کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1937568 | 1050720 | 2007 | 6 صفحه PDF | دانلود رایگان |

The microtubule motor cytoplasmic dynein and its activator dynactin drive vesicular transport and mitotic spindle organization. p150Glued 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 p150Glued and orchestrates its turnover via ubiquitination. FBXL5 binds to p150Gluedin vitro and in vivo. FBXL5 and p150Glued co-localize primarily in the cytoplasm with peri-nuclear enrichment in HeLa cells. Overexpression of FBXL5 promotes poly-ubiquitination of p150Glued and protein turnover of p150Glued. Our findings provide a potential mechanism by which p150Glued protein function is regulated by SCFs.
Journal: Biochemical and Biophysical Research Communications - Volume 359, Issue 1, 20 July 2007, Pages 34–39