Autoinhibition of RhoGEFs FARP1 and FARP2
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| Crystal structures reveal a multi-layered autoinhibtion mechanism for the guanine nucleotide exchange factors FARP2 and its homolog FARP1. (see details in: He et al, Structure, 2013) |
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Plexins as RapGAPs and a structure of the plexin/Rac1 complex
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| This study shows that Plexins are GTPase activating proteins specific for the small GTPase Rap. The RapGAP activity is activated by induced dimerization, and Rac1 binding does not contribute to this activation process directly. (see details in: Wang, He et al, Science Signaling, 2012) |
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REDD1 structure: a novel fold and a functional hotspot
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| The functional C-terminal domain of REDD1 adopts a novel topology. Two conserved segments form a surface patch critical for function (blue in the middel panel), indicating a hotspot for binding downstream signaling protein. (see details in: Vega-Rubin-de-Celis et al, Biochemistry, 2010) |
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Regulation mechanism of the Plexin A3 intracellular region
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| The GAP domain of Plexin A3 adopts an inactive conformation (left panel), which cannot accomodate Ras in its substrate binding site (middle panel). The N-terminal segment (red) and the RBD (blue) regulate the GAP through an allosteric mechanism. (see details in: He et al, PNAS, 2009; 100: 2586-2591) |
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| Previous Work |
Inhibition of EGFR by Mig6
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Activation of the EGFR kinase
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B7-2/CTLA4 Complex
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