Lipid Raft Association Restricts CD44-Ezrin Interaction and Promotion of Breast Cancer Cell Migration

Cancer cell migration is an early event in metastasis, the main cause of breast cancer-related deaths. Cholesterol-enriched membrane domains called lipid rafts influence the function of many molecules, including the raft-associated protein CD44. We describe a novel mechanism whereby rafts regulate interactions between CD44 and its binding partner ezrin in migrating breast cancer cells. Specifically, in nonmigrating cells, CD44 and ezrin localized to different membranous compartments: CD44 predominantly in rafts, and ezrin in nonraft compartments. After the induction of migration (either nonspecific or CD44-driven), CD44 affiliation with lipid rafts was decreased. This was accompanied by increased coprecipitation of CD44 and active (threonine-phosphorylated) ezrin-radixin-moesin (ERM) proteins in nonraft compartments and increased colocalization of CD44 with the nonraft protein, transferrin receptor. Pharmacological raft disruption using methyl-β-cyclodextrin also increased CD44-ezrin coprecipitation and colocalization, further suggesting that CD44 interacts with ezrin outside rafts during migration. Conversely, promoting CD44 retention inside lipid rafts by pharmacological inhibition of depalmitoylation virtually abolished CD44-ezrin interactions. However, transient single or double knockdown of flotillin-1 or caveolin-1 was not sufficient to increase cell migration over a short time course, suggesting complex crosstalk mechanisms. We propose a new model for CD44-dependent breast cancer cell migration, where CD44 must relocalize outside lipid rafts to drive cell migration. This could have implications for rafts as pharmacological targets to down-regulate cancer cell migration. Cancer cell migration is an early event in metastasis, the main cause of breast cancer-related deaths. Cholesterol-enriched membrane domains called lipid rafts influence the function of many molecules, including the raft-associated protein CD44. We describe a novel mechanism whereby rafts regulate interactions between CD44 and its binding partner ezrin in migrating breast cancer cells. Specifically, in nonmigrating cells, CD44 and ezrin localized to different membranous compartments: CD44 predominantly in rafts, and ezrin in nonraft compartments. After the induction of migration (either nonspecific or CD44-driven), CD44 affiliation with lipid rafts was decreased. This was accompanied by increased coprecipitation of CD44 and active (threonine-phosphorylated) ezrin-radixin-moesin (ERM) proteins in nonraft compartments and increased colocalization of CD44 with the nonraft protein, transferrin receptor. Pharmacological raft disruption using methyl-β-cyclodextrin also increased CD44-ezrin coprecipitation and colocalization, further suggesting that CD44 interacts with ezrin outside rafts during migration. Conversely, promoting CD44 retention inside lipid rafts by pharmacological inhibition of depalmitoylation virtually abolished CD44-ezrin interactions. However, transient single or double knockdown of flotillin-1 or caveolin-1 was not sufficient to increase cell migration over a short time course, suggesting complex crosstalk mechanisms. We propose a new model for CD44-dependent breast cancer cell migration, where CD44 must relocalize outside lipid rafts to drive cell migration. This could have implications for rafts as pharmacological targets to down-regulate cancer cell migration. The membrane protein CD44 is a multifaceted molecule involved in many different cellular processes, including organ development, neuronal axon guidance, immune functions, hematopoiesis, and migration.1Sherman L. Sleeman J. Dall P. Hekele A. Moll J. Ponta H. Herrlich P. The CD44 proteins in embryonic development and in cancer.Curr Top Microbiol Immunol. 1996; 213: 249-269Crossref PubMed Scopus (57) Google Scholar, 2Lin L. Cheung A.W. Chan S.O. Chiasmatic neurons in the ventral diencephalon of mouse embryos—changes in arrangement and heterogeneity in surface antigen expression.Brain Res Dev Brain Res. 2005; 158: 1-12Crossref PubMed Scopus (13) Google Scholar, 3Haynes B.F. Telen M.J. Hale L.P. Denning S.M. CD44—a molecule involved in leukocyte adherence and T-cell activation.Immunol Today. 1989; 10: 423-428Abstract Full Text PDF PubMed Scopus (507) Google Scholar, 4Smadja-Joffe F. Legras S. Girard N. Li Y. Delpech B. Bloget F. Morimoto CD44 and binding by 1996; PubMed Scopus Google as a for the of and its CD44 in the of PubMed Scopus Google Scholar, P. B. H. of interactions in and Res. PubMed Scopus Google and for the protein S. H. between CD44 and as a for Google CD44 is an of cellular and migration to its active influence the of the This interactions between CD44 and different of the proteins to the (ERM) The proteins a between CD44 and the cell that for cell migration. interacts with CD44 and its and the of domains with and the binding for CD44 and is by novel mechanism CD44 ezrin and cell PubMed Scopus Google with for binding to the Y. S. S. S. of (ERM) proteins and PubMed Scopus Google of CD44 also to for its in the novel mechanism CD44 ezrin and cell PubMed Scopus Google Scholar, of the a in Full Text PDF PubMed Google CD44 to in and membrane lipid S. H. 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