IndraLab

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USP14 deubiquitinates CXCR4. 7 / 7
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"These data suggest that the USP14 gene product indeed serves as a catalyst to deubiquitinate the CXCR4, because when its expression is reduced there is a reciprocal increase in CXCR4 ubiquitination."
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"Co-localization of CXCR4 and USP14 also is time-dependent following CXCL12 stimulation."
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"Deubiquitination of CXCR4 by USP14 would thus be expected to reduce the rate of ligand accelerated receptor degradation and result in an increased steady state level of receptors."
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"Deubiquitination of CXCR4 by USP14 Is Critical for Both CXCL12 induced CXCR4 Degradation and Chemotaxis but Not ERK Activation *."
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"The physical interaction of CXCR4 and USP14 is paralleled by USP14 catalyzed deubiquitination of the receptor; knockdown of endogenous USP14 by RNA interference (RNAi) blocks CXCR4 deubiquitination, whereas overexpression of USP14 promotes CXCR4 deubiquitination."
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"In summary, our findings demonstrate that CXCL12 activation of the CXCR4 leads to a dynamic ubiquitination and deubiquitination cycle and that USP14 preferentially interacts with and deubiquitinates CXCR4."
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"Deubiquitination of CXCR4 by USP14 is critical for both CXCL12 induced CXCR4 degradation and chemotaxis but not ERK ativation."
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