IndraLab

Statements

USP14 binds UBP6. 6 / 6
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"This mutual interaction of USP14 and Ubp6 with the proteasome is thought to enhance selectivity of the proteasome for ubiquitinated proteins and couple deubiquitination to degradation."
26998235
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"Binding of USP14 or its yeast ortholog, UBP6, to the proteasome activates the catalytic activity of the DUB through an unknown mechanism xref ."
19243136
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"Cleavage within ubiquitin chains by free forms of USP14 and Ubp6, as observed by many researchers, may reflect that free USP14 is not subject to occlusion from proteasome subunits."
27074503
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"One possible explanation is that Usp14 and Ubp6 in its substrate bound conformation exerts multiple regulatory effects on proteasomal function that are linked."
20005843
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"As described above, recent cryo-EM data suggest that the Ubp6 and USP14 bound proteasome strongly favors the S2 state conformation, in which the ubiquitin charged catalytic domain of Ubp6 and USP14 makes stable contacts with the base RPT ring [XREF_BIBR, XREF_BIBR, XREF_BIBR]."
32726943
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"USP14 and its yeast homolog Ubp6 both bind to the regulatory subunit of the proteasome via their Ub-like domain which greatly stimulates their catalytic activities ( xref , xref )."
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