ALS-causing P56S mutation and splicing variation on the hVAPB MSP domain transform its β-sandwich fold into lipid-interacting helical conformations

Biochemical and Biophysical Research Communications

Volumn 431, Issue 3, 2013, Pages 398-403

  Qin, Haina ^a   Wang, Wei ^a   Song, Jianxing ^a  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

Amyotrophic lateral sclerosis (ALS); Chameleon transformation; Dodecylphosphocholine (DPC); NMR spectroscopy; Protein aggregation; VAPB

Indexed keywords

CELLUBREVIN; MAJOR SPERM PROTEIN; MEMBRANE PROTEIN; PEPTIDES AND PROTEINS; PROTEIN P56S; UNCLASSIFIED DRUG; VESICLE ASSOCIATED MEMBRANE PROTEIN ASSOCIATED PROTEIN B;

AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; ENDOPLASMIC RETICULUM; GENE MUTATION; HUMAN; IN VITRO STUDY; IN VIVO STUDY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN LIPID INTERACTION; PROTEIN PROCESSING;

ALTERNATIVE SPLICING; AMYOTROPHIC LATERAL SCLEROSIS; CLONING, MOLECULAR; HUMANS; LIPIDS; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; VESICULAR TRANSPORT PROTEINS;

EID: 84873704015     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.01.039     Document Type: Article

References (29)

1. Bruijn L.I., Miller T.M., Cleveland D.W. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu. Rev. Neurosci. 2004, 27:723-749.
2. Pasinelli P., Brown R.H. Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat. Rev. Neurosci. 2006, 7:710-723.
3. Andersen P.M., Al-Chalabi A. Clinical genetics of amyotrophic lateral sclerosis: what do we really know?. Nat. Rev. Neurol. 2011, 7:603-615.
4. Nishimura A.L., Mitne-Neto M., Silva H.C., et al. A mutation in the vesicle trafficking protein VAPB causes late onset spinal muscular atrophy and amyotrophic lateral sclerosis. Am. J. Hum. Genet. 2004, 75:822-831.
5. Nishimura Y., Hayashi M., Inada H., et al. Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins. Biochem. Biophys. Res. Commun. 1999, 254:21-26.
6. Nachreiner T., Esser M., Tenten V., et al. Novel splice variants of the amyotrophic lateral sclerosis-associated gene VAPB expressed in human tissues. Biochem. Biophys. Res. Commun. 2010, 394:703-708.
7. Skehel P.A., Fabian-Fine R., Kandel E.R. Mouse VAP33 is associated with the endoplasmic reticulum and microtubules. Proc. Natl. Acad. Sci. USA 2000, 97:1101-1106.
8. Loewen C.J., Levine T.P. A highly conserved binding site in vesicle-associated membrane protein-associated protein (VAP) for the FFAT motif of lipid-binding proteins. J. Biol. Chem. 2005, 280:14097-14104.
9. Tsuda H., Han S.M., Yang Y., et al. The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors. Cell 2008, 133:963-977.
10. Lua S., Qin H., Lim L., et al. Structural, stability, dynamic and binding properties of the ALS-causing T46I mutant of the hVAPB MSP domain as revealed by NMR and MD simulations. PLoS One 2011, 6:e27072.
11. Pasquale E.B. Eph-Ephrin bidirectional signaling in physiology and disease. Cell 2008, 133:38-52.
12. Qin H., Shi J., Noberini R., et al. Crystal structure and NMR binding reveal that two small molecule antagonists target the high affinity Ephrin-binding channel of the EphA4 receptor. J. Biol. Chem. 2008, 283:29473-29484.
13. Han S.M., Tsuda H., Yang Y., et al. Secreted VAPB/ALS8 major sperm protein domains modulate mitochondrial localization and morphology via growth cone guidance receptors. Dev. Cell 2012, 22:348-362.
14. Gupta G., Qin H., Song J. Intrinsically unstructured domain 3 of hepatitis C virus NS5A forms a " fuzzy complex" with VAPB-MSP domain which carries ALS-causing mutations. PLoS One 2012, 7:e39261.
15. Chen H.J., Anagnostou G., Chai A., et al. Characterization of the properties of a novel mutation in VAPB in familial amyotrophic lateral sclerosis. J. Biol. Chem. 2010, 285:40266-40281.
16. Teuling E., Ahmed S., Haasdijk E., et al. Motor neuron disease-associated mutant vesicle-associated membrane protein- associated protein (VAP) B recruits wild-type VAPs into endoplasmic reticulum-derived tubular aggregates. J. Neurosci. 2007, 27:9801-9815.
17. Kanekura K., Suzuki H., Aiso S., et al. ER stress and unfolded protein response in amyotrophic lateral sclerosis. Mol. Neurobiol. 2009, 39:81-89.
18. Shi J., Lua S., Tong J.S., et al. Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis. Biochemistry 2010, 49:3887-3897.
19. Mitne-Neto M., Machado-Costa M., Marchetto M.C.N., et al. Downregulation of VAPB expression in motor neurons derived from induced pluripotent stem cells of ALS8 patients. Hum. Mol. Genet. 2011, 20:3642-3652.
20. Papiani G., Ruggiano A., Fossati M., et al. Restructured endoplasmic reticulum generated by mutant amyotrophic lateral sclerosis-linked VAPB is cleared by the proteasome. J. Cell Sci. 2012, 125:3601-3611.
21. Pace C.N., Vajdos F., Fee L., et al. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 1995, 4:2411-2423.
22. Sreerama N., Woody R.W. Estimation of protein secondary structure from CD spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal. Biochem. 2000, 282:252-260.
23. Song J. Insight into " insoluble proteins" with pure water. FEBS Lett. 2009, 583:953-959.
24. Delak K., Harcup C., Lakshminarayanan R., et al. The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form. Biochemistry 2009, 48:2272-2281.
25. Dyson H.J., Wright P.E. Unfolded proteins and protein folding studied by NMR. Chem. Rev. 2004, 104:3607-3622.
26. Bai Y., Chung J., Dyson H.J., Wright P.E. Structural and dynamic characterization of an unfolded state of poplar apo plastocyanin formed under nondenaturing conditions. Protein Sci. 2001, 10:1056-1066.
27. Liu J., Song J. NMR evidence for forming highly populated helical conformations in the partially folded hNck2 SH3 domain. Biophys. J. 2008, 95:4803-4812.
28. Nanga R.P., Brender J.R., Xu J., et al. Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. J. Am. Chem. Soc. 2009, 131:8252-8261.
29. Elfrink K., Ollesch J., Stöhr J., et al. Structural changes of membrane-anchored native PrP(C). Proc. Natl. Acad. Sci. USA 2008, 105:10815-10819.