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Statements

USP11 binds XIAP. 17 / 18
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"As shown in XREF_FIG D-F, replacing Leu207 with proline, but not mutation of Cys203 or Lys206 to alanine, significantly destabilizes XIAP, presumably, due to the perturbation of the interfacial interaction between USP11 and XIAP and reduced deubiquitylation capacity of USP11."
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"In addition, expression of wild-type XIAP leads to the inhibition of anoikis, we observed that disruption of interaction between XIAP and USP11 by expression of XIAP L207P mutant (interaction deficient) significantly attenuates the inhibition of anoikis by XIAP (Supplemental Fig. 6)."
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"The interaction of XIAP with USP11 was confirmed by blotting complexes having endogenous USP11 precipitated with XIAP specific antibodies ( xref C) or complexes of overexpressed tagged USP11 with antibodies against Myc tag ( xref D) and probing for XIAP."
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"C-terminus of USP11 interacts with the BIR2 domain of XIAP and deubiquitinates it leading to inhibition of apoptosis (Zhou et al., xref ; Table xref )."
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No evidence text available
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"Based on protein complex purification coupled with mass spectrometry, we have demonstrated that XIAP is a target of USP11, wherein USP11 directly binds to XIAP through Leu207 on XIAP and stabilizes it by deubiquitylation of XIAP."
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No evidence text available
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"As shown in xref D–F, replacing Leu207 with proline, but not mutation of Cys203 or Lys206 to alanine, significantly destabilizes XIAP, presumably, due to the perturbation of the interfacial interaction between USP11 and XIAP and reduced deubiquitylation capacity of USP11."
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"To validate the impact of Cys203 and Leu207 as well as Lys206 on XIAP in mediating the interaction of XIAP with USP11, we performed a multiple sequence alignment at that particular region (residues 200–210), using the aligned the amino acid stretch from 200 to 210 of human XIAP with mouse, rat and xenopus XIAP sequences as well as the human CIAP1 and CIAP2."
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"XIAP is directly bound to USP11 as shown here by both experimental and computational examinations."
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"These results further suggested that Leu207 was the critical residue on XIAP in mediating the binding between USP11 and XIAP."
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"The above analysis helped us narrow down the interfacial residues of the XIAP and USP11 complex to 503-963 (on USP11) and 200-210 (on XIAP)."
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"XIAP is directly bound to USP11 as shown here by both experimental and computational examinations."
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No evidence text available
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"To further characterize and visualize the mechanism of interaction between USP11 and XIAP, we performed molecular docking simulations, using the computational methods described earlier ( xref )."
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"Thus, further efforts to elucidate the underlying mechanism of USP11 regulation by UPS in response to growth factor signaling will shed light on the role of USP11-XIAP interaction in regulating tumorigenesis."
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