LAUSR

Receptor for activated C kinase 1 (RACK1), a scaffold protein, plays a crucial role in the progression of various cancers. However, the biological function and underlying mechanism of RACK1 in multiple myeloma (MM) cells remain unclear. The present study aimed to explore the function of RACK1 on the cell proliferation, adhesion, and bortezomib-induced apoptosis in MM. We found that RACK1 was significantly overexpressed in myeloma cell lines and primary myeloma cells compared with normal bone marrow plasma cells. Moreover, immunofluorescence revealed that RACK1 was primarily expressed in the cytoplasm of MM cells. Knockdown of RACK1 impaired growth of MM cells, blocked entry into the S-phase of the cell cycle, and resulted in reduced cell adhesion rates. More importantly, knockdown of RACK1 decreased the proliferation of MM cells by activating P-P38 and P-ERK in the MAPK/ERK signaling pathway. We also found that altered expression of RACK1 is associated with bortezomib-mediated MM cell apoptosis. In summary, these results may provide a possible target for therapy in MM.