The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol

Science

Volumn 336, Issue 6085, 2012, Pages 1168-1171

  Barrett, Paul J ^a   Song, Yuanli ^a   Van Horn, Wade D ^a   Hustedt, Eric J ^a   Schafer, Johanna M ^a   Hadziselimovic, Arina ^a   Beel, Andrew J ^a   Sanders, Charles R ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; CHOLESTEROL; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL;

AMINO ACID; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; MEMBRANE; NERVOUS SYSTEM DISORDER; NUCLEAR MAGNETIC RESONANCE; PROTEIN;

ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; MICELLE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN LIPID INTERACTION; PROTEIN MOTIF; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS;

EID: 84861675099     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1219988     Document Type: Article

References (33)

1. R. J. O'Brien, P. C. Wong, Annu. Rev. Neurosci. 34, 185 (2011).
2. C. Haass, D. J. Selkoe, Nat. Rev. Mol. Cell Biol. 8, 101 (2007).
3. A. C. Fonseca, R. Resende, C. R. Oliveira, C. M. Pereira, Exp. Neurol. 223, 282 (2010).
4. M. Simons et al., Proc. Natl. Acad. Sci. U.S.A. 95, 6460 (1998).
5. S. Wahrle et al., Neurobiol. Dis. 9, 11 (2002).
6. T. L. Kukar et al., J. Biol. Chem. 286, 39804 (2011).
7. M. Takami et al., J. Neurosci. 29, 13042 (2009).
8. J. X. Lu, W. M. Yau, R. Tycko, Biophys. J. 100, 711 (2011).
9. A. Botev et al., Biochemistry 50, 828 (2011).
10. K. D. Nadezhdin, O. V. Bocharova, E. V. Bocharov, A. S. Arseniev, Acta Naturae 2010, 69 (2011).
11. A. J. Beel et al., Biochemistry 47, 9428 (2008).
12. T. Sato et al., Proc. Natl. Acad. Sci. U.S.A. 106, 1421 (2009).
13. P. Kienlen-Campard et al., J. Biol. Chem. 283, 7733 (2008).
14. L. M. Munter et al., EMBO J. 26, 1702 (2007).
15. N. Miyashita, J. E. Straub, D. Thirumalai, J. Am. Chem. Soc. 131, 17843 (2009).
16. P. Osenkowski et al., J. Mol. Biol. 385, 642 (2009).
17. F. Renzi et al., J. Biol. Chem. 286, 21440 (2011).
18. S. Urban, Biochem. J. 425, 501 (2010).
19. M. S. Wolfe, Chem. Rev. 109, 1599 (2009).
20. J. Hardy, R. Crook, Alzheimer Research Forum, www.alzforum.org/res/com/ mut/app/ (2012).
21. G. van Meer, D. R. Voelker, G. W. Feigenson, Nat. Rev. Mol. Cell Biol. 9, 112 (2008).
22. R. M. Epand, Biochim. Biophys. Acta 1778, 1576 (2008).
23. M. A. Lemmon et al., J. Biol. Chem. 267, 7683 (1992).
24. K. R. MacKenzie, J. H. Prestegard, D. M. Engelman, Science 276, 131 (1997).
25. S. Kim et al., Proc. Natl. Acad. Sci. U.S.A. 102, 14278 (2005).
26. T. L. Kukar et al., Nature 453, 925 (2008).
27. S. A. Sagi et al., J. Biol. Chem. 286, 39794 (2011).
28. R. Ehehalt, P. Keller, C. Haass, C. Thiele, K. Simons, J. Cell Biol. 160, 113 (2003).
29. S. J. Lee et al., Nat. Med. 4, 730 (1998).
30. P. Osenkowski, W. Ye, R. Wang, M. S. Wolfe, D. J. Selkoe, J. Biol. Chem. 283, 22529 (2008).
31. S. Bodovitz, W. L. Klein, J. Biol. Chem. 271, 4436 (1996).
32. E. Kojro, G. Gimpl, S. Lammich, W. Marz, F. Fahrenholz, Proc. Natl. Acad. Sci. U.S.A. 98, 5815 (2001).
33. K. Yanagisawa, Subcell. Biochem. 38, 179 (2005).