Abstract

Lafora disease (LD) is a fatal, autosomal recessive, glycogen-storage disorder that manifests as severe epilepsy. LD results from mutations in the gene encoding either the glycogen phosphatase laforin or the E3 ubiquitin ligase malin. Individuals with LD develop cytoplasmic, aberrant glycogen inclusions in nearly all tissues that more closely resemble plant starch than human glycogen. This Minireview discusses the unique window into glycogen metabolism that LD research offers. It also highlights recent discoveries, including that glycogen contains covalently bound phosphate and that neurons synthesize glycogen and express both glycogen synthase and glycogen phosphorylase.

Document Type

Review

Publication Date

2-26-2018

Notes/Citation Information

Published in The Journal of Biological Chemistry, v. 293, no. 19, p. 7117-7125.

This research was originally published in The Journal of Biological Chemistry. Matthew S. Gentry, Joan J. Guinovart, Berge A. Minassian, Peter J. Roach, and Jose M. Serratosa. Lafora Disease Offers a Unique Window into Neuronal Glycogen Metabolism. J. Biol. Chem. 2018; 293:7117-7125. © 2018 by The American Society for Biochemistry and Molecular Biology, Inc.

The copyright holder has granted the permission for posting the article here.

Digital Object Identifier (DOI)

https://doi.org/10.1074/jbc.R117.803064

Funding Information

This work was supported by the National Institutes of Health under Award Numbers R01NS070899 (to M. S. G.), P01NS097197 (to M. S. G.), R01NS056454 (to P. J. R.), and R01DK037221 (to P. J. R.); a Mitzutani Foundation for Glycoscience award 130095 (to M. S. G.); a National Science Foundation CAREER award MCB-1252345 (to M. S. G.); and Ministerio de Economia de Spain, Industria y Competitividad Grants SAF2014-59594-R (to J. M. S.) and SAF2014-55525-P (to J. J. G.).

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