The Dsl1 Tethering Complex Actively Participates in Soluble NSF (N-Ethylmaleimide-sensitive Factor) Attachment Protein Receptor (SNARE) Complex Assembly at the Endoplasmic Reticulum inSaccharomyces cerevisiae
作者： Melanie Diefenbacher , Holmfridur Thorsteinsdottir , Anne Spang
关键词: Mutant protein 、 Vesicle tethering 、 Golgi apparatus 、 Coatomer 、 Vesicle fusion 、 SNARE complex assembly 、 Biology 、 Cell biology 、 Endoplasmic reticulum 、 SNARE complex 、 Biochemistry 、 Molecular biology
摘要: Intracellular transport is largely dependent on vesicles that bud off from one compartment and fuse with the target compartment. The first contact of an incoming vesicle membrane mediated by tethering factors. factor responsible for recruiting Golgi-derived to ER Dsl1 complex, which comprised essential proteins Dsl1p, Dsl3p, Tip20p. We investigated role Tip20p subunit at analyzing two mutants, tip20-5 tip20-8. Both mutants contained multiple mutations were scattered throughout TIP20 sequence. Individual could not reproduce temperature-sensitive phenotype tip20-8, indicating overall structure might be altered in mutants. Using molecular dynamics simulations comparing Tip20-8p revealed some regions, particularly N-terminal domain parts stalk region, more flexible mutant protein, consistent its increased susceptibility proteolysis. Tip20-5p prevented proper trans-SNARE complex assembly vitro. Moreover, disturbed interaction between Dsl1p coatomer coat Dsl1p-coatomer stabilized or regulated provide evidence a direct particular Tip20p, formation stabilization SNARE complexes.
highwire.org参考文章(65)
Fred Sherman, Getting started with yeast. Methods in Enzymology. ,vol. 350, pp. 3- 41 ,(2002) , 10.1016/S0076-6879(02)50954-X
Bruno Antonny, David Madden, Susan Hamamoto, Lelio Orci, Randy Schekman, Dynamics of the COPII coat with GTP and stable analogues Nature Cell Biology. ,vol. 3, pp. 531- 537 ,(2001) , 10.1038/35078500
Francesco Parlati, James A. McNew, Ryouichi Fukuda, Rebecca Miller, Thomas H. Söllner, James E. Rothman, Topological restriction of SNARE-dependent membrane fusion Nature. ,vol. 407, pp. 194- 198 ,(2000) , 10.1038/35025076
Axel T. Brunger, Klaus M. Fiebig, Luke M. Rice, Elizabeth Pollock, Folding intermediates of SNARE complex assembly. Nature Structural & Molecular Biology. ,vol. 6, pp. 117- 123 ,(1999) , 10.1038/5803
R. Bryan Sutton, Dirk Fasshauer, Reinhard Jahn, Axel T. Brunger, Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution Nature. ,vol. 395, pp. 347- 353 ,(1998) , 10.1038/26412
D.J. Sweet, H.R. Pelham, The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic protein that interacts with the cytoplasmic domain of Sec20p. The EMBO Journal. ,vol. 12, pp. 2831- 2840 ,(1993) , 10.1002/J.1460-2075.1993.TB05944.X
Juan S Bonifacino, Benjamin S Glick, The Mechanisms of Vesicle Budding and Fusion Cell. ,vol. 116, pp. 153- 166 ,(2004) , 10.1016/S0092-8674(03)01079-1
Jia-Shu Yang, Stella Y. Lee, Minggeng Gao, Sylvain Bourgoin, Paul A. Randazzo, Richard T. Premont, Victor W. Hsu, ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat Journal of Cell Biology. ,vol. 159, pp. 69- 78 ,(2002) , 10.1083/JCB.200206015
Luis Galiano, Fangyu Ding, Angelo M. Veloro, Mandy E. Blackburn, Carlos Simmerling, Gail E. Fanucci, Drug pressure selected mutations in HIV-1 protease alter flap conformations. Journal of the American Chemical Society. ,vol. 131, pp. 430- 431 ,(2009) , 10.1021/JA807531V
Bin Yang, Lino Gonzalez, Rytis Prekeris, Martin Steegmaier, Raj J. Advani, Richard H. Scheller, SNARE Interactions Are Not Selective: IMPLICATIONS FOR MEMBRANE FUSION SPECIFICITY Journal of Biological Chemistry. ,vol. 274, pp. 5649- 5653 ,(1999) , 10.1074/JBC.274.9.5649