IndraLab

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Ubiquitin activates USP14. 7 / 8
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"On the substrate-engaged pathway, ubiquitin-dependent activation of USP14 allosterically reprograms the conformational landscape of the AAA-ATPase motor and stimulates opening of the core particle gate 8-10 , enabling observation of a near-complete cycle of asymmetric ATP hydrolysis around the ATPase ring during processive substrate unfolding."
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"The 26S proteasome-mediated degradation of a ubiquitinated protein target involves an initial Ub recognition step that is primarily mediated by subunits Rpn10 and Rpn13 of the 19S RP [8,9], followed by deubiquitination of the substrate by Rpn11 or one of two other proteasome-associated deubiquitinating enzymes (DUBs), UCH37 and USP14."
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"Thus, USP14 affinity towards the proteasome reflects interactions of both its UBL and USP domains and is enhanced by Ub –Sic1 , consistent with previous studies ."
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"This is followed by a distinct association step of its USP domain with the OB ring of the AAA-ATPase motor in a ubiquitin-dependent manner, which allosterically activates USP14 and reciprocally stabilizes the proteasome in the substrate-inhibited states."
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"Intriguingly, Ub deficiency induced the upregulation of USP14 in mammals (Ryu KY, unpublished data) and Ubp6 in yeast XREF_BIBR, thereby sparing Ub from proteasomal degradation and increasing levels of free Ub in an attempt to reach Ub homeostasis."
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"On the substrate-engaged pathway, ubiquitin-dependent activation of USP14 allosterically reprograms the conformational landscape of the AAA-ATPase motor and stimulates opening of the core particle gate xref – xref , enabling observation of a near-complete cycle of asymmetric ATP hydrolysis around the ATPase ring during processive substrate unfolding."
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"Ubiquitin promotes the Ubp6 and Usp14 noncatalytic effect [52,56-58]."
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