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| pubmed-article:12037680 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:12037680 | pubmed:dateCreated | 2002-5-30 | lld:pubmed |
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| pubmed-article:12037680 | pubmed:abstractText | Protein kinase CK2 is a ubiquitous and pleiotropic Ser/Thr protein kinase involved in cell growth and transformation. Here we report the identification by yeast interaction trap of a CK2 interacting protein, UBC3B, which is highly homologous to the E2 ubiquitin conjugating enzyme UBC3/CDC34. UBC3B complements the yeast cdc34-2 cell cycle arrest mutant in S. cerevisiae and transfers ubiquitin to a target substrate in vitro. UBC3B is specifically phosphorylated by CK2 in vitro and in vivo. We mapped by deletions and site directed mutagenesis the phosphorylation site to a serine residue within the C-terminal domain in position 233 of UBC3B and in the corresponding serine residue of UBC3. Following CK2-dependent phosphorylation both UBC3B and UBC3 bind to the F-box protein beta-TrCP, the substrate recognition subunit of an SCF (Skp1, Cul1, F-box) ubiquitin ligase. Furthermore, we observed that co-transfection of CK2alpha' together with UBC3B, but not with UBC3DeltaC, enhances the degradation of beta-catenin. Taken together these data suggest that CK2-dependent phosphorylation of UBC3 and UBC3B functions by regulating beta-TrCP substrate recognition. | lld:pubmed |
| pubmed-article:12037680 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12037680 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12037680 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12037680 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12037680 | pubmed:issn | 0950-9232 | lld:pubmed |
| pubmed-article:12037680 | pubmed:author | pubmed-author:PinnaLorenzo... | lld:pubmed |
| pubmed-article:12037680 | pubmed:author | pubmed-author:MeggioFlavioF | lld:pubmed |
| pubmed-article:12037680 | pubmed:author | pubmed-author:OlivieroSalva... | lld:pubmed |
| pubmed-article:12037680 | pubmed:author | pubmed-author:SempliciFranc... | lld:pubmed |
| pubmed-article:12037680 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12037680 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:12037680 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:12037680 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12037680 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12037680 | pubmed:pagination | 3978-87 | lld:pubmed |
| pubmed-article:12037680 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:12037680 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12037680 | pubmed:articleTitle | CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation. | lld:pubmed |
| pubmed-article:12037680 | pubmed:affiliation | Dipartimento di Biologia Molecolare, Università degli Studi di Siena, Italy. | lld:pubmed |
| pubmed-article:12037680 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12037680 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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