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    Lipid raft association restricts CD44-ezrin interaction and promotion of breast cancer cell migration.

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    Authors
    Donatello, Simona
    Babina, Irina S
    Hazelwood, Lee D
    Hill, Arnold D K
    Nabi, Ivan R
    Hopkins, Ann M
    Affiliation
    Department of Surgery, Royal College of Surgeons in Ireland, Beaumont Hospital, Dublin 9, Ireland.
    Issue Date
    2012-12
    MeSH
    Antigens, CD44
    Breast Neoplasms
    Caveolin 1
    Cell Compartmentation
    Cell Line, Tumor
    Cell Movement
    Cytoskeletal Proteins
    Female
    Gene Knockdown Techniques
    Humans
    Hyaluronic Acid
    Membrane Microdomains
    Membrane Proteins
    Models, Biological
    Protein Binding
    Protein Transport
    Subcellular Fractions
    beta-Cyclodextrins
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    Citation
    Lipid raft association restricts CD44-ezrin interaction and promotion of breast cancer cell migration. 2012, 181 (6):2172-87 Am. J. Pathol.
    Journal
    The American journal of pathology
    URI
    http://hdl.handle.net/10147/292693
    DOI
    10.1016/j.ajpath.2012.08.025
    PubMed ID
    23031255
    Additional Links
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3502863/
    Abstract
    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.
    Item Type
    Article
    Language
    en
    ISSN
    1525-2191
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.ajpath.2012.08.025
    Scopus Count
    Collections
    Beaumont Hospital

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