IndraLab

Statements

TP53 binds ATXN3. 33 / 40
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"Li-Fraumeni syndrome (LFS) is an autosomal dominant disease that is associated with germline TP53 mutations and it predisposes affected individuals to a high risk of developing multiple tumors."
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"We wonder whether the polyQ expansion affects the ATX-3 and p53 interaction."
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"We have found that ATX-3 interacts with p53 and functions as a novel p53 DUB."
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"Therefore, both the Josephin and UIM domain coordinately regulate the interaction between ATX-3 and p53 ( xref )."
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"The interaction between ATX-3 and p53 was confirmed under physiological condition ( xref ) and with in vitro purified forms ( xref ), indicating a direct association between these two proteins."
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No evidence text available
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"Consistently, as shown in xref , the cysteine 14 mutation did not affect the binding of ATX-3 to either native or ubiquitinated p53, whereas the ΔN mutant lost its binding to both forms of p53."
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"Instructively, mutations effecting the expression of p53 are associated with Li Fraumini syndrome, an autosomal dominant hereditary cancer predisoposition syndrome."
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"As ATX-3 interacts with p53 under physiological conditions and regulates the ubiquitination of p53 in cells, it is possible that ATX-3 may regulate the turnover of p53 via the Ub-proteasome pathway."
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No evidence text available
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"ATX-3 Interacts with p53."
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"During deubiquitination process, ATX3 mainly associates with ubiquitinated p53 through its UIMs domain."
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"Ataxin-3, the machado-joseph disease deubiquitinase, interacts with p53 and functions as a novel p53 DUB [XREF_BIBR]."
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No evidence text available
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"The interaction between ATX-3 and p53 suggested that p53 might be a substrate of ATX-3."
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"ATX-3 binds to native and polyubiquitinated p53 and deubiquitinates and stabilizes p53 by repressing its degradation through the ubiquitin (Ub)-proteasome pathway."
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"The interaction between ATX-3 and p53 was confirmed under physiological condition (XREF_FIG) and with in vitro purified forms (XREF_FIG), indicating a direct association between these two proteins."
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"Here in our study, we discovered that ATX-3 interacts with p53 and functions as a DUB for p53."
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"Liu et al. found that the pathological ATX3 binds to p53 with a stronger affinity compared to wild-type ATX3."
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"Taken together, these results indicated that the binding of ATX-3 to p53 was synergistically regulated by the Josephin domain and the UIMs, with the former being primarily responsible for the binding of ATX-3 to the native p53 and further facilitating the latter to bind to ubiquitinated p53."
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"We have found that ATX-3 interacts with p53 and functions as a novel p53 DUB."
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"Ten of the mutations we described have been reported in Li-Fraumeni families ( xref ), an autosomal dominant syndrome associated with germline TP53 mutations, characterised by a high incidence of a range of tumours, with WT not being one of the cardinal tumours included in the diagnostic criteria."
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No evidence text available
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"The interaction between ATX-3 and p53 suggested that p53 might be a substrate of ATX-3."
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"Taken together, these results indicated that the binding of ATX-3 to p53 was synergistically regulated by the Josephin domain and the UIMs, with the former being primarily responsible for the binding of ATX-3 to the native p53 and further facilitating the latter to bind to ubiquitinated p53."
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"Therefore, both the Josephin and UIM domain coordinately regulate the interaction between ATX-3 and p53 (XREF_FIG)."
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"Here in our study, we discovered that ATX-3 interacts with p53 and functions as a DUB for p53."
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"Germ line mutations in p53 are associated with an inherited autosomal dominant TRANSGENIC MODELS AND CANCER TREATMENT 571 predisposition to early onset cancer referred to as the Li-Fraumeni syndro[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"We have observed that the Josephin domain of ATX-3 is sufficient for the direct binding of ATX-3 to native p53, whereas the ubiquitinated p53 interacts with ATX-3 primarily through the UIMs, indicating that UIMs function to help recruit and bind the ubiquitinated p53 ( xref )."
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No evidence text available
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"As ATX-3 interacts with p53 under physiological conditions and regulates the ubiquitination of p53 in cells, it is possible that ATX-3 may regulate the turnover of p53 via the Ub-proteasome pathway."
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"The direct interaction between ATX-3 and p53 is primarily mediated by the Josephin domain, and the first two UIM domains function to enhance the interaction by trapping the Ub-chains on p53."
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"ATX-3 binds to native and polyubiquitinated p53 and deubiquitinates and stabilizes p53 by repressing its degradation through the ubiquitin (Ub)-proteasome pathway."
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