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A more recent version of this article appeared on May 1, 2002
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Submitted on July 3, 2001
Revised on January 11, 2002
Accepted on February 1, 2002
1 University of Pennsylvania (present address: Xencor, Inc., Monrovia, CA 91016
2 University of Pennsylvania
3 143 Rosenthal Bldg., 3800 Spruce Street, Philadelphia, PA 19104-6046
* Corresponding author. E-mail address: holzbaur{at}vet.upenn.edu.
We screened for polypeptides that interact specifically with dynein, and identified a novel 24-kDa protein (PLAC-24) that binds directly to dynein intermediate chain. PLAC-24 is not a dynactin subunit, and the binding of PLAC-24 to the dynein intermediate chain is independent of the association between dynein and dynactin. Immunocytochemistry using PLAC-24-specific polyclonal antibodies revealed a punctate perinuclear distribution of the polypeptide in fibroblasts and isolated epithelial cells. However, as epithelial cells in culture make contact with adjacent cells, PLAC-24 is specifically recruited to the cortex at sites of contact, where the protein co-localizes with components of the adherens junction. Disruption of the cellular cytoskeleton with latrunculin or nocodazole indicates that the localization of PLAC-24 to the cortex is dependent on intact actin filaments but not on microtubules. Overexpression of ß-catenin also leads to a loss of PLAC-24 from sites of cell-cell contact. Based on these data and the recent observation that cytoplasmic dynein is also localized to sites of cell-cell contact in epithelial cells, we propose that PLAC-24 is part of a multi-protein complex localized to sites of intercellular contact that may function to tether microtubule plus ends to the actin-rich cellular cortex.
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