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Título

Mucin 1 (MUC1) is a novel partner for MAL2 in breast carcinoma cells

AutorFanayan, Susan; Shehata, Mona; Agterof, Annelies P.; McGuckin, Michael A.; Alonso, Miguel A.; Byrne, Jennifer A.
Palabras claveMucin 1
Breast Carcinoma
Fecha de publicación28-ene-2009
EditorBioMed Central
CitaciónBMC Cell Biology 2009, 10:7 2009
ResumenBackground: The MAL2 gene, encoding a four-transmembrane protein of the MAL family, is amplified and overexpressed in breast and other cancers, yet the significance of this is unknown. MAL-like proteins have trafficking functions, but their molecular roles are largely obscure, partly due to a lack of known binding partners. Methods: Yeast two-hybrid screening of a breast carcinoma cDNA expression library was performed using a full-length MAL2 bait, and subsequent deletion mapping experiments were performed. MAL2 interactions were confirmed by co-immunoprecipitation analyses and confocal microscopy was employed to compare protein subcellular distributions. Sucrose density gradient centrifugation of membranes extracted in cold Triton X-100 was employed to compare protein distributions between Triton X-100-soluble and -insoluble fractions. Results: The tumor-associated protein mucin 1 (MUC1) was identified as a potential MAL2 partner, with MAL2/ MUC1 interactions being confirmed in myc-tagged MAL2-expressing MCF-10A cells using coimmunoprecipitation assays. Deletion mapping experiments demonstrated a requirement for the first MAL2 transmembrane domain for MUC1 binding, whereas the MAL2 N-terminal domain was required to bind D52-like proteins. Confocal microscopy identified cytoplasmic co-localisation of MUC1 and MAL2 in breast cell lines, and centrifugation of cell lysates to equilibrium in sucrose density gradients demonstrated that MAL2 and MUC1 proteins were co-distributed between Triton X-100-soluble and -insoluble fractions. However coimmunoprecipitation analyses detected MAL2/MUC1 interactions in Triton X-100-soluble fractions only. Myc- MAL2 expression in MCF-10A cells was associated with both increased MUC1 detection within Triton X-100- soluble and -insoluble fractions, and increased MUC1 detection at the cell surface. Conclusion: These results identify MUC1 as a novel MAL2 partner, and suggest a role for MAL2 in regulating MUC1 expression and/or localisation.
Versión del editorhttp://dx.doi.org/10.1186/1471-2121-10-7
URIhttp://hdl.handle.net/10261/24398
DOI10.1186/1471-2121-10-7
ISSN1471-2121
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