| http://purl.uniprot.org/citations/17532294 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17532294 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17532294 | http://www.w3.org/2000/01/rdf-schema#comment | "The microtubule motor cytoplasmic dynein and its activator dynactin drive vesicular transport and mitotic spindle organization. p150(Glued) is the dynactin subunit responsible for binding to dynein and microtubules. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which governs phosphorylation-dependent ubiquitination and subsequent proteolysis. Our recent study showed that the proteolysis of mitotic kinesin CENP-E is mediated by SCF via a direct Skp1 link [D. Liu, N. Zhang, J. Du, X. Cai, M. Zhu, C. Jin, Z. Dou, C. Feng, Y. Yang, L. Liu, K. Takeyasu, W. Xie, X. Yao, Interaction of Skp1 with CENP-E at the midbody is essential for cytokinesis, Biochem. Biophys. Res. Commun. 345 (2006) 394-402]. Here we show that F-box protein FBXL5 interacts with p150(Glued) and orchestrates its turnover via ubiquitination. FBXL5 binds to p150(Glued)in vitro and in vivo. FBXL5 and p150(Glued) co-localize primarily in the cytoplasm with peri-nuclear enrichment in HeLa cells. Overexpression of FBXL5 promotes poly-ubiquitination of p150(Glued) and protein turnover of p150(Glued). Our findings provide a potential mechanism by which p150(Glued) protein function is regulated by SCFs."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2007.05.068"xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2007.05.068"xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/author | "Liu J."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/author | "Liu J."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/author | "Zhang N."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/author | "Zhang N."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/author | "Ding X."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/author | "Ding X."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/author | "Jin C."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/author | "Jin C."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/author | "Yao X."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/author | "Yao X."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/author | "Aikhionbare F."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/author | "Aikhionbare F."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/pages | "34-39"xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/pages | "34-39"xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/title | "FBXL5 interacts with p150Glued and regulates its ubiquitination."xsd:string |
| http://purl.uniprot.org/citations/17532294 | http://purl.uniprot.org/core/title | "FBXL5 interacts with p150Glued and regulates its ubiquitination."xsd:string |