Laforin in autophagy: A possible link between carbohydrate and protein in Lafora disease?

Autophagy

Volumn 6, Issue 8, 2010, Pages 1229-1231

  Puri, Rajat ^a   Ganesh, Subramaniam ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY KANPUR   (India)

Author keywords

Carbohydrate metabolism; Epilepsy; Lafora disease; Laforin; Malin; Neurodegeneration; Polyglucosan inclusions

Indexed keywords

CARBOHYDRATE; GLYCOGEN; LAFORIN; LAFORIN PHOSPHATASE; MALIN; PHOSPHATASE; PHOSPHATE; PHOSPHOPROTEIN PHOSPHATASE; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

ATAXIA; AUTOPHAGY; CYTOPLASM; HUMAN; INTELLECTUAL IMPAIRMENT; MYOCLONUS EPILEPSY; NONHUMAN; NOTE; PHAGOSOME; PROTEIN DEGRADATION; PROTEIN DEPHOSPHORYLATION;

EID: 78649240333     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.6.8.13307     Document Type: Note

References (28)

1. Ganesh S, Puri R, Singh S, Mittal S, Dubey D. Recent advances in the molecular basis of Lafora's progressive myoclonus epilepsy. J Hum Genet 2006; 51:1-8.
2. Singh S, Ganesh S. Lafora progressive myoclonus epilepsy: a meta-analysis of reported mutations in the first decade following the discovery of the EPM2A and NHLRC1 genes. Hum Mutat 2009; 30:715-23.
3. Ganesh S, Delgado-Escueta AV, Suzuki T, Francheschetti S, Riggio C, Avanzini G, et al. Genotype-phenotype correlations for EPM2A mutations in Lafora's progressive myoclonus epilepsy: exon 1 mutations associate with an early-onset cognitive deficit subphenotype. Hum Mol Genet 2002; 11:1263-71.
4. Van Heycop Ten Ham MW. Lafora disease, a form of progressive myoclonus epilepsy. In Vinken PJ, Bruyn GW, Eds. The Epilepsies - Handbook of Clinical Neurology, North-Holland, Amsterdam 1975; 382-422.
5. Yokoi S, Austin J, Witmer F, Sakai M. Studies in myoclonus epilepsy (Lafora body form). I. Isolation and preliminary characterization of Lafora bodies in two cases. Arch Neurol 1968; 19:15-33.
6. Sakai M, Austin J, Witmer F, Trueb L. Studies in myoclonus epilepsy (Lafora body form). II. Polyglucosans in the systemic deposits of myoclonus epilepsy and in corpora amylacea. Neurology 1970; 20:160-76.
7. Minassian BA, Lee JR, Herbrick JA, Huizenga J, Soder S, Mungall AJ, et al. Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy. Nat Genet 1998; 20:171-4.
8. Chan EM, Young EJ, Ianzano L, Munteanu I, Zhao X, Christopoulos CC, et al. Mutations in NHLRC1 cause progressive myoclonus epilepsy. Nat Genet 2003; 35:125-7.
9. Ganesh S, Agarwala KL, Ueda K, Akagi T, Shoda K, Usui T, et al. Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes. Hum Mol Genet 2000; 9:2251-61.
10. Gentry MS, Worby CA, Dixon JE. Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin. Proc Natl Acad Sci USA 2005; 102:8501-6.
11. Lohi H, Ianzano L, Zhao XC, Chan EM, Turnbull J, Scherer SW, et al. Novel glycogen synthase kinase 3 and ubiquitination pathways in progressive myoclonus epilepsy. Hum Mol Genet 2005; 14:2727-36.
12. Mittal S, Dubey D, Yamakawa K, Ganesh S. Lafora disease proteins malin and laforin are recruited to aggresomes in response to proteasomal impairment. Hum Mol Genet 2007; 16:753-62.
13. Ganesh S, Delgado-Escueta AV, Sakamoto T, Avila MR, Machado-Salas J, Hoshii Y, et al. Targeted disruption of the EPM2A gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioural response in mice. Hum Mol Genet 2002; 11:1251-62.
14. Depaoli-Roach AA, Tagliabracci VS, Segvich DM, Meyer CM, Irimia JM, Roach PJ. Genetic depletion of the malin E3 ubiquitin ligase in mice leads to Lafora bodies and the accumulation of insoluble laforin. J Biol Chem 2010; DOI:10.1074/jbc. M110.148668.
15. Wang W, Lohi H, Skurat AV, DePaoli-Roach AA, Minassian BA, Roach PJ. Glycogen metabolism in tissues from a mouse model of Lafora disease. Arch Biochem Biophys 2007; 457:264-9.
16. Tagliabracci VS, Turnbull J, Wang W, Girard JM, Zhao X, Skurat AV, et al. Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo. Proc Natl Acad Sci USA 2007; 104:19262-6.
17. Wang J, Stuckey JA, Wishart MJ, Dixon JE. A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen. J Biol Chem 2002; 277:2377-80.
18. Ganesh S, Tsurutani N, Suzuki T, Hoshii Y, Ishihara T, Delgado-Escueta AV, et al. The carbohydrate-binding domain of Lafora disease protein targets Lafora polyglucosan bodies. Biochem Biophys Res Commun 2004; 313:1101-9.
19. Chan EM, Ackerley CA, Lohi H, Ianzano L, Cortez MA, Shannon P, et al. Laforin preferentially binds the neurotoxic starch-like polyglucosans, which form in its absence in progressive myoclonus epilepsy. Hum Mol Genet 2004; 13:1117-29.
20. Worby CA, Gentry MS, Dixon JE. Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates. J Biol Chem 2006; 281:30412-8.
21. Tagliabracci VS, Girard JM, Segvich D, Meyer C, Turnbull J, Zhao X, et al. Abnormal metabolism of glycogen phosphate as a cause for Lafora disease. J Biol Chem 2008; 283:33816-25.
22. Garyali P, Siwach P, Singh PK, Puri R, Mittal S, Sengupta S, et al. The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system. Hum Mol Genet 2009; 18:688-700.
23. Aguado C, Sarkar S, Korolchuk VI, Criado O, Vernia S, Boya P, et al. Laforin, the most common protein mutated in Lafora disease, regulates autophagy. Hum Mol Genet 2010; 19:2867-76.
24. Mizushima N. Autophagy: process and function. Genes Dev 2007; 21:2861-73.
25. Komatsu M, Waguri S, Chiba T, Murata S, Iwata J, Tanida I, et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 2006; 441:880-4.
26. Kotoulas OB, Kalamidas SA, Kondomerkos DJ. Glycogen autophagy in glucose homeostasis. Pathol Res Pract 2006; 202:631-8.
27. Raben N, Hill V, Shea L, Takikita S, Baum R, Mizushima N, et al. Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease. Hum Mol Genet 2008; 17:3897-908.
28. Vernia S, Rubio T, Heredia M, Rodríguez de Córdoba S, Sanz P. Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin. PLoS One 2009; 4:5907.