A charge-sensitive loop in the FKBP38 catalytic domain modulates Bcl-2 binding

Journal of Molecular Recognition

Volumn 24, Issue 1, 2011, Pages 23-34

  Maestre Martínez, Mitcheell ^a,c   Haupt, Katja ^a   Edlich, Frank ^a,d   Neumann, Piotr ^b,e   Parthier, Christoph ^b   Stubbs, Milton T ^b   Fischer, Gunter ^a   Lücke, Christian ^a  

^a MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

^b MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^c MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^d NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE   (United States)

^e UNIVERSITY OF GÖTTINGEN   (Germany)

Author keywords

apoptosis; Bcl 2; chemical shift perturbation; FK506 binding protein; NMR spectroscopy; paramagnetic relaxation enhancement; PPIase; pseudocontact shift; X ray crystallography

Indexed keywords

ASPARAGINE; CALCIUM; CATION; FK 506 BINDING PROTEIN; FKBP8 PROTEIN, HUMAN; MUTANT PROTEIN; PROTEIN BCL 2;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; STATIC ELECTRICITY;

AMINO ACID SEQUENCE; ASPARAGINE; BINDING SITES; CALCIUM; CATALYTIC DOMAIN; CATIONS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-BCL-2; SEQUENCE ALIGNMENT; STATIC ELECTRICITY; TACROLIMUS BINDING PROTEINS;

EID: 78049365922     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.1020     Document Type: Article

References (32)

1. Bai X, Ma D, Liu A, Shen X, Wang QJ, Liu Y, Jiang Y, 2007. Rheb activates mTOR by antagonizing its endogenous inhibitor, FKBP38. Science 318: 977-980.
2. Berridge MJ, Lipp P, Bootman MD, 2000. The versatility and universality of calcium signalling. Nat. Rev. Mol. Cell Biol. 1: 11-21.
3. Bertini I, Janik MB, Lee YM, Luchinat C, Rosato A, 2001. Magnetic susceptibility tensor anisotropies for a lanthanide ion series in a fixed protein matrix. J. Am. Chem. Soc. 123: 4181-4188.
4. Bertini I, Luchinat C, Parigi G, 2002. Magnetic susceptibility in paramagnetic NMR. Prog. Nucl. Magn. Reson. Spectrosc. 40: 249-273.
5. Bertini I, Gupta YK, Luchinat C, Parigi G, Peana M, Sgheri L, Yuan J, 2007. Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains. J. Am. Chem. Soc. 129: 12786-12794.
6. Cho A, Ko HW, Eggenschwiler JT, 2008. FKBP8 cell-autonomously controls neural tube patterning through a Gli2- and Kif3a-dependent mechanism. Dev. Biol. 321: 27-39.
7. Collaborative Computational Project, Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50: 760-763.
8. Deniaud A, Sharaf el dein O, Maillier E, Poncet D, Kroemer G, Lemaire C, Brenner C, 2008. Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis. Oncogene 27: 285-299.
9. 2+/calmodulin. EMBO J. 24: 2688-2699.
10. Edlich F, Weiwad M, Wildemann D, Jarczowski F, Kilka S, Moutty MC, Jahreis G, Lücke C, Schmidt W, Striggow F, Fischer G, 2006. The specific FKBP38 inhibitor N-(N′,N′-dimethylcarboxamidomethyl)cycloheximide has potent neuroprotective and neurotrophic properties in brain ischemia. J. Biol. Chem. 281: 14961-14970.
11. 2+ target recognition activates the Bcl-2 regulator FKBP38. J. Biol. Chem. 282: 36496-36504.
12. Eldridge AM, Kang H-S, Johnson E, Gunsalus R, Dahlquist FW, 2002. Effect of phosphorylation on the interdomain interaction of the response regulator, NarL. Biochemistry 41: 15173-15180.
13. Erdmann F, Jarczowski F, Weiwad M, Fischer G, Edlich F, 2007. Hsp90-mediated inhibition of FKBP38 regulates apoptosis in neuroblastoma cells. FEBS Lett. 581: 5709-5714.
14. Fanghänel J, Fischer G, 2004. Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases. Front Biosci. 9: 3453-3478.
15. Fischer S, Michnick S, Karplus M, 1993. A mechanism for rotamase catalysis by the FK506 binding protein (FKBP). Biochemistry 32: 13830-13837.
16. 2+ to glutamic acid-rich polypeptides from the rod outer segment. Biophys. J. 92: 3207-3214.
17. Ichas F, Mazat JP, 1998. From calcium signaling to cell death: two conformations for the mitochondrial permeability transition pore. Switching from low- to high-conductance state. Biochim. Biophys. Acta 1366: 33-50.
18. Kang CB, Hong Y, Dhe-Paganon S, Yoon HS, 2008. FKBP family proteins: immunophilins with versatile biological functions. Neurosignals 16: 318-325.
19. Lee S, Park HI, Sang Q-XA, 2007. Calcium regulates tertiary structure and enzymatic activity of human endometase/matrilysin-2 and its role in promoting human breast cancer cell invasion. Biochem. J. 403: 31-42.
20. Leslie AGW, 1994. MOSFLM Version 5.30 User Guide. Medical Research Council, Laboratory of Molecular Biology: Cambridge, UK.
21. Ma D, Bai X, Guo S, Jiang Y, 2008. The switch I region of Rheb is critical for its interaction with FKBP38. J. Biol. Chem. 283: 25963-25970.
22. Maestre-Martínez M, Edlich F, Jarczowski F, Weiwad M, Fischer G, Lücke C, 2006. Solution structure of the FKBP domain of human FKBP38. J. Biomol. NMR 34: 197-202.
23. Mulder FA, Schipper D, Bott R, Boelens R, 1999. Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins. J. Mol. Biol. 292: 111-123.
24. Okamoto T, Nishimura Y, Ichimura T, Suzuki K, Miyamura T, Suzuki T, Moriishi K, Matsuura Y, 2006. Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90. EMBO J. 25: 5015-5025.
25. Okamoto T, Omori H, Kaname Y, Abe T, Nishimura Y, Suzuki T, Miyamura T, Yoshimori T, Moriishi K, Matsuura Y, 2008. A single-amino-acid mutation in hepatitis C virus NS5A disrupting FKBP8 interaction impairs viral replication. J. Virol. 82: 3480-3489.
26. 2+ liaison. Sci. STKE 2004. 1-9 (re1).
27. Saris NE, Carafoli E, 2005. A historical review of cellular calcium handling, with emphasis on mitochondria. Biochemistry (Moscow) 70: 187-194. (Pubitemid 40512327)
28. 3- is a convenient paramagnetic shift reagent for protein NMR studies. J. Am. Chem. Soc. 131: 10352-10353.
29. Wang J, Tong W, Zhang X, Chen L, Yi Z, Pan T, Hu Y, Xiang L, Yuan Z, 2006. Hepatitis C virus non-structural protein NS5A interacts with FKBP38 and inhibits apoptosis in Huh7 hepatoma cells. FEBS Lett. 580: 4392-4400.
30. Wang X, Fonseca BD, Tang H, Liu R, Elia A, Clemens MJ, Bommer UA, Proud CG, 2008. Re-evaluating the roles of proposed modulators of mammalian target of rapamycin complex 1 (mTORC1) signaling. J. Biol. Chem. 283: 30482-30492.
31. 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR 6: 135-140.
32. Wong RL, Wlodarczyk BJ, Min KS, Scott ML, Kartiko S, Yu W, Merriweather MY, Vogel P, Zambrowicz BP, Finnell RH, 2008. Mouse Fkbp8 activity is required to inhibit cell death and establish dorso-ventral patterning in the posterior neural tube. Hum. Mol. Genet. 17: 587-601.