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Laforin is a cell membrane and endoplasmic reticulum–associated protein tyrosine phosphatase
Author(s) -
Minassian Berge A.,
Andrade Danielle M.,
Ianzano Leonarda,
Young Edwin J.,
Chan Elayne,
Ackerley Cameron A.,
Scherer Stephen W.
Publication year - 2001
Publication title -
annals of neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.764
H-Index - 296
eISSN - 1531-8249
pISSN - 0364-5134
DOI - 10.1002/1531-8249(20010201)49:2<271::aid-ana52>3.0.co;2-d
Subject(s) - endoplasmic reticulum , lafora disease , progressive myoclonus epilepsy , protein tyrosine phosphatase , subcellular localization , microbiology and biotechnology , biology , phosphatase , stim1 , tyrosine , membrane protein , epilepsy , biochemistry , neuroscience , membrane , cytoplasm , phosphorylation
Lafora disease (LD) is the only progressive myoclonus epilepsy with polyglucosan bodies. Among conditions with polyglucosan bodies, LD is unique for the subcellular location of its polyglucosans in neuronal perikarya and dendrites and not in axons. Here we report that the protein encoded by the EPM2A gene, which is mutated in LD, localizes at the plasma membrane and the endoplasmic reticulum and that it is a functional protein tyrosine phosphatase. The significance of these findings in the epilepsy of LD and in the origin and characteristic subcellular location of Lafora bodies is discussed. Ann Neurol 2001;49:271–275