Escherichia coli expression, refolding and characterization of human laforin

Protein Expression and Purification

Volumn 71, Issue 2, 2010, Pages 195-199

  Castanheira, Pedro ^a   Moreira, Susana ^b   Gama, Miguel ^b   Faro, Carlos ^a,c  

^a Bioinformatics Unit   (Portugal)

^b UNIVERSITY OF MINHO   (Portugal)

^c UNIVERSITY OF COIMBRA   (Portugal)

Author keywords

Carbohydrate binding module; Dual specificity phosphatase; Inclusion bodies; Lafora disease; Laforin; Refolding

Indexed keywords

DUAL SPECIFICITY PHOSPHATASE; PROTEIN;

ARTICLE; CELL INCLUSION; ESCHERICHIA COLI; GENETICS; HUMAN; METABOLISM; MUTATION; MYOCLONUS EPILEPSY;

DUAL-SPECIFICITY PHOSPHATASES; ESCHERICHIA COLI; HUMANS; INCLUSION BODIES; LAFORA DISEASE; MUTATION; PROTEINS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 77949659387     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.02.004     Document Type: Article

References (23)

1. Ganesh S., Agarwala K.L., Ueda K., Akagi T., Shoda K., Usui T., Hashikawa T., Osada H., Delgado-Escueta A.V., and Yamakawa K. Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes. Hum. Mol. Genet. 9 (2000) 2251-2261
2. Wang J., Stuckey J.A., Wishart M.J., and Dixon J.E. A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen. J. Biol. Chem. 277 (2002) 2377-2380
3. Chan E.M., Andrade D.M., Franceschetti S., and Minassian B. Progressive myoclonus epilepsies: EPM1, EPM2A, EPM2B. Adv. Neurol. 95 (2005) 47-57
4. Minassian B.A., Lee J.R., Herbrick J.A., Huizenga J., Soder S., Mungall A.J., Dunham I., Gardner R., Fong C.Y., Carpenter S., Jardim L., Satishchandra P., Andermann E., Snead III O.C., Lopes-Cendes I., Tsui L.C., Delgado-Escueta A.V., Rouleau G.A., and Scherer S.W. Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy. Nat. Genet. 20 (1998) 171-174
5. Minassian B.A. Lafora's disease: towards a clinical, pathologic, and molecular synthesis. Pediatr. Neurol. 25 (2001) 21-29
6. Lafora G.R., and Glueck B. Article on the histopathology of myoclonic epilepsy. Z. Gesamte Neurol. Psychiatrie 6 (1911) 1-14
7. Tagliabracci V.S., Turnbull J., Wang W., Girard J.M., Zhao X., Skurat A.V., Delgado-Escueta A.V., Minassian B.A., Depaoli-Roach A.A., and Roach P.J. Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo. Proc. Natl. Acad. Sci. USA 104 (2007) 19262-19266
8. Fernandez-Sanchez M.E., Criado-Garcia O., Heath K.E., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa J.M., and Rodriguez de C.S. Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. Hum. Mol. Genet. 12 (2003) 3161-3171
9. Worby C.A., Gentry M.S., and Dixon J.E. Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG). J. Biol. Chem. 283 (2008) 4069-4076
10. Lohi H., Ianzano L., Zhao X.C., Chan E.M., Turnbull J., Scherer S.W., Ackerley C.A., and Minassian B.A. Novel glycogen synthase kinase 3 and ubiquitination pathways in progressive myoclonus epilepsy. Hum. Mol. Genet. 14 (2005) 2727-2736
11. Gentry M.S., Worby C.A., and Dixon J.E. Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin. Proc. Natl. Acad. Sci. USA 102 (2005) 8501-8506
12. Vilchez D., Ros S., Cifuentes D., Pujadas L., Valles J., Garcia-Fojeda B., Criado-Garcia O., Fernandez-Sanchez E., Medrano-Fernandez I., Dominguez J., Garcia-Rocha M., Soriano E., Rodriguez de C.S., and Guinovart J.J. Mechanism suppressing glycogen synthesis in neurons and its demise in progressive myoclonus epilepsy. Nat. Neurosci. 10 (2007) 1407-1413
13. Hsu S., Kim Y., Li S., Durrant E.S., Pace R.M., Woods V.L., and Gentry M.S. Structural insights into glucan phosphatase dynamics using amide hydrogen-deuterium exchange mass spectrometry. Biochemistry (2009)
14. Gentry M.S., and Pace R.M. Conservation of the glucan phosphatase laforin is linked to rates of molecular evolution and the glucan metabolism of the organism. BMC Evol. Biol. 9 (2009) 138
15. Liu Y., Wang Y., Wu C., Liu Y., and Zheng P. Dimerization of laforin is required for its optimal phosphatase activity, regulation of GSK3beta phosphorylation, and Wnt signaling. J. Biol. Chem. 281 (2006) 34768-34774
16. Girard J.M., Le K.H., and Lederer F. Molecular characterization of laforin, a dual-specificity protein phosphatase implicated in Lafora disease. Biochimie 88 (2006) 1961-1971
17. Wang W., and Roach P.J. Glycogen and related polysaccharides inhibit the laforin dual-specificity protein phosphatase. Biochem. Biophys. Res. Commun. 325 (2004) 726-730
18. Chan E.M., Ackerley C.A., Lohi H., Ianzano L., Cortez M.A., Shannon P., Scherer S.W., and Minassian B.A. Laforin preferentially binds the neurotoxic starch-like polyglucosans, which form in its absence in progressive myoclonus epilepsy. Hum. Mol. Genet. 13 (2004) 1117-1129
19. Castanheira P., Samyn B., Sergeant K., Clemente J.C., Dunn B.M., Pires E., Van B.J., and Faro C. Activation, proteolytic processing, and peptide specificity of recombinant cardosin A. J. Biol. Chem. 280 (2005) 13047-13054
20. Fahnert B., Lilie H., and Neubauer P. Inclusion bodies: formation and utilisation. Adv. Biochem. Eng. Biotechnol. 89 (2004) 93-142
21. Montalibet J., Skorey K.I., and Kennedy B.P. Protein tyrosine phosphatase: enzymatic assays. Methods 35 (2005) 2-8
22. Gottlin E.B., Xu X., Epstein D.M., Burke S.P., Eckstein J.W., Ballou D.P., and Dixon J.E. Kinetic analysis of the catalytic domain of human cdc25B. J. Biol. Chem. 271 (1996) 27445-27449
23. Peters G.H., Branner S., Moller K.B., Andersen J.N., and Moller N.P. Enzyme kinetic characterization of protein tyrosine phosphatases. Biochimie 85 (2003) 527-534