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CK2 phosphorylates USP48. 6 / 6
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"These results indicate that CK2-mediated phosphorylation of USP48 at its C-terminal CK2 consensus sites and its binding to K48-linked Ub-chains ( Fig. 5 H), both of which promote USP48 Ub-chain-trimmi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"CK2-mediated phosphorylation of USP48 at C-terminal CK2 consensus sites, in vitro and in response to TNF, enhances its Ub-chain-trimming activity ( Fig. 8 A–C)."
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"We demonstrate that (I) USP48 preferentially trims long (K48-linked) Ub-chains, an as yet unique property within the USP family, (II) CK2 phosphorylates USP48 at C-terminal CK2 consensus sites, thereb[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Phosphorylation of USP48 at its C-terminal CK2 consensus sites was evidenced in in vitro phosphorylation assays with recombinant CK2 and epitope-tagged USP48 variants, which, after overexpression, had[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The ability of CK2 to phosphorylate USP48 at C-terminal sites was confirmed in kinase assays with recombinant USP48 variants, tagged at the N-term with GST."
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"In support of a functional role of CK2 in the regulation of USP48 catalytic activity, phosphorylation of USP48 at CK2 consensus sites as well as co-IP of CK2α and CSN (CSN3) were observed 2 h after TN[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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