FBXL5 interacts with p150 {sup Glued} and regulates its ubiquitination
- Division of Cellular Dynamics, Hefei National Laboratory for Physical Sciences and Chinese University of Science and Technology, Hefei 230027 (China)
- Cancer Biology Program, Morehouse School of Medicine, Atlanta, GA 30310 (United States)
- Division of Cellular Dynamics, Hefei National Laboratory for Physical Sciences and Chinese University of Science and Technology, Hefei 230027 (China) and Cancer Biology Program, Morehouse School of Medicine, Atlanta, GA 30310 (United States)
The microtubule motor cytoplasmic dynein and its activator dynactin drive vesicular transport and mitotic spindle organization. p150 {sup 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 {sup Glued} and orchestrates its turnover via ubiquitination. FBXL5 binds to p150 {sup Glued} in vitro and in vivo. FBXL5 and p150 {sup Glued} co-localize primarily in the cytoplasm with peri-nuclear enrichment in HeLa cells. Overexpression of FBXL5 promotes poly-ubiquitination of p150 {sup Glued} and protein turnover of p150 {sup Glued} . Our findings provide a potential mechanism by which p150 {sup Glued} protein function is regulated by SCFs.
- OSTI ID:
- 20991444
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 359, Issue 1; Other Information: DOI: 10.1016/j.bbrc.2007.05.068; PII: S0006-291X(07)00988-6; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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