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Vol. 17, Issue 5, 2366-2376, May 2006

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The Cadherin-11 Cytoplasmic Juxtamembrane Domain Promotes -Catenin Turnover at Adherens Junctions and Intercellular Motility

Hans P. Kiener ^*, Christopher S. Stipp  , Philip G. Allen ^*, Jonathan M.G. Higgins ^*, and Michael B. Brenner ^*

^* Department of Medicine, Division of Rheumatology, Immunology, and Allergy, Brigham and Women's Hospital, Boston, MA 02115; Dana-Farber Cancer Institute, Department of Cancer Immunology and AIDS, Harvard Medical School, Boston, MA 02115

Submitted August 11, 2005; Revised February 21, 2006; Accepted February 27, 2006
Monitoring Editor: Ben Margolis

Cadherins mediate homophilic cell adhesion and contribute to tissue morphogenesis and architecture. Cadherin cell adhesion contacts are actively remodeled and impact cell movement and migration over other cells. We found that expression of a mutant cadherin-11 lacking the cytoplasmic juxtamembrane domain (JMD) diminished the turnover of -catenin at adherens junctions as measured by fluorescence recovery after photobleaching. This resulted in markedly diminished cell intercalation into monolayers reflecting reduced cadherin-11-dependent cell motility on other cells. Furthermore, the actin cytoskeleton in cadherin-11 JMD cells revealed a more extensive cortical F-actin ring that correlated with significantly higher levels of activated Rac1. Together, these data implicate the cadherin-11 cytoplasmic JMD as a regulator of -catenin turnover at adherens junctions and actin-cytoskeletal organization that is critical for intercellular motility and rearrangement in multicellular clusters.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Present address: Department of Biological Sciences, University of Iowa, Iowa City, IA 52242.

Address correspondence to: Michael B. Brenner (mbrenner{at}rics.bwh.harvard.edu).

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