Crystal structure of a mycobacterial Insig homolog provides insight into how these sensors monitor sterol levels

Science

Volumn 349, Issue 6244, 2015, Pages 187-191

  Ren, Ruobing ^a,b,c   Zhou, Xinhui ^a,b,c   He, Yuan ^a,b,c   Ke, Meng ^a,b,c   Wu, Jianping ^a,b,c   Liu, Xiaohui ^d   Yan, Chuangye ^a,b,c   Wu, Yixuan ^a,b,c   Gong, Xin ^a,b,c   Lei, Xiaoguang ^d   Yan, S Frank ^e   Radhakrishnan, Arun ^f   Yan, Nieng ^a,b,c  

^a TSINGHUA UNIVERSITY   (China)

^b Tsinghua University   (China)

^c Tsinghua University   (China)

^d NATIONAL INSTITUTE OF BIOLOGICAL SCIENCES   (China)

^e Roche Innovation Center Shanghai   (China)

^f UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

25 HYDROXYCHOLESTEROL; BACTERIAL PROTEIN; BROMINE; DIACYLGLYCEROL; INSULIN INDUCED GENE 1 PROTEIN; INSULIN INDUCED GENE 2 PROTEIN; UNCLASSIFIED DRUG; 25-HYDROXYCHOLESTEROL; CHOLESTEROL DERIVATIVE; INSIG1 PROTEIN, HUMAN; INSIG2 PROTEIN, HUMAN; MEMBRANE PROTEIN; SIGNAL PEPTIDE; STEROL REGULATORY ELEMENT BINDING PROTEIN;

BACTERIUM; BIOCHEMICAL COMPOSITION; CHEMICAL BINDING; CRYSTAL STRUCTURE; CYTOLOGY; MOLECULAR ANALYSIS; PROTEIN; SENSOR; STEROL;

ARTICLE; BACTERIAL GENE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENDOPLASMIC RETICULUM MEMBRANE; HUMAN; HYDROGEN BOND; INSULIN INDUCED GENE; LIPID STORAGE; MYCOBACTERIUM; MYCOBACTERIUM VANBAALENII; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; SENSOR; SURFACE PROPERTY; CHEMISTRY; METABOLISM; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

MYCOBACTERIUM VANBAALENII;

BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DIGLYCERIDES; HUMANS; HYDROXYCHOLESTEROLS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MEMBRANE PROTEINS; MYCOBACTERIUM; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; STEROL REGULATORY ELEMENT BINDING PROTEINS;

EID: 84937558798     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aab1091     Document Type: Article

References (37)

1. M. S. Brown, J. L. Goldstein, Science 232, 34-47 (1986).
2. M. S. Brown, J. L. Goldstein, Cell 89, 331-340 (1997).
3. W. Shao, P. J. Espenshade, Cell Metab. 16, 414-419 (2012).
4. J. L. Goldstein, R. A. DeBose-Boyd, M. S. Brown, Cell 124, 35-46 (2006).
5. J. L. Goldstein, M. S. Brown, Cell 161, 161-172 (2015).
6. C. Yokoyama et al., Cell 75, 187-197 (1993).
7. X. Hua et al., . Proc. Natl. Acad. Sci. U.S.A. 90, 11603-11607 (1993).
8. X. Wang, R. Sato, M. S. Brown, X. Hua, J. L. Goldstein, Cell 77, 53-62 (1994).
9. X. Hua, A. Nohturfft, J. L. Goldstein, M. S. Brown, Cell 87, 415-426 (1996).
10. J. Sakai et al., J. Biol. Chem. 272, 20213-20221 (1997).
11. X. Gong et al., Cell Res. 25, 401-411 (2015).
12. A. Nohturfft, M. S. Brown, J. L. Goldstein, J. Biol. Chem. 273, 17243-17250 (1998).
13. T. Yang, J. L. Goldstein, M. S. Brown, J. Biol. Chem. 275, 29881-29886 (2000).
14. T. Yang et al., Cell 110, 489-500 (2002).
15. D. Yabe, M. S. Brown, J. L. Goldstein, Proc. Natl. Acad. Sci. U.S.A. 99, 12753-12758 (2002).
16. P. J. Espenshade, W. P. Li, D. Yabe, Proc. Natl. Acad. Sci. U.S.A. 99, 11694-11699 (2002).
17. L. P. Sun, L. Li, J. L. Goldstein, M. S. Brown, J. Biol. Chem. 280, 26483-26490 (2005).
18. J. Sakai et al., Mol. Cell 2, 505-514 (1998).
19. R. B. Rawson et al., Mol. Cell 1, 47-57 (1997).
20. R. B. Rawson, Nat. Rev. Mol. Cell Biol. 4, 631-640 (2003).
21. E. Ikonen, Nat. Rev. Mol. Cell Biol. 9, 125-138 (2008).
22. J. Sakai et al., Cell 85, 1037-1046 (1996).
23. M. S. Brown, J. L. Goldstein, Proc. Natl. Acad. Sci. U.S.A. 96, 11041-11048 (1999).
24. A. Radhakrishnan, Y. Ikeda, H. J. Kwon, M. S. Brown, J. L. Goldstein, Proc. Natl. Acad. Sci. U.S.A. 104, 6511-6518 (2007).
25. Y. Jo, R. A. Debose-Boyd, Crit. Rev. Biochem. Mol. Biol. 45, 185-198 (2010).
26. J. S. Burg et al., Cell Metab. 8, 522-531 (2008).
27. L. Feng et al., Science 318, 1608-1612 (2007).
28. J. D. Feramisco, J. L. Goldstein, M. S. Brown, J. Biol. Chem. 279, 8487-8496 (2004).
29. Molecular Operating Environment (MOE) (Chemical Computing Group, Montreal, Canada, 2013).
30. D. Deng et al., Nature 510, 121-125 (2014).
31. L. Sun et al., Nature 490, 361-366 (2012).
32. A. Penmatsa, K. H. Wang, E. Gouaux, Nature 503, 85-90 (2013).
33. A. Yamashita, S. K. Singh, T. Kawate, Y. Jin, E. Gouaux, Nature 437, 215-223 (2005).
34. A. L. Hughes, B. L. Todd, P. J. Espenshade, Cell 120, 831-842 (2005).
35. I. Flury et al., EMBO J. 24, 3917-3926 (2005).
36. T. F. Osborne, P. J. Espenshade, Genes Dev. 23, 2578-2591 (2009).
37. W. L. DeLano, The PyMOL Molecular Graphics System, www.pymol.org (2002).