Mechanism and dynamics of INPP5E transport into and inside the ciliary compartment.
作者： Stefanie Kristine Kösling , Eyad Kalawy Fansa , Stefano Maffini , Alfred Wittinghofer
关键词: Wild type 、 Intraflagellar transport 、 Cell biology 、 Photobleaching 、 Cilium 、 Fluorescence microscope 、 Fluorescence recovery after photobleaching 、 Centriole 、 Chemistry 、 Dynein
摘要: The inositol polyphosphate 5'-phosphatase E (INPP5E) localizes to cilia. We showed that the carrier protein phosphodiesterase 6 delta subunit (PDE6δ) mediates sorting of farnesylated INPP5E into cilia due high affinity binding and release by ADP-ribosylation factor (Arf)-like Arl3·GTP. However, dynamics transport inside ciliary compartment are not fully understood. Here, we investigate movement using live cell fluorescence microscopy recovery after photobleaching (FRAP) analysis. show PDE6δ dynein system essential for entry INPP5E. its innerciliary is regulated solely intraflagellar (IFT) system, independent from activity farnesylation. By contrast, Arl3 within occurs freely diffusion IFT-independently. farnesylation defective CaaX box mutant loses exclusive localization. accumulation this at centrioles suggests an trap mechanism entry, in case wild type overcome interaction with PDE6δ. Collectively, postulate a three-step regulating localization INPP5E, consisting farnesylation- PDE6δ-mediated targeting, INPP5E-PDE6δ complex cilium transfer IFT retention
mpg.de
sci-hub.se 参考文章(93)
Guangshuo Ou, Oliver E. Blacque, Joshua J. Snow, Michel R. Leroux, Jonathan M. Scholey, Functional coordination of intraflagellar transport motors Nature. ,vol. 436, pp. 583- 587 ,(2005) , 10.1038/NATURE03818
Malte Schmick, Nachiket Vartak, Björn Papke, Marija Kovacevic, Dina C. Truxius, Lisaweta Rossmannek, Philippe I.H. Bastiaens, KRas Localizes to the Plasma Membrane by Spatial Cycles of Solubilization, Trapping and Vesicular Transport Cell. ,vol. 157, pp. 459- 471 ,(2014) , 10.1016/J.CELL.2014.02.051
Robert A. Bloodgood, Preferential turnover of membrane proteins in the intact Chlamydomonas flagellum. Experimental Cell Research. ,vol. 150, pp. 488- 493 ,(1984) , 10.1016/0014-4827(84)90594-9
Hillary Van Valkenburgh, Jack F. Shern, J. Daniel Sharer, Xinjun Zhu, Richard A. Kahn, ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins. Journal of Biological Chemistry. ,vol. 276, pp. 22826- 22837 ,(2001) , 10.1074/JBC.M102359200
Florence De Smedt, Alain Boom, Xavier Pesesse, Serge N. Schiffmann, Christophe Erneux, Post-translational Modification of Human Brain Type I Inositol-1,4,5-trisphosphate 5-Phosphatase by Farnesylation Journal of Biological Chemistry. ,vol. 271, pp. 10419- 10424 ,(1996) , 10.1074/JBC.271.17.10419
Monique Jacoby, James J Cox, Stéphanie Gayral, Daniel J Hampshire, Mohammed Ayub, Marianne Blockmans, Eileen Pernot, Marina V Kisseleva, Philippe Compere, Serge N Schiffmann, Fanni Gergely, John H Riley, David Perez-Morga, C Geoffrey Woods, Stéphane Schurmans, INPP5E mutations cause primary cilium signaling defects, ciliary instability and ciliopathies in human and mouse Nature Genetics. ,vol. 41, pp. 1027- 1031 ,(2009) , 10.1038/NG.427
Malte Schmick, Astrid Kraemer, Philippe I.H. Bastiaens, Ras moves to stay in place Trends in Cell Biology. ,vol. 25, pp. 190- 197 ,(2015) , 10.1016/J.TCB.2015.02.004
Tomer Avidor-Reiss, Andreia M Maer, Edmund Koundakjian, Andrey Polyanovsky, Thomas Keil, Shankar Subramaniam, Charles S Zuker, Decoding Cilia Function: Defining Specialized Genes Required for Compartmentalized Cilia Biogenesis Cell. ,vol. 117, pp. 527- 539 ,(2004) , 10.1016/S0092-8674(04)00412-X
Ari J. Firestone, Joshua S. Weinger, Maria Maldonado, Kari Barlan, Lance D. Langston, Michael O’Donnell, Vladimir I. Gelfand, Tarun M. Kapoor, James K. Chen, Small-molecule inhibitors of the AAA+ ATPase motor cytoplasmic dynein Nature. ,vol. 484, pp. 125- 129 ,(2012) , 10.1038/NATURE10936
Stephanie K. Florio, Rabi K. Prusti, Joseph A. Beavo, Solubilization of Membrane-bound Rod Phosphodiesterase by the Rod Phosphodiesterase Recombinant δ Subunit Journal of Biological Chemistry. ,vol. 271, pp. 24036- 24047 ,(1996) , 10.1074/JBC.271.39.24036