Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55

Science

Volumn 322, Issue 5901, 2008, Pages 576-580

  Hyung, Ho Lee ^a   Elia, Natalie ^b   Ghirlando, Rodolfo ^a   Lippincott Schwartz, Jennifer ^b   Hurley, James H ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; DIMER; PROTEIN ALIX; PROTEIN CEP55; UNCLASSIFIED DRUG;

CRYSTAL STRUCTURE; CYTOLOGY; MACHINERY; MEMBRANE; PEPTIDE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYTOKINESIS; DAUGHTER CELL; ENDOSOME; GENETIC TRANSFECTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN LOCALIZATION;

AMINO ACID MOTIFS; CALCIUM-BINDING PROTEINS; CELL CYCLE PROTEINS; CELLULAR STRUCTURES; CRYSTALLOGRAPHY, X-RAY; CYTOKINESIS; DIMERIZATION; DNA-BINDING PROTEINS; ENDOSOMES; HELA CELLS; HUMANS; HYDROGEN BONDING; HYDROPHOBICITY; MODELS, BIOLOGICAL; MODELS, MOLECULAR; NUCLEAR PROTEINS; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN CONFORMATION; TRANSCRIPTION FACTORS; TRANSFECTION;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 54949088988     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1162042     Document Type: Article

References (30)

1. M. Glotzer, Science 307, 1735 (2005).
2. F. A. Barr, U. Gruneberg, Cell 131, 847 (2007).
3. R. Prekeris, G. W. Gould, J. Cell Sci. 121, 1569 (2008).
4. W. M. Zhao, A. Seki, G. W. Fang, Mol. Biol. Cell 17, 3881 (2006).
5. I. Martinez-Garay, A. Rustom, H. H. Gerdes, K. Kutsche, Genomics 87, 243 (2006).
6. M. Fabbro et al., Dev. Cell 9, 477 (2005).
7. T. Slagsvold, K. Pattni, L. Malerod, H. Stenmark, Trends Cell Biol. 16, 317 (2006).
8. R. L. Williams, S. Urbe, Nat. Rev. Mol. Cell Biol. 8, 355 (2007).
9. D. P. Nickerson, D. W. Russell, G. Odorizzi, EMBO Rep. 8, 644 (2007).
10. S. Saksena, J. Sun, T. Chu, S. D. Emr, Trends Biochem. Sci. 32, 561 (2007).
11. J. H. Hurley, Curr. Opin. Cell Biol. 20, 4 (2008).
12. J. G. Carlton, J. Martin-Serrano, Science 316, 1908 (2007); published online 6 June 2007 (10.1126/science.1143422).
13. E. Morita et al., EMBO J. 26, 4215 (2007).
14. J. G. Carlton, M. Agromayor, J. Martin-Serrano, Proc. Natl. Acad. Sci. U.S.A. 105, 10541 (2008).
15. P. I. Hanson, R. Roth, Y. Lin, J. E. Heuser, J. Cell Biol. 180, 389 (2008).
16. A. Lupas, M. Van Dyke, J. Stock, Science 252, 1162 (1991).
17. E. K. O'Shea, J. D. Klemm, P. S. Kim, T. Alber, Science 254, 539 (1991).
18. E. Morita, W. I. Sundquist, Annu. Rev. Cell Dev. Biol. 20, 395 (2004).
19. P. D. Bieniasz, Virology 344, 55 (2006).
20. K. Fujii, J. H. Hurley, E. O. Freed, Nat. Rev. Microbiol. 5, 912 (2007).
21. Single-letter abbreviations for amino acid residues: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; Y, Tyr; X, any amino acid.
22. O. Pornillos, S. L. Alam, D. R. Davis, W. I. Sundquist, Nat. Struct. Biol. 9, 812 (2002).
23. U. M. Munshi, J. Kim, K. Nagashima, J. H. Hurley, E. O. Freed, J. Biol. Chem. 282, 3847 (2007).
24. Q. Zhai et al., Nat. Struct. Mol. Biol. 15, 43 (2008).
25. M. S. Kostelansky et al., Cell 129, 485 (2007).
26. R. D. Fisher et al., Cell 128, 841 (2007).
27. J. Mccullough, R. D. Fisher, F. G. Whitby, W. I. Sundquist, C. P. Hill, Proc. Natl. Acad. Sci. U.S.A. 105, 7687 (2008).
28. E. Pineda-Molina et al., Traffic 7, 1007 (2006).
29. J. Kim et al., Dev. Cell 8, 937 (2005).
30. We thank B. Beach for generating DNA constructs, E. Freed and K. Kutsche for providing DNAs, T. Alber for discussions, and the staff of SER-CAT for user support at the Advanced Photon Source (APS). Use of the APS was supported by the U.S. Department of Energy, Basic Energy Sciences, Office of Science, under contract W-31-109-Eng-38. Supported by NIH intramural support, NIDDK (J.H.H.), NICHD (J.L.), and IATAP (J.H.H. and J.L.). Crystallographic coordinates have been deposited in the RCSB Protein Data Bank with accession number 3E1R.