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lüll Cell-surface and mitotic-spindle RHAMM: moonlighting or dual oncogenic functions?Maxwell CA; McCarthy J; Turley EJ Cell Sci 2008[Apr]; 121 (Pt 7): 925-32Tumor cells use a wide variety of post-translational mechanisms to modify the functional repertoire of their transcriptome. One emerging but still understudied mechanism involves the export of cytoplasmic proteins that then partner with cell-surface receptors and modify both the surface-display kinetics and signaling properties of these receptors. Recent investigations demonstrate moonlighting roles for the proteins epimorphin, FGF1, FGF2, PLK1 and Ku80, to name a few, during oncogenesis and inflammation. Here, we review the molecular mechanisms of unconventional cytoplasmic-protein export by focusing on the mitotic-spindle/hyaluronan-binding protein RHAMM, which is hyper-expressed in many human tumors. Intracellular RHAMM associates with BRCA1 and BARD1; this association attenuates the mitotic-spindle-promoting activity of RHAMM that might contribute to tumor progression by promoting genomic instability. Extracellular RHAMM-CD44 partnering sustains CD44 surface display and enhances CD44-mediated signaling through ERK1 and ERK2 (ERK1/2); it might also contribute to tumor progression by enhancing and/or activating the latent tumor-promoting properties of CD44. The unconventional export of proteins such as RHAMM is a novel process that modifies the roles of tumor suppressors and promoters, such as BRCA1 and CD44, and might provide new targets for therapeutic intervention.|Animals[MESH]|BRCA1 Protein/metabolism[MESH]|Extracellular Matrix Proteins/genetics/*metabolism[MESH]|Gene Expression Regulation, Neoplastic[MESH]|Humans[MESH]|Hyaluronan Receptors/genetics/*metabolism[MESH]|Models, Biological[MESH]|Neoplasms/genetics/metabolism/pathology[MESH]|Protein Transport[MESH]|Spindle Apparatus/*metabolism[MESH] |