The interplay between SASH1 and CEACAM1 in cancer cells.
116 THE INTERPLAY BETWEEN SASH1 AND CEACAM1 IN CANCER CELLS
SAM and SH3 domain containing protein 1 (SASH1) is identified to be a tumor suppressor gene for breast cancer. Reduced expression of SASH1 has been found in 74% of breast tumors when compared to normal breast epithelial cells, as well as in lung and thyroid tumors. The carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1), another promising tumor suppressor protein, has been shown to upregulate SASH1. To better understand the relationship between SASH1 and CEACAM1, we explored the localization of SASH1 in the presence or absence of CEACAM1 and the binding partners of SASH1. SASH1 appeared in the nucleus and the cytoplasm of the immortalized, ovarian cancer cell line HeLa in the both presence and absence of CEACAM1. Furthermore, beta-actin was identified as a binding partner of SASH1. We have also determined SASH1 does not normally have tyrosine phosphorylation in HeLa cells. Further analysis of the SASH1 tyrosine phosphorylation status in HeLa cells transfected with CEACAM 1, as well as the SASH1 serine and threonine phosphorylation status in HeLa cells, should shed more light on the function of SASH 1.
J. Ou and K. Stubblefield. City of Hope, Department of Immunology, Duarte, CA 91010. Mentor: John Shively. City of Hope, Department of Immunology, Duarte, CA 91010
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|Title Annotation:||SATURDAY ABSTRACTS IN PROGRAM ORDER|
|Author:||Ou, J.; Stubblefield, K.|
|Publication:||Bulletin (Southern California Academy of Sciences)|
|Article Type:||Author abstract|
|Date:||Aug 1, 2014|
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