IndraLab

Statements

ATXN3 inhibits Ubiquitin. 11 / 12
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"Together, these results indicate that ataxin-3 functions with CHIP to prevent the incorporation of additional ubiquitin to chains on substrates once they reach a certain length."
21855799
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"Thus, in one possible mechanism of suppression, ataxin-3 could suppress toxicity by simply increasing the pool of free ubiquitin."
15808507
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"For instance, the deubiquitinase Ataxin-3 was shown to interact with C-terminus of Hsc70 Interacting Protein (CHIP), a major mammalian E3 ligase involved in cytosolic PQC, to limit the length of ubiquitin chains built on CHIP substrates XREF_BIBR."
27698423
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"By binding the minimum length poly-ubiquitin chain on substrates, ATXN3 may prevent complete removal of the ubiquitin chain by other DUBs, and thus facilitate its recognition by the 26S proteasome."
31669734
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"We have found that aggregation of polyQ expanded Atx3 can sequester P97 and Ub conjugates into the protein aggregates or inclusions through specific interactions both in vitro and in cells."
25231079
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"These results support a model in which ataxin-3 effectively limits ubiquitin chain extension once chains reach a critical length."
21855799
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"When substrates are soluble, ATX3 prevents their premature degradation by removing K48‐linked Ub chains to slow down the rate of p97‐dependent degradation."
31613024
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"PolyQ expanded huntingtin and ataxin-3 sequester ubiquitin adaptors hHR23B and UBQLN2 into aggregates via conjugated ubiquitin."
29401586
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"Absence of ataxin-3 UIMs 1 and 2 shows reduced binding of ubiquitin chains."
27731380
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"An unbiased, semi-automated quantitative analysis (XREF_SUPPLEMENTARY) revealed that knock-down of ataxin-3 indeed impaired the accumulation ofRNF8 (Fig XREF_FIG A), RNF168 (Fig XREF_FIG B), and ubiquitin conjugates atlaser induced DSBs (Fig XREF_FIG C)."
28275011
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"In CHIP ubiquitination assays, ataxin-3 functions to restrict the length of ubiquitin chains attached to CHIP substrates, terminating ubiquitin incorporation once chains reach a critical length."
21855799