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Structural basis for p50RhoGAP BCH domain–mediated regulation of Rho inactivation
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Significance
Small GTPases are binary proteins that rapidly switch between active and inactive states through the actions of GEF- and GTPase-activating proteins (GAPs), respectively. GAPs play significant roles in cellular signaling, and their dysregulation is linked to numerous cancers. Here, we show that the BNIP-2 and Cdc42GAP Homology (BCH) domain of p50RhoGAP, known to autoinhibit the adjacent GAP domain, adopts an intertwined, dimeric structure with unique RhoA interactions. The β5-strand of the BCH domain plays a crucial role in the autoinhibition of the GAP domain. A mutation in the β5-strand destabilizes this autoinhibition and leads to RhoGAP activation. Our studies on the dynamics of the RhoGAP BCH domain will clarify its potential role in cancer and other diseases.
Proceedings of the National Academy of Sciences
Title: Structural basis for p50RhoGAP BCH domain–mediated regulation of Rho inactivation
Description:
Significance
Small GTPases are binary proteins that rapidly switch between active and inactive states through the actions of GEF- and GTPase-activating proteins (GAPs), respectively.
GAPs play significant roles in cellular signaling, and their dysregulation is linked to numerous cancers.
Here, we show that the BNIP-2 and Cdc42GAP Homology (BCH) domain of p50RhoGAP, known to autoinhibit the adjacent GAP domain, adopts an intertwined, dimeric structure with unique RhoA interactions.
The β5-strand of the BCH domain plays a crucial role in the autoinhibition of the GAP domain.
A mutation in the β5-strand destabilizes this autoinhibition and leads to RhoGAP activation.
Our studies on the dynamics of the RhoGAP BCH domain will clarify its potential role in cancer and other diseases.
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