Abstract
Abstract : BAG-family proteins regulate diverse cellular functions, including cell survival, cell proliferation, and cell motility. BAG-family proteins contain a conserved domain that allows them to bind 70-kD heat shock (Hsp70) family molecular chaperones and regulate their activity. Structural analysis of the Hsc70-binding BAG domain of BAGl has revealed an anti-parallel two helix bundle, proceeded by an additional long alpha-helix. Site-directed mutagenesis has confirmed that the polar surfaces of the alpha-helices in the BAG domain are directly involved in chaperone binding, which has been confirmed by NMR experiments. Similarly, an 80 amino acid region (229-308) of Hsc70 has been determined to represent a minimal domain sufficient for binding the BAG domain. In addition to the Hsc70-binding domain, BAG-family proteins also contain a diversity of additional domains, which allow them to interact with specific target proteins or which target them to specific locations within cells. The BAG-family proteins operate as bridging molecules that recruit molecular chaperones to target proteins and ultimately affecting diverse cellular behaviors including cell division, migration, differentiation, and death in cancer cells. Recently BAG3 was reported as a regulator of cell growth. Our preliminary result also shows BAG3 might have a tumorigenic activity.
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