSEMBLY, Junctions, Cytoskeleton & Matrix of the Oral Epithelium, Function of Desmoglein 1/Pemphigus Foliaceus Antigen