The Nuclear Envelope Protein, LAP1B, Is a Novel Protein Phosphatase 1 Substrate
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Mendeley | Further Information

{"title"=>"The Nuclear Envelope Protein, LAP1B, Is a Novel Protein Phosphatase 1 Substrate", "type"=>"journal", "authors"=>[{"first_name"=>"Mariana", "last_name"=>"Santos"}, {"first_name"=>"Sandra", "last_name"=>"Rebelo"}, {"first_name"=>"Paula J M", "last_name"=>"Van Kleeff"}, {"first_name"=>"Connie E.", "last_name"=>"Kim"}, {"first_name"=>"William T.", "last_name"=>"Dauer"}, {"first_name"=>"Margarida", "last_name"=>"Fardilha"}, {"first_name"=>"Odete A.", "last_name"=>"da Cruz e Silva"}, {"first_name"=>"Edgar F.", "last_name"=>"da Cruz e Silva"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "doi"=>"10.1371/journal.pone.0076788", "pmid"=>"24116158"}, "id"=>"25d9a13b-dcf3-3cc4-946b-8269634c8fea", "abstract"=>"Protein phosphatase 1 (PP1) binding proteins are quintessential regulators, determining substrate specificity and defining subcellular localization and activity of the latter. Here, we describe a novel PP1 binding protein, the nuclear membrane protein lamina associated polypeptide 1B (LAP1B), which interacts with the DYT1 dystonia protein torsinA. The PP1 binding domain in LAP1B was here identified as the REVRF motif at amino acids 55-59. The LAP1B:PP1 complex can be immunoprecipitated from cells in culture and rat cortex and the complex was further validated by yeast co-transformations and blot overlay assays. PP1, which is enriched in the nucleus, binds to the N-terminal nuclear domain of LAP1B, as shown by immunocolocalization and domain specific binding studies. PP1 dephosphorylates LAP1B, confirming the physiological relevance of this interaction. These findings place PP1 at a key position to participate in the pathogenesis of DYT1 dystonia and related nuclear envelope-based diseases.", "link"=>"http://www.mendeley.com/research/nuclear-envelope-protein-lap1b-novel-protein-phosphatase-1-substrate-1", "reader_count"=>21, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Researcher"=>7, "Student > Ph. D. Student"=>5, "Student > Postgraduate"=>1, "Student > Master"=>3, "Student > Bachelor"=>3, "Professor"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Researcher"=>7, "Student > Ph. D. Student"=>5, "Student > Postgraduate"=>1, "Student > Master"=>3, "Student > Bachelor"=>3, "Professor"=>1}, "reader_count_by_subject_area"=>{"Engineering"=>1, "Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>6, "Agricultural and Biological Sciences"=>10, "Medicine and Dentistry"=>2, "Neuroscience"=>1}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Neuroscience"=>{"Neuroscience"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>10}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>6}, "Unspecified"=>{"Unspecified"=>1}}, "reader_count_by_country"=>{"Belgium"=>2, "United States"=>1}, "group_count"=>1}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1226917"], "description"=>"<p>HeLa cells were transfected with Myc-LAP1B and then processed for immunocytochemistry using specific antibodies to Myc-tag and endogenous lamin B1 and PP1γ and α isoforms. <b>A</b>- Immunolocalization of both myc-LAP1B and lamin B1. <b>B</b>- Immunolocalization of myc-LAP1B and PP1γ and α isoforms. The presence of the complexes is evidenced by the ROI (region of interest). <b>C, D</b>- Confocal profiles representing the green fluorescence intensity (FITC-conjugated secondary antibody labelling Myc-LAP1B) and the red fluorescence intensity (Alexa Fluor 594- conjugated secondary antibody labelling PP1γ [C] or PP1α [D]) in a specific distance (arrow); asterisks denote co-localizing points. <b>E</b>- Quantification of % of co-localization between LAP1B and PP1 isoforms. Values are mean ± SEM, n= 75 cells (for PP1γ) and 55 cells (for PP1α). Photographs were acquired using a LSM 510-Meta confocal microscope. Bars, 10 µm.</p>", "links"=>[], "tags"=>["hela"], "article_id"=>816365, "categories"=>["Biological Sciences"], "users"=>["Mariana Santos", "Sandra Rebelo", "Paula J. M. Van Kleeff", "Connie E. Kim", "William T. Dauer", "Margarida Fardilha", "Odete A. da Cruz e Silva", "Edgar F. da Cruz e Silva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076788.g006", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Subcellular_distribution_of_the_LAP1B_PP1_complex_in_HeLa_cells_/816365", "title"=>"Subcellular distribution of the LAP1B:PP1 complex in HeLa cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:56:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226902"], "description"=>"<p><b>A</b>- Nucleotide and corresponding amino acid sequence of human LAP1B encoded by clone 135. Stop and start codons are coloured blue. The three well conserved PP1 binding motifs (RVxF) are highlighted in red (positions 55-59, 212-215 and 538-541 in aa sequence) and a second generic PP1 binding motif (SILK) is coloured green (position 306-309 in aa sequence). The transmembrane domain is highlighted in orange (position 339-361 in aa sequence). <b>B</b>- Schematic illustration of LAP1B domains. Sequence of human LAP1B was aligned against others species using ClustalW algorithm. Sequence conservation is indicated by asterisks (identical sequences), colons (conserved substitutions) and periods (semi-conserved substitutions). BM1, BM2 and BM3, RVxF-like PP1 binding motif 1, 2 and 3, respectively; INM, inner nuclear membrane; ONM, Outer nuclear membrane; SILK, a second generic PP1 binding motif; TM, transmembrane domain.</p>", "links"=>[], "tags"=>["lap1b"], "article_id"=>816350, "categories"=>["Biological Sciences"], "users"=>["Mariana Santos", "Sandra Rebelo", "Paula J. M. Van Kleeff", "Connie E. Kim", "William T. Dauer", "Margarida Fardilha", "Odete A. da Cruz e Silva", "Edgar F. da Cruz e Silva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076788.g001", "stats"=>{"downloads"=>1, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Human_LAP1B_sequence_and_domains_/816350", "title"=>"Human LAP1B sequence and domains.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:56:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226911"], "description"=>"<p>A- COS-7 cells were transfected with Myc-LAP1B, Myc-LAP1B-BM2 or Myc-LAP1B-BM3 and immunoprecipitated with PP1γ bound to protein G- DynaBeads. B- Non-transfected COS-7 cells were immunoprecipitated with PP1γ or PP1α antibodies bound to protein G- Dynabeads. C-SH-SY5Y cells were immunoprecipitated with PP1γ or PP1α antibodies bound to protein G- Dynabeads. D- Rat cortex extracts were immunoprecipitated with PP1γ, PP1α or LAP1 antibodies bound to protein G- Dynabeads. The negative controls were performed by incubating cell extracts with beads. IP, immunoprecipitation. IB, immunoblotting.</p>", "links"=>[], "tags"=>["cos-7", "sh-sy5y", "cells"], "article_id"=>816359, "categories"=>["Biological Sciences"], "users"=>["Mariana Santos", "Sandra Rebelo", "Paula J. M. Van Kleeff", "Connie E. Kim", "William T. Dauer", "Margarida Fardilha", "Odete A. da Cruz e Silva", "Edgar F. da Cruz e Silva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076788.g004", "stats"=>{"downloads"=>1, "page_views"=>24, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Co_immunoprecipitation_of_the_PP1_LAP1B_complex_in_COS_7_cells_SH_SY5Y_cells_and_rat_cortex_/816359", "title"=>"Co-immunoprecipitation of the PP1:LAP1B complex in COS-7 cells, SH-SY5Y cells and rat cortex.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:56:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226912"], "description"=>"<p>Two samples of purified recombinant PP1γ protein were separated by SDS-PAGE and the resulting blot was overlaid with LAP1B-IVT (1) or LAP1B (ΔA185)-IVT (2). IB, immunoblotting.</p>", "links"=>[], "tags"=>["overlay", "assay", "lap1b"], "article_id"=>816360, "categories"=>["Biological Sciences"], "users"=>["Mariana Santos", "Sandra Rebelo", "Paula J. M. Van Kleeff", "Connie E. Kim", "William T. Dauer", "Margarida Fardilha", "Odete A. da Cruz e Silva", "Edgar F. da Cruz e Silva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076788.g005", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Blot_overlay_assay_of_LAP1B_variants_/816360", "title"=>"Blot overlay assay of LAP1B variants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:56:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226906"], "description"=>"<div><p><b>Immunoblotting analysis using a His-tag antibody is also shown</b>. </p>\n\t\t\t\t\t\t<p>A-Schematic representation of LAP1B deletion mutants cloned into the pET-28c vector. The expected molecular weight (MW) of each construct is indicated. The red boxes represent the RVxF motifs, the green boxes correspond to the SILK motif, and the yellow boxes represent the transmembrane domain. B- Blot overlay assay of full-length LAP1B. Increasing amounts of recombinant full-length LAP1B (12, 24 and 48 µL) were loaded on each well as indicated. C- Blot overlay assay of LAP1B deletion mutants. Deletion mutants: 1, LAP1B–BM1; 2, LAP1B–BM2; 3, LAP1B–BM1/2+TM; 4, LAP1B–BM1/2-TM; 5, LAP1B-BM3+TM; 6, LAP1B-BM3-TM. Non-induced (NI) and pET-28c vector without an insert (pET) were used as negative controls and Nek2A (Nek) as positive control. Bacterial cultures were collected 3 hours after IPTG (1mM) induction at 37°C.</p></div>", "links"=>[], "tags"=>["overlay", "assay"], "article_id"=>816354, "categories"=>["Biological Sciences"], "users"=>["Mariana Santos", "Sandra Rebelo", "Paula J. M. Van Kleeff", "Connie E. Kim", "William T. Dauer", "Margarida Fardilha", "Odete A. da Cruz e Silva", "Edgar F. da Cruz e Silva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076788.g002", "stats"=>{"downloads"=>3, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Blot_overlay_assay_with_PP1_947_1_/816354", "title"=>"Blot overlay assay with PP1γ1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:56:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226919"], "description"=>"<p>SH-SY5Y cells were incubated with 0, 0.25 or 500 nM okadaic acid (OA) for 3 hours and immunoprecipitated with LAP1 antibody. Immunoprecipitates were incubated at 30°C for 1 hour with or without 100 ng of PP1γ1 protein. The negative controls were performed by incubation of cells extracts with beads. In the left panel are presented the cell lysates correspondent of each condition immunoprecipitated (right panel). IP, immunoprecipitation. IB, immunoblotting.</p>", "links"=>[], "tags"=>["dephosphorylation"], "article_id"=>816367, "categories"=>["Biological Sciences"], "users"=>["Mariana Santos", "Sandra Rebelo", "Paula J. M. Van Kleeff", "Connie E. Kim", "William T. Dauer", "Margarida Fardilha", "Odete A. da Cruz e Silva", "Edgar F. da Cruz e Silva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076788.g008", "stats"=>{"downloads"=>2, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_In_vitro_dephosphorylation_of_LAP1B_/816367", "title"=>"<i>In vitro</i> dephosphorylation of LAP1B.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:56:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226920", "https://ndownloader.figshare.com/files/1226921"], "description"=>"<div><p>Protein phosphatase 1 (PP1) binding proteins are quintessential regulators, determining substrate specificity and defining subcellular localization and activity of the latter. Here, we describe a novel PP1 binding protein, the nuclear membrane protein lamina associated polypeptide 1B (LAP1B), which interacts with the DYT1 dystonia protein torsinA. The PP1 binding domain in LAP1B was here identified as the REVRF motif at amino acids 55-59. The LAP1B:PP1 complex can be immunoprecipitated from cells in culture and rat cortex and the complex was further validated by yeast co-transformations and blot overlay assays. PP1, which is enriched in the nucleus, binds to the N-terminal nuclear domain of LAP1B, as shown by immunocolocalization and domain specific binding studies. PP1 dephosphorylates LAP1B, confirming the physiological relevance of this interaction. These findings place PP1 at a key position to participate in the pathogenesis of DYT1 dystonia and related nuclear envelope-based diseases.</p> </div>", "links"=>[], "tags"=>["phosphatase"], "article_id"=>816368, "categories"=>["Biological Sciences"], "users"=>["Mariana Santos", "Sandra Rebelo", "Paula J. M. Van Kleeff", "Connie E. Kim", "William T. Dauer", "Margarida Fardilha", "Odete A. da Cruz e Silva", "Edgar F. da Cruz e Silva"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0076788.s001", "https://dx.doi.org/10.1371/journal.pone.0076788.s002"], "stats"=>{"downloads"=>3, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_Nuclear_Envelope_Protein_LAP1B_Is_a_Novel_Protein_Phosphatase_1_Substrate_/816368", "title"=>"The Nuclear Envelope Protein, LAP1B, Is a Novel Protein Phosphatase 1 Substrate", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2013-10-07 01:56:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226918"], "description"=>"<p>HEK293 cells were immunoprecipitated with PP1 antibody bound to protein A- sepharose beads. The negative controls were performed by incubating cell extracts with beads. IP, immunoprecipitation. IB, immunoblotting.</p>", "links"=>[], "tags"=>["pp1", "binding", "proteins"], "article_id"=>816366, "categories"=>["Biological Sciences"], "users"=>["Mariana Santos", "Sandra Rebelo", "Paula J. M. Van Kleeff", "Connie E. Kim", "William T. Dauer", "Margarida Fardilha", "Odete A. da Cruz e Silva", "Edgar F. da Cruz e Silva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076788.g007", "stats"=>{"downloads"=>0, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Co_immunoprecipitation_of_PP1_binding_proteins_at_the_nuclear_envelope_/816366", "title"=>"Co-immunoprecipitation of PP1 binding proteins at the nuclear envelope.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:56:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/1226908"], "description"=>"<p>Full-length LAP1B and its deletion mutants cloned in the pACT2 vector are represented. The red boxes represent the RVxF motifs present in the constructs, the green boxes correspond to the SILK motif, and the yellow boxes represent the transmembrane domain. A- Positive interactions were observed between LAP1B and PP1α, PP1γ1 and PP1γ2, but not with the C-terminus of PP1γ2 (PP1γ2End). B- PP1γ1 interacted with LAP1B-BM1 and BM1/2 but not with LAP1B-BM2 and BM3. C- Association of murine p53 and SV40 large T antigen was used as positive control (+) and co-transformation of pAS2-1 and pACT2 vectors as negative control (-).</p>", "links"=>[], "tags"=>["co-transformation", "assay"], "article_id"=>816356, "categories"=>["Biological Sciences"], "users"=>["Mariana Santos", "Sandra Rebelo", "Paula J. M. Van Kleeff", "Connie E. Kim", "William T. Dauer", "Margarida Fardilha", "Odete A. da Cruz e Silva", "Edgar F. da Cruz e Silva"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0076788.g003", "stats"=>{"downloads"=>2, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Yeast_co_transformation_assay_in_SD_QDO_X_945_gal_medium_/816356", "title"=>"Yeast co-transformation assay in SD/QDO/X-α-gal medium.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-10-07 01:56:11"}

PMC Usage Stats | Further Information

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  • {"unique-ip"=>"5", "full-text"=>"4", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"8"}
  • {"unique-ip"=>"5", "full-text"=>"4", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"2", "cited-by"=>"0", "year"=>"2018", "month"=>"11"}
  • {"unique-ip"=>"1", "full-text"=>"1", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"2"}
  • {"unique-ip"=>"5", "full-text"=>"6", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
  • {"unique-ip"=>"2", "full-text"=>"1", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"4"}
  • {"unique-ip"=>"5", "full-text"=>"5", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"5"}
  • {"unique-ip"=>"7", "full-text"=>"5", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"8"}

Relative Metric

{"start_date"=>"2013-01-01T00:00:00Z", "end_date"=>"2013-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences/Agriculture", "average_usage"=>[241, 422, 551, 659, 765, 866, 954, 1043, 1142, 1235, 1311, 1397, 1462]}, {"subject_area"=>"/Biology and life sciences/Biochemistry", "average_usage"=>[266, 468, 593, 703, 804, 903, 993, 1084, 1171, 1256, 1339, 1422, 1492]}, {"subject_area"=>"/Biology and life sciences/Cell biology", "average_usage"=>[272, 472, 600, 713, 815, 911, 1004, 1094, 1185, 1273, 1358, 1441]}]}
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