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Figure 7


Fig. 7. Proposed roles of BNIPXL in regulating Lbc-RhoA-mediated stress fiber formation and cellular transformation. BNIPXL exerts distinct roles in regulating RhoA pathways that are linked to actin cytoskeleton reorganization and oncogenic transformation. The BNIPXL BCH domain targets RhoA via preferential GDP-RhoA binding and also by sequestering the RhoA upstream activator Lbc by targeting its catalytic DH-PH domains. In addition, the N-terminus devoid of the BCH domain, binds to the proline-rich moiety in the C-terminus regulatory region of proto-Lbc. In a concerted manner, these interactions lead to the disruption of stress fibers and suppression of Lbc-induced cellular transformation. This provides further evidence that BCH domain acts as a regulatory GTPase-binding module that targets both small GTPases and their immediate regulators (see text for details).





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