Laforin preferentially binds the neurotoxic starch-like polyglucosans, which form in its absence in progressive myoclonus epilepsy

Human Molecular Genetics

Volumn 13, Issue 11, 2004, Pages 1117-1129

  Chan, Elayne M ^a   Ackerley, Cameron A ^b   Lohi, Hannes ^a   Ianzano, Leonarda ^a   Cortez, Miguel A ^b   Shannon, Patrick ^a   Scherer, Stephen W ^a   Minassian, Berge A ^a,b  

^a UNIVERSITY OF TORONTO   (Canada)

^b HOSPITAL FOR SICK CHILDREN   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; GLYCOGEN; LAFORIN; NEUROTOXIN; PHOSPHATASE; PROTEIN EPM2AIP1; STARCH; STARCH LIKE POLYGLUCOSAN; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; BIOACCUMULATION; BIOPSY TECHNIQUE; CELL COMPARTMENTALIZATION; CONTROLLED STUDY; DENDRITE; DISEASE ASSOCIATION; ENDOPLASMIC RETICULUM; ENZYME BINDING; ENZYME INACTIVATION; ENZYME LOCALIZATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GENE OVEREXPRESSION; HUMAN; HUMAN TISSUE; IMMUNOGOLD ELECTRON MICROSCOPY; IN VITRO STUDY; IN VIVO STUDY; LIVER; MONITORING; MOUSE; MUSCLE; MYOCLONUS EPILEPSY; NERVE CELL; NERVE FIBER; NONHUMAN; PATHOGENESIS; PERIKARYON; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN LOCALIZATION; TRANSGENIC MOUSE;

ACTINS; ANIMALS; BRAIN; ENDOPLASMIC RETICULUM; GENE TRANSFER TECHNIQUES; GLUCANS; GLYCOGEN; HUMANS; IMMUNOCHEMISTRY; INCLUSION BODIES; LAFORA DISEASE; LIVER; MICE; MICE, TRANSGENIC; PROMOTER REGIONS (GENETICS); PROTEIN BINDING; PROTEIN-TYROSINE-PHOSPHATASE; PROTO-ONCOGENE PROTEINS C-MYC; STARCH;

MUS MUSCULUS;

EID: 2942737274     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/ddh130     Document Type: Article

References (35)

1. Lafora, G.R. and Gluck, B. (1911) Beitrag zur histopathologie der myoklonischen epilepsie. Z. Ges. Neurol. Psychiat., 6, 1-14.
2. Minassian, B.A. (2002) Progressive myoclonus epilepsy with polyglucosan bodies: Lafora disease. Adv. Neurol., 89, 199-210.
3. Sakai, M., Austin, J., Witmer, F. and Trueb, L. (1970) Studies in myoclonus epilepsy (Lafora body form). II. Polyglucosans in the systemic deposits of myoclonus epilepsy and in corpora amylacea. Neurology, 20, 160-176.
4. Gambetti, P., Di Mauro, S., Hirt, L. and Blume, R.P. (1971) Myoclonic epilepsy with Lafora bodies. Some ultrastructural, histochemical, and biochemical aspects. Arch. Neurol., 25, 483-493.
5. Cavanagh, J.B. (1999) Corpora-amylacea and the family of polyglucosan diseases. Brain Res. Brain Res. Rev., 29, 265-295.
6. Van Heycop ten Ham, M. (1974) Lafora disease, a form of progressive myoclonus epilepsy. Handbook of Clinical Neurology, 15, 382-422.
7. Collins, G.H., Cowden, R.R. and Nevis, A.H. (1968) Myoclonus epilepsy with Lafora bodies. An ultrastructural and cytochemical study. Arch. Pathol., 86, 239-254.
8. Toga, M., Dubois, D. and Hassoun, J. (1968) Ultrastructure of Lafora bodies. Acta Neuropathol. (Berl.), 10, 132-142.
9. 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. et al. (1998) Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy. Nat. Genet., 20, 171-174.
10. Ganesh, S., Agarwala, K.L., Ueda, K., Akagi, T., Shoda, K., Usui, T., Hashikawa, T., Osada, H., Delgado-Escueta, A.V. and Yamakawa, K. (2000) Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes. Hum. Mol. Genet., 9, 2251-2261.
11. Minassian, B.A., Andrade, D.M., Ianzano, L., Young, E.J., Chan, E., Ackerley, C.A. and Scherer, S.W. (2001) Laforin is a cell membrane and endoplasmic reticulum-associated protein tyrosine phosphatase. Ann. Neurol., 49, 271-275.
12. Chan, E.M., Young, E.J., Ianzano, L., Munteanu, I., Zhao, X., Christopoulos, C.C., Avanzini, G., Elia, M., Ackerley, C.A., Jovic, N.J. et al. (2003) Mutations in NHLRC1 cause progressive myoclonus epilepsy. Nat. Genet., 35, 125-127.
13. Ganesh, S., Delgado-Escueta, A.V., Sakamoto, T., Avila, M.R., Machado-Salas, J., Hoshii, Y., Akagi, T., Gomi, H., Suzuki, T., Amano, K. et al. (2002) Targeted disruption of the Epm2a gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice. Hum. Mol. Genet., 11, 1251-1262.
14. Minassian, B.A., Ianzano, L., Meloche, M., Andermann, E., Rouleau, G.A., Delgado-Escueta, A.V. and Scherer, S.W. (2000) Mutation spectrum and predicted function of laforin in Lafora's progressive myoclonus epilepsy. Neurology, 55, 341-346.
15. Wang, J., Stuckey, J.A., Wishart, M.J. and Dixon, J.E. (2002) A unique carbohydrate binding domain targets the Lafora disease phosphatase to glycogen. J. Biol. Chem., 277, 2377-2380.
16. Carpenter, S., Karpati, G., Andermann, F., Jacob, J.C. and Andermann, E. (1974) Lafora's disease: peroxisomal storage in skeletal muscle. Neurology, 24, 531-538.
17. Nishimura, R.N., Ishak, K.G., Reddick, R., Porter, R., James, S. and Barranger, J.A. (1980) Lafora disease: diagnosis by liver biopsy. Ann. Neurol., 8, 409-415.
18. Baumann, R.J., Kocoshis, S.A. and Wilson, D. (1983) Lafora disease: liver histopathology in presymptomatic children. Ann. Neurol., 14, 86-89.
19. Zhang, J., Somani, A.K., Yuen, D., Yang, Y., Love, P.E. and Siminovitch, K. A. (1999) Involvement of the SHP-1 tyrosine phosphatase in regulation of T cell selection. J. Immunol., 163, 3012-3021.
20. Maegawa, H., Hasegawa, M., Sugai, S., Obata, T., Ugi, S., Morino, K., Egawa, K., Fujita, T., Sakamoto, T., Nishio, Y. et al. (1999) Expression of a dominant negative SHP-2 in transgenic mice induces insulin resistance. J. Biol. Chem., 274, 30236-30243.
21. Aoki, Y., Huang, Z., Thomas, S.S., Bhide, P.G., Huang, I., Moskowitz, M.A. and Reeves, S.A. (2000) Increased susceptibility to ischemia-induced brain damage in transgenic mice overexpressing a dominant negative form of SHP2. FASEB J., 14, 1965-1973.
22. Miyazaki, J., Takaki, S., Araki, K., Tashiro, F., Tominaga, A., Takatsu, K. and Yamamura, K. (1989) Expression vector system based on the chicken beta-actin promoter directs efficient production of interleukin-5. Gene, 79, 269-277.
23. Ianzano, L., Zhao, X.C., Minassian, B.A. and Scherer, S.W. (2003) Identification of a novel protein interacting with laforin, the EPM2a progressive myoclonus epilepsy gene product. Genomics, 81, 579-587.
24. Ganesh, S., Tsurutani, N., Suzuki, T., Ueda, K., Agarwala, K.L., Osada, H., Delgado-Escueta, A.V. and Yamakawa, K. (2003) The Lafora disease gene product laforin interacts with HIRIP5, a phylogenetically conserved protein containing a NifU-like domain. Hum. Mol. Genet., 12, 2359-2368.
25. 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 Cordoba, S. (2003) 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, 3161-3171.
26. Fong, N.M., Jensen, T.C., Shah, A.S., Parekh, N.N., Saltiel, A.R. and Brady, M.J. (2000) Identification of binding sites on protein targeting to glycogen for enzymes of glycogen metabolism. J. Biol. Chem., 275, 35034-35039.
27. Broadwell, R.D. and Cataldo, A.M. (1983) The neuronal endoplasmic reticulum: its cytochemistry and contribution to the endomembrane system. I. Cell bodies and dendrites. J. Histochem. Cytochem., 31, 1077-1088.
28. Broadwell, R.D. and Cataldo, A.M. (1984) The neuronal endoplasmic reticulum: its cytochemistry and contribution to the endomembrane system. II. Axons and terminals. J. Comp. Neurol., 230, 231-248.
29. Villar-Palasi, C. and Guinovart, J.J. (1997) The role of glucose 6-phosphate in the control of glycogen synthase. FASEB J., 11, 544-558.
30. Steward, O. and Banker, G.A. (1992) Getting the message from the gene to the synapse: sorting and intracellular transport of RNA in neurons. Trends Neurosci., 15, 180-186.
31. Flint, A.J., Tiganis, T., Barford, D. and Tonks, N.K. (1997) Development of 'substrate-trapping' mutants to identify physiological substrates of protein tyrosine phosphatases. Proc. Natl Acad. Sci. USA, 94, 1680-1685.
32. Sun, H., Charles, C.H., Lau, L.F. and Tonks, N.K. (1993) MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell, 75, 487-493.
33. Snead, O.C., III (1988) gamma-Hydroxybutyrate model of generalized absence seizures: further characterization and comparison with other absence models. Epilepsia, 29, 361-368.
34. Paxinos, G. and Watson, C. (1986) The Rat Brain in Stereotaxic Coordinates, 2nd edn. Academic Press, San Diego, CA.
35. Cortez, M.A., McKerlie, C. and Snead, O.C., III (2001) A model of atypical absence seizures: EEG, pharmacology, and developmental characterization. Neurology, 56, 341-349.