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USP14 deubiquitinates CXCR4. 8 / 10
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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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"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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"A previous study showed that USP14 modulates cancer cell motility by deubiquitinating the chemokine receptor CXC chemokine receptor 4 (CXCR4)."

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"Knockdown of endogenous USP14 blocks CXCR4 deubiquitination and leading to downregulated chemotactic response to CXCL12 [117]."

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"Mines et al. found that USP14 could induce deubiquitination of CXCR4, thus facilitating its degradation [ 44 ]."

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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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"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."