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ZRANB1 deubiquitinates UVRAG. 3 / 3
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"However, the deubiquitinase <span class="match term0">ZRANB1</span> specifically cleaves SMURF1-induced K29 and K33-linked polyubiquitin chains from <span class="match term1">UVRAG</span>, thereby increasing the binding of <span class="match term1">UVRAG</span> to RUBCN and inhibiting autophagy flux"

reach
"Furthermore, deubiquitination of UVRAG by ZRANB1 inhibits the autophagy-dependent degradation of EGFR and thereby promotes HCC progression."

"Here we report that UVRAG is ubiquitinated by SMURF1 at lysine residues 517 and 559, which decreases the association of UVRAG with RUBCN and promotes autophagosome maturation. However, the deubiquitinase ZRANB1 specifically cleaves SMURF1-induced K29 and K33-linked polyubiquitin chains from UVRAG, thereby increasing the binding of UVRAG to RUBCN and inhibiting autophagy flux."