The structure of the conserved neurotrophic factors MANF and CDNF explains why they are bifunctional

Protein Engineering, Design and Selection

Volumn 22, Issue 4, 2009, Pages 233-241

  Parkash, Vimal ^a   Lindholm, Päivi ^a   Peränen, Johan ^a   Kalkkinen, Nisse ^a   Oksanen, Esko ^a   Saarma, Mart ^a   Leppänen, Veli Matti ^a,b   Goldman, Adrian ^a,b  

^a UNIVERSITY OF HELSINKI   (Finland)

^b UNIVERSITY OF HELSINKI   (Finland)

Author keywords

ER stress; MANF and CDNF; Natively unfolded protein; Neurotrophic factor; Saposin

Indexed keywords

ER STRESS; MANF AND CDNF; NATIVELY UNFOLDED PROTEIN; NEUROTROPHIC FACTOR; SAPOSIN;

AMINO ACIDS; MAMMALS;

NEURONS;

ARGININE; CONSERVED DOPAMINE NEUROTROPHIC FACTOR; ISOMERASE; LIPID BINDING PROTEIN; LYSINE; MESENCEPHALIC ASTROCYTE DERIVED NEUROTROPHIC FACTOR; NEUROTROPHIC FACTOR; OXIDOREDUCTASE; SAPONIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CELL PROTECTION; CELL REGENERATION; CELL SURVIVAL; DISULFIDE BOND; DOPAMINERGIC NERVE CELL; ENDOPLASMIC RETICULUM STRESS; IN VIVO STUDY; MESENCEPHALON; NEUROPROTECTION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE;

CRYSTALLOGRAPHY, X-RAY; DISULFIDES; HUMANS; LIPID METABOLISM; NERVE GROWTH FACTORS; NERVE TISSUE PROTEINS; PROTEIN FOLDING; SAPOSINS; SEQUENCE ALIGNMENT; STRESS, PHYSIOLOGICAL;

MAMMALIA;

EID: 65349083373     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzn080     Document Type: Article

References (37)

1. Ahn,V.E., Faull,K.F., Whitelegge,J.P., Fluharty,A.L. and Privé,G.G. (2003) Proc. Natl Acad. Sci. USA, 100, 38-43.
2. Ahn,V.E., Leyko,P., Alattia,J.-R., Chen,L. and Privé,G.G. (2006) Protein Sci., 15, 1849-1857.
3. Airavaara,M., Shen,H., Kuo,C.C., Peränen,J., Saarma,M., Hoffer,B. and Wang,Y. (2009) J. Comp. Neurol. In press.
4. Anderson,D.H., Sawaya,M.R., Cascio,D., Ernst,W., Modlin,R., Krensky,A. and Eisenberg,D. (2003) J. Mol. Biol., 325, 355-365.
5. Apostolou,A., Shen,Y., Liang,Y., Luo,J. and Fang,S. (2008) Exp. Cell Res., 314, 2454-2467.
6. Bellizzi,J.J., Widom,J., Kemp,C.W. and Clardy,J. (1999) Structure, 7, R263-R267.
7. Bruhn,H. (2005) Biochem. J., 389, 249 -257.
8. Collaborative Computational Project, No. 4. (1994) Acta Crystallogr. D Biol. Crystallogr., 50, 760-763.
9. Collet,J.-F., D'souza,J.C., Jakob,U. and Bardwell,J.C. (2003) J. Biol. Chem.., 278, 45325-45332.
10. DeLano,W.L. (2002). The PyMOL Molecular Graphics System. DeLano Scientific, Palo Alto, CA, USA.
11. Emsley,P. and Cowtan,K. (2004) Acta Crystallogr. D Biol. Crystallogr., 60, 2126-2132.
12. Fraternali,F. and Cavallo,L. (2002) Nucleic Acids Res., 30, 2950-2960.
13. Holm,L. and Sander,C. (1993) J. Mol. Biol., 233, 123-138.
14. Horibe,T., Gomi,M., Iguchi,D., Ito,H., Kitamura,Y., Masuoka,T., Tsujimoto,I., Kimura,T. and Kikuchi,M. (2004) J. Biol. Chem., 279, 4604-4611.
15. Ibáñez,C.F. (1998) Trends Neurosci., 21, 438-444.
16. Kabsch,W. (1993) J. Appl. Cryst., 26, 795-800.
17. Keinänen,K., Jouppila,A. and Kuusinen,A. (1998) Biochem. J., 330, 1461 -1467.
18. Laskowski,R.A., MacArthur,M.W., Moss,D.S.M. and Thornton,J. (1993) J. Appl. Cryst., 26, 283-291.
19. Lee,A.-H., Iwakoshi,N.N. and Glimcher,L.H. (2003) Mol. Cell. Biol., 23, 7448 -7459.
20. Leppänen,V.-M., Bespalov,M.M., Runeberg-Roos,P., Puurand,U., Merits,A., Saarma,M. and Goldman,A. (2004) EMBO J., 23, 1452-1462.
21. Liepinsh,E., Andersson,M., Ruysschaert,J.-M. and Otting,G. (1997) Nat. Struct. Biol., 4, 793 -795.
22. Linde,C.M., Grundström,S., Nordling,E., Refai,E., Brennan,P.J. and Andersson,M. (2005) Infect. Immun., 73, 6332-6339.
23. Lindholm,P. et al. (2007) Nature, 448, 73 -77.
24. Lindholm,P., Peränen,J., Andressoo,J.-O., Kalkkinen,N., Kokaia,Z., Lindvall,O., Timmusk,T. and Saarma,M. (2008) Mol. Cell. Neurosci., 39, 356-371.
25. Linding,R., Jensen,L.J., Diella,F., Bork,P., Gibson,T.J. and Russell,R.B. (2003) Structure, 11, 1453 -1459.
26. Liu,A., Wenzel,N. and Qi,X. (2005) Arch. Biochem. Biophys., 443, 101 -112.
27. Marciniak,S.J. and Ron,D. (2006) Physiol. Rev., 86, 1133 -1149.
28. Mizobuchi,N., Hoseki,J., Kubota,H., Toyokuni,S., Nozaki,J., Naitoh,M., Koizumi,A. and Nagata,K. (2007) Cell Struct. Funct., 32, 41 -50.
29. Morris,R.J., Perrakis,A. and Lamzin,V.S. (2002) Acta Crystallogr. D Biol. Crystallogr., 58, 968-975.
30. Murshudov,G.N., Vagin,A.A. and Dodson,E.J. (1997) Acta Crystallogr. D Biol. Crystallogr., 53, 1022-1025.
31. Murzin,A.G., Brenner,S.E., Hubbard,T. and Chothia,C. (1995) J. Mol. Biol., 247, 536-540.
32. Palgi,M., Lindström,R., Peranen,J., Piepponen,T.P., Saarma,M. and Heino,T.I. (2009) Proc. Natl Acad. Sci. USA Published online January 22. doi:10.1073/pnas.0810996106.
33. Peränen,J., Rikkonen,M., Hyvönen,M. and Kääriä inen,L. (1996) Anal Biochem., 236, 371 -373.
34. Petrova,P. et al. (2003) J. Mol. Neurosci., 20, 173-188.
35. Qi,X. and Chu,Z. (2004) Arch. Biochem. Biophys., 424, 210-218.
36. Rossmann,M., Schultz-Heienbrok,R., Behlke,J., Remmel,N., Alings,C., Sandhoff,K., Saenger,W. and Maier,T. (2008) Structure, 16, 809-817. Schneider,T.R. and Sheldrick,G.M. (2002) Acta Crystallogr. D Biol. Crystallogr., 58, 1772-1779.
37. Shridhar,V., Rivard,S., Shridhar,R., Mullins,C., Bostick,L., Sakr,W., Grignon,D., Miller,O.J. and Smith,D.I. (1996) Oncogene, 12, 1931-1939.