Structure and membrane remodeling activity of ESCRT-III helical polymers

Science

Volumn 350, Issue 6267, 2015, Pages 1548-1551

  McCullough, John ^a   Clippinger, Amy K ^b   Talledge, Nathaniel ^a,c   Skowyra, Michael L ^b   Saunders, Marissa G ^a   Naismith, Teresa V ^b   Colf, Leremy A ^a   Afonine, Pavel ^d   Arthur, Christopher ^e   Sundquist, Wesley I ^a   Hanson, Phyllis I ^b   Frost, Adam ^a,c  

^a UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^e Thermo Fisher Scientific   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHARGED MULTIVESICULAR BODY PROTEIN 1B; ESCRT PROTEIN; INCREASED SODIUM TOLERANCE 1; PROTEIN; UNCLASSIFIED DRUG; BIOPOLYMER; CHMP1B PROTEIN, HUMAN; CHMP4A PROTEIN, HUMAN; OLC1 PROTEIN, HUMAN; ONCOPROTEIN;

MEMBRANE; MODELING; POLYMER; PROTEIN; TOLERANCE;

ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CONFORMATIONAL TRANSITION; ELECTRON MICROSCOPY; IN VITRO STUDY; IN VIVO STUDY; IONIC STRENGTH; LIPOSOME MEMBRANE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN POLYMERIZATION; PROTEIN STRUCTURE; CHEMISTRY; CRYOELECTRON MICROSCOPY; HUMAN; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; ULTRASTRUCTURE;

BIOPOLYMERS; CELL MEMBRANE; CRYOELECTRON MICROSCOPY; ENDOSOMAL SORTING COMPLEXES REQUIRED FOR TRANSPORT; HUMANS; ONCOGENE PROTEINS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84950271437     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aad8305     Document Type: Article

References (31)

1. J. H. Hurley, EMBO J. 34, 2398-2407 (2015).
2. P. I. Hanson, A. Cashikar, Annu. Rev. Cell Dev. Biol. 28, 337-362 (2012).
3. J. McCullough, L. A. Colf, W. I. Sundquist, Annu. Rev. Biochem. 82, 663-692 (2013).
4. M. Bajorek et al., Nat. Struct. Mol. Biol. 16, 754-762 (2009).
5. T. Muzioł et al., Dev. Cell 10, 821-830 (2006).
6. J. Xiao et al., Mol. Biol. Cell 20, 3514-3524 (2009).
7. Y. Lin, L. A. Kimpler, T. V. Naismith, J. M. Lauer, P. I. Hanson, J. Biol. Chem. 280, 12799-12809 (2005).
8. S. Lata et al., J. Mol. Biol. 378, 818-827 (2008).
9. W. M. Henne, N. J. Buchkovich, Y. Zhao, S. D. Emr, Cell 151, 356-371 (2012).
10. M. J. Dobro et al., Mol. Biol. Cell 24, 2319-2327 (2013).
11. G. Effantin et al., Cell. Microbiol. 15, 213-226 (2013).
12. S. Ghazi-Tabatabai et al., Structure 16, 1345-1356 (2008).
13. C. Moriscot et al., PLOS ONE 6, e21921 (2011).
14. Q.-T. Shen et al., J. Cell Biol. 206, 763-777 (2014).
15. S. Lata et al., Science 321, 1354-1357 (2008).
16. G. Bodon et al., J. Biol. Chem. 286, 40276-40286 (2011).
17. P. I. Hanson, R. Roth, Y. Lin, J. E. Heuser, J. Cell Biol. 180, 389-402 (2008).
18. A. G. Cashikar et al., eLife 3, e02184 (2014).
19. J. Guizetti et al., Science 331, 1616-1620 (2011).
20. A. Zamborlini et al., Proc. Natl. Acad. Sci. U.S.A. 103, 19140-19145 (2006).
21. S. Shim, L. A. Kimpler, P. I. Hanson, Traffic 8, 1068-1079 (2007).
22. N. J. Buchkovich, W. M. Henne, S. Tang, S. D. Emr, Dev. Cell 27, 201-214 (2013).
23. D. P. Nickerson, M. West, R. Henry, G. Odorizzi, Mol. Biol. Cell 21, 1023-1032 (2010).
24. C. Dimaano, C. B. Jones, A. Hanono, M. Curtiss, M. Babst, Mol. Biol. Cell 19, 465-474 (2008).
25. D. P. Nickerson, M. West, G. Odorizzi, J. Cell Biol. 175, 715-720 (2006).
26. S. M. Rue, S. Mattei, S. Saksena, S. D. Emr, Mol. Biol. Cell 19, 475-484 (2008).
27. E. Morita, FEBS J. 279, 1399-1406 (2012).
28. R. Allison et al., J. Cell Biol. 202, 527-543 (2013).
29. W. Stoorvogel, V. Oorschot, H. J. Geuze, J. Cell Biol. 132, 21-33 (1996).
30. Y. Kozlovsky, M. M. Kozlov, Biophys. J. 85, 85-96 (2003).
31. Materials and methods are available as supplementary materials on Science Online.