Pri sORF peptides induce selective proteasome-mediated protein processing

Science

Volumn 349, Issue 6254, 2015, Pages 1356-1358

  Zanet, J ^a,b   Benrabah, E ^a,b   Li, T ^c   Pelissier Monier A ^a,b   Chanut Delalande, H ^a,b   Ronsin, B ^a,b   Bellen, H J ^c   Payre, F ^a,b   Plaza, S ^a,b  

^a UNIVERSITÉ PAUL SABATIER   (France)

^b CNRS   (France)

^c BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DROSOPHILA PROTEIN; PEPTIDE; PRI PROTEIN; PROTEASOME; RNA; UBIQUITIN CONJUGATING ENZYME E2; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; OVO PROTEIN, DROSOPHILA; TRANSCRIPTION FACTOR; UBCD6 PROTEIN, DROSOPHILA; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE; UBR3 PROTEIN, DROSOPHILA;

ENZYME ACTIVITY; GENOME; PEPTIDE; PROTEIN; RICE; RNA;

ARTICLE; CARBOXY TERMINAL SEQUENCE; DROSOPHILA; NONHUMAN; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN INTERACTION; PROTEIN PROCESSING; RNA INTERFERENCE; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; DROSOPHILA MELANOGASTER; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; UBIQUITINATION;

AMINO ACID SEQUENCE; ANIMALS; DNA-BINDING PROTEINS; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; GENE EXPRESSION REGULATION; MOLECULAR SEQUENCE DATA; OPEN READING FRAMES; PEPTIDES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN STRUCTURE, TERTIARY; PROTEOLYSIS; RNA INTERFERENCE; TRANSCRIPTION FACTORS; UBIQUITIN-CONJUGATING ENZYMES; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION;

EID: 84942903178     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aac5677     Document Type: Article

References (30)

1. J. E. Smith et al., Cell Reports 7, 1858-1866 (2014).
2. K. Hanada et al., Proc. Natl. Acad. Sci. U. S. A. 110, 2395-2400 (2013).
3. D. Lauressergues et al., Nature 520, 90-93 (2015).
4. N. T. Ingolia et al., Cell Reports 8, 1365-1379 (2014).
5. J. Ma et al., J. Proteome Res. 13, 1757-1765 (2014).
6. J. Savard, H. Marques-Souza, M. Aranda, D. Tautz, Cell 126, 559-569 (2006).
7. T. Kondo et al., Nat. Cell Biol. 9, 660-665 (2007).
8. M. I. Galindo, J. I. Pueyo, S. Fouix, S. A. Bishop, J. P. Couso, PLOS Biol. 5, e106 (2007).
9. F. Payre, A. Vincent, S. Carreno, Nature 400, 271-275 (1999).
10. D. L. Stern, N. Frankel, Philos. Trans. R. Soc. London B Biol. Sci. 368, 20130028 (2013).
11. J. Crocker et al., Cell 160, 191-203 (2015).
12. T. Kondo et al., Science 329, 336-339 (2010).
13. D. Menoret et al., Genome Biol. 14, R86 (2013).
14. H. Chanut-Delalande et al., Nat. Cell Biol. 16, 1035-1044 (2014).
15. A. Vinayagam et al., Sci. Signal. 6, rs5 (2013).
16. S. Fishbain et al., Nat. Struct. Mol. Biol. 22, 214-221 (2015).
17. S. Prakash, L. Tian, K. S. Ratliff, R. E. Lehotzky, A. Matouschek, Nat. Struct. Mol. Biol. 11, 830-837 (2004).
18. L. Tian, R. A. Holmgren, A. Matouschek, Nat. Struct. Mol. Biol. 12, 1045-1053 (2005).
19. A. Varshavsky, Annu. Rev. Biochem. 81, 167-176 (2012).
20. T. Tasaki et al., J. Biol. Chem. 282, 18510-18520 (2007).
21. C. Meisenberg et al., Nucleic Acids Res. 40, 701-711 (2012).
22. M. Ditzel et al., Mol. Cell 32, 540-553 (2008).
23. Q. Huang et al., Cell Death Differ. 21, 1961-1970 (2014).
24. S. Yamamoto et al., Cell 159, 200-214 (2014).
25. G. C. Turner, F. Du, A. Varshavsky, Nature 405, 579-583 (2000).
26. E. G. Magny et al., Science 341, 1116-1120 (2013).
27. D. M. Anderson et al., Cell 160, 595-606 (2015).
28. A. Pauli et al., Science 343, 1248636 (2014).
29. S. A. Slavoff, J. Heo, B. A. Budnik, L. A. Hanakahi, A. Saghatelian, J. Biol. Chem. 289, 10950-10957 (2014).
30. A. Patgiri, K. K. Yadav, P. S. Arora, D. Bar-Sagi, Nat. Chem. Biol. 7, 585-587 (2011).