Lafora disease offers a unique window into neuronal glycogen metabolism

Matthew S. Gentry; Joan J. Guinovart; Berge A. Minassian; Peter J. Roach; Jose M. Serratosa

doi:10.1074/jbc.R117.803064

Lafora disease offers a unique window into neuronal glycogen metabolism

Matthew S. Gentry, Joan J. Guinovart, Berge A. Minassian, Peter J. Roach, Jose M. Serratosa

Research output: Contribution to journal › Review article › peer-review

58 Scopus citations

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.

Original language	English
Pages (from-to)	7117-7125
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	293
Issue number	19
DOIs	https://doi.org/10.1074/jbc.R117.803064
State	Published - May 11 2018

Bibliographical note

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.). This is the fourth article in the Thematic Minireview series “Brain glycogen metabolism.” The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health, Mitzutani Foundation, National Science Foundation, and Ministerio de Economia de Spain.

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 Foun-dation 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.). This is the fourth article in the Thematic Minireview series “Brain glycogen metabolism.” The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health, Mitzutani Foundation, National Science Foundation, and Ministerio de Economia de Spain.

Publisher Copyright:
© 2018 by The American Society for Biochemistry and Molecular Biology, Inc.

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1074/jbc.R117.803064

Cite this

@article{50afb305b20f4009bbf1e42f22acece4,

title = "Lafora disease offers a unique window into neuronal glycogen metabolism",

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.",

author = "Gentry, {Matthew S.} and Guinovart, {Joan J.} and Minassian, {Berge A.} and Roach, {Peter J.} and Serratosa, {Jose M.}",

note = "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.). This is the fourth article in the Thematic Minireview series “Brain glycogen metabolism.” The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health, Mitzutani Foundation, National Science Foundation, and Ministerio de Economia de Spain. 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 Foun-dation 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.). This is the fourth article in the Thematic Minireview series “Brain glycogen metabolism.” The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health, Mitzutani Foundation, National Science Foundation, and Ministerio de Economia de Spain. Publisher Copyright: {\textcopyright} 2018 by The American Society for Biochemistry and Molecular Biology, Inc.",

year = "2018",

month = may,

day = "11",

doi = "10.1074/jbc.R117.803064",

language = "English",

volume = "293",

pages = "7117--7125",

number = "19",

}

TY - JOUR

T1 - Lafora disease offers a unique window into neuronal glycogen metabolism

AU - Gentry, Matthew S.

AU - Guinovart, Joan J.

AU - Minassian, Berge A.

AU - Roach, Peter J.

AU - Serratosa, Jose M.

N1 - 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.). This is the fourth article in the Thematic Minireview series “Brain glycogen metabolism.” The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health, Mitzutani Foundation, National Science Foundation, and Ministerio de Economia de Spain. 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 Foun-dation 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.). This is the fourth article in the Thematic Minireview series “Brain glycogen metabolism.” The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health, Mitzutani Foundation, National Science Foundation, and Ministerio de Economia de Spain. Publisher Copyright: © 2018 by The American Society for Biochemistry and Molecular Biology, Inc.

PY - 2018/5/11

Y1 - 2018/5/11

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85046972198&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85046972198&partnerID=8YFLogxK

U2 - 10.1074/jbc.R117.803064

DO - 10.1074/jbc.R117.803064

M3 - Review article

C2 - 29483193

AN - SCOPUS:85046972198

SN - 0021-9258

VL - 293

SP - 7117

EP - 7125

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 19

ER -

Lafora disease offers a unique window into neuronal glycogen metabolism

Abstract

Bibliographical note

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this