A PTG Variant Contributes to a Milder Phenotype in Lafora Disease
Publication Date
June 30, 2011
Journal
PLOS ONE
Authors
Rosa Guerrero, Santiago Vernia, Raúl Sanz, Irene Abreu Rodríguez, et al
Volume
6
Issue
6
Pages
e21294
DOI
https://dx.plos.org/10.1371/journal.pone.0021294
Publisher URL
http://journals.plos.org/plosone/article?id=10.1371%2Fjournal.pone.0021294
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/21738631
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3127956
Europe PMC
http://europepmc.org/abstract/MED/21738631
Web of Science
000292291800010
Scopus
79959796096
Mendeley
http://www.mendeley.com/research/ptg-variant-contributes-milder-phenotype-lafora-disease
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Mendeley | Further Information

{"title"=>"A PTG variant contributes to a Milder Phenotype in Lafora disease", "type"=>"journal", "authors"=>[{"first_name"=>"Rosa", "last_name"=>"Guerrero", "scopus_author_id"=>"23973044500"}, {"first_name"=>"Santiago", "last_name"=>"Vernia", "scopus_author_id"=>"6508277253"}, {"first_name"=>"Raúl", "last_name"=>"Sanz", "scopus_author_id"=>"55179007700"}, {"first_name"=>"Irene", "last_name"=>"Abreu-Rodríguez", "scopus_author_id"=>"41960925300"}, {"first_name"=>"Carmen", "last_name"=>"Almaraz", "scopus_author_id"=>"35081678800"}, {"first_name"=>"María", "last_name"=>"García-Hoyos", "scopus_author_id"=>"6506124851"}, {"first_name"=>"Roberto", "last_name"=>"Michelucci", "scopus_author_id"=>"7005403451"}, {"first_name"=>"Carlo Alberto", "last_name"=>"Tassinari", "scopus_author_id"=>"7103038233"}, {"first_name"=>"Patrizia", "last_name"=>"Riguzzi", "scopus_author_id"=>"6602158494"}, {"first_name"=>"Carlo", "last_name"=>"Nobile", "scopus_author_id"=>"7006001212"}, {"first_name"=>"Pascual", "last_name"=>"Sanz", "scopus_author_id"=>"7102001749"}, {"first_name"=>"José M.", "last_name"=>"Serratosa", "scopus_author_id"=>"7004891877"}, {"first_name"=>"Pilar", "last_name"=>"Gómez-Garre", "scopus_author_id"=>"12781472700"}], "year"=>2011, "source"=>"PLoS ONE", "identifiers"=>{"isbn"=>"1932-6203 (Electronic)\\n1932-6203 (Linking)", "pmid"=>"21738631", "doi"=>"10.1371/journal.pone.0021294", "pui"=>"362045212", "issn"=>"19326203", "sgr"=>"79959796096", "scopus"=>"2-s2.0-79959796096"}, "id"=>"fe5706c8-2b9d-37d1-9dfa-95dac8c6d655", "abstract"=>"Lafora disease is an autosomal recessive form of progressive myoclonus epilepsy with no effective therapy. Although the outcome is always unfavorable, onset of symptoms and progression of the disease may vary. We aimed to identify modifier genes that may contribute to the clinical course of Lafora disease patients with EPM2A or EPM2B mutations. We established a list of 43 genes coding for proteins related to laforin/malin function and/or glycogen metabolism and tested common polymorphisms for possible associations with phenotypic differences using a collection of Lafora disease families. Genotype and haplotype analysis showed that PPP1R3C may be associated with a slow progression of the disease. The PPP1R3C gene encodes protein targeting to glycogen (PTG). Glycogen targeting subunits play a major role in recruiting type 1 protein phosphatase (PP1) to glycogen-enriched cell compartments and in increasing the specific activity of PP1 toward specific glycogenic substrates (glycogen synthase and glycogen phosphorylase). Here, we report a new mutation (c.746A>G, N249S) in the PPP1R3C gene that results in a decreased capacity to induce glycogen synthesis and a reduced interaction with glycogen phosphorylase and laforin, supporting a key role of this mutation in the glycogenic activity of PTG. This variant was found in one of two affected siblings of a Lafora disease family characterized by a remarkable mild course. Our findings suggest that variations in PTG may condition the course of Lafora disease and establish PTG as a potential target for pharmacogenetic and therapeutic approaches.", "link"=>"http://www.mendeley.com/research/ptg-variant-contributes-milder-phenotype-lafora-disease", "reader_count"=>14, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Researcher"=>5, "Student > Doctoral Student"=>2, "Student > Postgraduate"=>1, "Student > Master"=>2, "Other"=>1, "Student > Bachelor"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Researcher"=>5, "Student > Doctoral Student"=>2, "Student > Postgraduate"=>1, "Student > Master"=>2, "Other"=>1, "Student > Bachelor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Biochemistry, Genetics and Molecular Biology"=>2, "Medicine and Dentistry"=>2, "Agricultural and Biological Sciences"=>4, "Veterinary Science and Veterinary Medicine"=>1, "Sports and Recreations"=>1, "Chemistry"=>1, "Computer Science"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Chemistry"=>{"Chemistry"=>1}, "Sports and Recreations"=>{"Sports and Recreations"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>4}, "Computer Science"=>{"Computer Science"=>1}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}, "Unspecified"=>{"Unspecified"=>2}, "Veterinary Science and Veterinary Medicine"=>{"Veterinary Science and Veterinary Medicine"=>1}}, "reader_count_by_country"=>{"Portugal"=>1}, "group_count"=>1}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/759847"], "description"=>"<p>(A) Electropherograms show the two containing-variation regions in control (top) and affected individuals (bottom). Nucleotides that change are indicated. B) Schematic drawing of the genomic structure of <i>PPP1R3C</i>. Position of the variations found in Lafora disease patients is shown.</p>", "links"=>[], "tags"=>["genetics and genomics", "neurological disorders"], "article_id"=>430208, "categories"=>["Genetics", "Neuroscience"], "users"=>["Rosa Guerrero", "Santiago Vernia", "Raúl Sanz", "Irene Abreu-Rodríguez", "Carmen Almaraz", "María García-Hoyos", "Roberto Michelucci", "Carlo Alberto Tassinari", "Patrizia Riguzzi", "Carlo Nobile", "Pascual Sanz", "José M. Serratosa", "Pilar Gómez-Garre"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021294.g001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Mutational_analysis_of_PPP1R3C_/430208", "title"=>"Mutational analysis of <i>PPP1R3C</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-06-30 00:03:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/760457"], "description"=>"<p>A) Partial structures of constructs used in reporter assays. B) Gene reporter assays in PC12 and EOMA cells. Cells were transiently co-transfected with the reporter constructs containing the rs62620038 (position −50) variant or empty vector, as indicated. Each bar represents the average fold-induction relative to the empty vector.</p>", "links"=>[], "tags"=>["variant", "pgl3", "basic-derived"], "article_id"=>430811, "categories"=>["Genetics", "Neuroscience"], "users"=>["Rosa Guerrero", "Santiago Vernia", "Raúl Sanz", "Irene Abreu-Rodríguez", "Carmen Almaraz", "María García-Hoyos", "Roberto Michelucci", "Carlo Alberto Tassinari", "Patrizia Riguzzi", "Carlo Nobile", "Pascual Sanz", "José M. Serratosa", "Pilar Gómez-Garre"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021294.g006", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Impact_of_the_8722_50T_gt_C_variant_in_pGL3_basic_derived_constructs_/430811", "title"=>"Impact of the −50T>C variant in pGL3 basic-derived constructs.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-06-30 00:13:31"}
  • {"files"=>["https://ndownloader.figshare.com/files/760258"], "description"=>"<p>(A) Crude extracts from homogenates of cultured HEK293 cells transfected with pCMV-HA empty plasmid (none) or plasmids expressing wild type (WT) and mutated HA- PTG (N249S) were obtained and analyzed by Western blotting using anti-GS and anti- PTG. Actin was used as a control for gel loading. (B) HEK293 cells were co-transfected or not with plasmids pCMV-myc-laforin/pcDNA-HA-malin and with pCMV-HA (empty plasmid; none) or plasmids expressing wild type (WT) or mutated HA- PTG (N249S). Eighteen hours after the transfection, the amount of accumulated glycogen was measured as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0021294#s4\" target=\"_blank\">Materials and Methods</a>.</p>", "links"=>[], "tags"=>["n249s", "ptg", "glycogen", "synthesis", "blocking", "activate"], "article_id"=>430595, "categories"=>["Genetics", "Neuroscience"], "users"=>["Rosa Guerrero", "Santiago Vernia", "Raúl Sanz", "Irene Abreu-Rodríguez", "Carmen Almaraz", "María García-Hoyos", "Roberto Michelucci", "Carlo Alberto Tassinari", "Patrizia Riguzzi", "Carlo Nobile", "Pascual Sanz", "José M. Serratosa", "Pilar Gómez-Garre"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021294.g004", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_presence_of_N249S_in_PTG_reduces_glycogen_synthesis_by_blocking_its_capacity_to_activate_GS_/430595", "title"=>"The presence of N249S in PTG reduces glycogen synthesis by blocking its capacity to activate GS.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-06-30 00:09:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/760125"], "description"=>"<p>Yeast CTY10.5d strain was transformed with plasmids pACT2 (empty plasmid), pACT2- PTG (wt), or pACT2-N249S-PTG (N249S) and co-transformed with plasmids pBTM-PP1α (LexA-PP1), pBTM-AMPKβ2 (LexA-AMPKß2), pEG202-laforin (LexA-laforin) and pEF202-RABPYGM (LexA-GPh). Protein interaction was estimated by measuring the β-Galactosidase activity in permeabilized yeast cells and expressed in Miller units. Abbreviations: PP1α, protein phosphatase 1; AMPKβ2, AMP-activated protein kinase subunit β2; GPh, glycogen phosphorylase. When indicated, crude extracts (25 µg) from two independent transformants were analyzed by western blotting using anti-LexA and ant-HA antibodies.</p>", "links"=>[], "tags"=>["two-hybrid", "assays", "ptg"], "article_id"=>430484, "categories"=>["Genetics", "Neuroscience"], "users"=>["Rosa Guerrero", "Santiago Vernia", "Raúl Sanz", "Irene Abreu-Rodríguez", "Carmen Almaraz", "María García-Hoyos", "Roberto Michelucci", "Carlo Alberto Tassinari", "Patrizia Riguzzi", "Carlo Nobile", "Pascual Sanz", "José M. Serratosa", "Pilar Gómez-Garre"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021294.g003", "stats"=>{"downloads"=>0, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Yeast_two_hybrid_interaction_assays_of_PTG_with_different_proteins_/430484", "title"=>"Yeast two-hybrid interaction assays of PTG with different proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-06-30 00:08:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/382125"], "description"=>"<div><p>Lafora disease is an autosomal recessive form of progressive myoclonus epilepsy with no effective therapy. Although the outcome is always unfavorable, onset of symptoms and progression of the disease may vary. We aimed to identify modifier genes that may contribute to the clinical course of Lafora disease patients with <em>EPM2A</em> or <em>EPM2B</em> mutations. We established a list of 43 genes coding for proteins related to laforin/malin function and/or glycogen metabolism and tested common polymorphisms for possible associations with phenotypic differences using a collection of Lafora disease families. Genotype and haplotype analysis showed that <em>PPP1R3C</em> may be associated with a slow progression of the disease. The <em>PPP1R3C</em> gene encodes protein targeting to glycogen (PTG). Glycogen targeting subunits play a major role in recruiting type 1 protein phosphatase (PP1) to glycogen-enriched cell compartments and in increasing the specific activity of PP1 toward specific glycogenic substrates (glycogen synthase and glycogen phosphorylase). Here, we report a new mutation (c.746A>G, N249S) in the <em>PPP1R3C</em> gene that results in a decreased capacity to induce glycogen synthesis and a reduced interaction with glycogen phosphorylase and laforin, supporting a key role of this mutation in the glycogenic activity of PTG. This variant was found in one of two affected siblings of a Lafora disease family characterized by a remarkable mild course. Our findings suggest that variations in PTG may condition the course of Lafora disease and establish PTG as a potential target for pharmacogenetic and therapeutic approaches.</p> </div>", "links"=>[], "tags"=>["ptg", "variant", "contributes", "milder", "phenotype", "lafora"], "article_id"=>135472, "categories"=>["Genetics", "Neuroscience"], "users"=>["Rosa Guerrero", "Santiago Vernia", "Raúl Sanz", "Irene Abreu-Rodríguez", "Carmen Almaraz", "María García-Hoyos", "Roberto Michelucci", "Carlo Alberto Tassinari", "Patrizia Riguzzi", "Carlo Nobile", "Pascual Sanz", "José M. Serratosa", "Pilar Gómez-Garre"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021294", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/A_PTG_Variant_Contributes_to_a_Milder_Phenotype_in_Lafora_Disease/135472", "title"=>"A PTG Variant Contributes to a Milder Phenotype in Lafora Disease", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-06-30 01:31:12"}
  • {"files"=>["https://ndownloader.figshare.com/files/760366"], "description"=>"<p>A) Human neuroblastoma SH-SY5Y cells were transfected with plasmid pSUPER-laf to deplete the levels of laforin. Crude extracts from these cells were analyzed by western blotting using anti-laforin and anti-actin antibodies. B) SH-SY5Y cells depleted (sh-laforin) or not (control) of laforin were transfected with plasmids pCMV-HA (empty plasmid; none) or plasmids expressing wild type (WT) or mutated HA- PTG (N249S). Eighteen hours after the transfection, the amount of accumulated glycogen was measured as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0021294#s4\" target=\"_blank\"><i>Materials and Methods</i></a>. The dotted line represent the levels of glycogen in control conditions. Crude extracts from the same cells were analyzed by western blotting using anti-HA and anti-actin antibodies.</p>", "links"=>[], "tags"=>["n249s", "mutation", "ptg", "diminishes", "glycogen", "accumulated", "laforin-depleted"], "article_id"=>430713, "categories"=>["Genetics", "Neuroscience"], "users"=>["Rosa Guerrero", "Santiago Vernia", "Raúl Sanz", "Irene Abreu-Rodríguez", "Carmen Almaraz", "María García-Hoyos", "Roberto Michelucci", "Carlo Alberto Tassinari", "Patrizia Riguzzi", "Carlo Nobile", "Pascual Sanz", "José M. Serratosa", "Pilar Gómez-Garre"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021294.g005", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_N249S_mutation_in_PTG_diminishes_the_amount_of_glycogen_accumulated_in_laforin_depleted_cells_/430713", "title"=>"The N249S mutation in PTG diminishes the amount of glycogen accumulated in laforin-depleted cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-06-30 00:11:53"}
  • {"files"=>["https://ndownloader.figshare.com/files/759991"], "description"=>"<p>Multiple alignments of the motif shared by substrate binding domain of human PTG amino acid sequence and paralogues and homologues from various species are shown and identities are shadowed. The mutated asparagine residue (position 249 in the protein) is indicated with a vertical box. Asterisks mark esential aspartic residues that surround asparagine. Abbreviations are as follows: PBS, PP1 binding site; CBM21, carbohydrate binding module type-21; GBS, glycogen binding site; SBS, substrate binding site; PP1, protein phosphatase 1; AMPK, AMP-activated protein kinase; GPh, glycogen phosphorylase; GS, glycogen synthase; GPK, glycogen phosphorylase kinase.</p>", "links"=>[], "tags"=>["ptg", "alignments", "amino"], "article_id"=>430341, "categories"=>["Genetics", "Neuroscience"], "users"=>["Rosa Guerrero", "Santiago Vernia", "Raúl Sanz", "Irene Abreu-Rodríguez", "Carmen Almaraz", "María García-Hoyos", "Roberto Michelucci", "Carlo Alberto Tassinari", "Patrizia Riguzzi", "Carlo Nobile", "Pascual Sanz", "José M. Serratosa", "Pilar Gómez-Garre"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0021294.g002", "stats"=>{"downloads"=>1, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Schematic_drawing_of_PTG_domain_structure_and_multiple_alignments_of_human_PTG_amino_acid_sequence_/430341", "title"=>"Schematic drawing of PTG domain structure and multiple alignments of human PTG amino acid sequence.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-06-30 00:05:41"}

PMC Usage Stats | Further Information

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Relative Metric

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