The Amino-Terminus of Nitric Oxide Sensitive Guanylyl Cyclase α1 Does Not Affect Dimerization but Influences Subcellular Localization
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{"title"=>"The amino-terminus of Nitric oxide sensitive guanylyl cyclase α 1 does not affect dimerization but influences subcellular localization", "type"=>"journal", "authors"=>[{"first_name"=>"Jan R.", "last_name"=>"Kraehling", "scopus_author_id"=>"36241674600"}, {"first_name"=>"Mareike", "last_name"=>"Busker", "scopus_author_id"=>"53979471400"}, {"first_name"=>"Tobias", "last_name"=>"Haase", "scopus_author_id"=>"16506940600"}, {"first_name"=>"Nadine", "last_name"=>"Haase", "scopus_author_id"=>"55901885200"}, {"first_name"=>"Markus", "last_name"=>"Koglin", "scopus_author_id"=>"6602308180"}, {"first_name"=>"Monika", "last_name"=>"Linnenbaum", "scopus_author_id"=>"52563915300"}, {"first_name"=>"Soenke", "last_name"=>"Behrends", "scopus_author_id"=>"7006495294"}], "year"=>2011, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "pui"=>"362706600", "sgr"=>"80053585971", "doi"=>"10.1371/journal.pone.0025772", "scopus"=>"2-s2.0-80053585971", "isbn"=>"1932-6203 (Electronic)\\n1932-6203 (Linking)", "pmid"=>"21984946"}, "id"=>"d9acb915-37c8-3ac1-bb84-b804745d9644", "abstract"=>"Nitric oxide sensitive guanylyl cyclase (NOsGC) is a heterodimeric enzyme formed by an α- and a β₁-subunit. A splice variant (C-α₁) of the α₁-subunit, lacking at least the first 236 amino acids has been described by Sharina et al. 2008 and has been shown to be expressed in differentiating human embryonic cells. Wagner et al. 2005 have shown that the amino acids 61-128 of the α₁-subunit are mandatory for quantitative heterodimerization implying that the C-α₁-splice variant should lose its capacity to dimerize quantitatively.", "link"=>"http://www.mendeley.com/research/aminoterminus-nitric-oxide-sensitive-guanylyl-cyclase-%CE%B1-1-not-affect-dimerization-influences-subcell", "reader_count"=>6, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Researcher"=>2, "Student > Ph. D. Student"=>2, "Professor"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Researcher"=>2, "Student > Ph. D. Student"=>2, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>1, "Agricultural and Biological Sciences"=>2, "Neuroscience"=>1, "Pharmacology, Toxicology and Pharmaceutical Science"=>1}, "reader_count_by_subdiscipline"=>{"Neuroscience"=>{"Neuroscience"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>2}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>1}, "Unspecified"=>{"Unspecified"=>1}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>1}}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/729618"], "description"=>"<p>Specific activity was measured under basal conditions (<i>black column</i>), in the presence of 100 µM NO (DEA/NO, <i>white column</i>) and in the presence of 10 µM cinaciguat (<i>gray columns</i>). Data are expressed as means ± SEM. The experiments were repeated at least three times and one representative result is shown.</p>", "links"=>[], "tags"=>["cyclase", "purified", "variants"], "article_id"=>399968, "categories"=>["Biochemistry", "Chemistry"], "users"=>["Jan R. Kraehling", "Mareike Busker", "Tobias Haase", "Nadine Haase", "Markus Koglin", "Monika Linnenbaum", "Soenke Behrends"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025772.g006", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Guanylyl_cyclase_activity_of_purified_variants_of_the_enzyme_/399968", "title"=>"Guanylyl cyclase activity of purified variants of the enzyme.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-30 02:46:08"}
  • {"files"=>["https://ndownloader.figshare.com/files/729917"], "description"=>"<p>As a marker of the endoplasmic reticulum <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0025772#pone.0025772-Maines1\" target=\"_blank\">[11]</a> ECFP tagged heme oxygenase 1 (human, HO-1) was co-transfected. A, α<sub>1</sub> full-length shows cytosolic distribution. B, C-α<sub>1</sub> shows a similar distribution like ECFP-HO-1. C, addition of an untagged β<sub>1</sub>-subunit led in some cells a similar subcellular distribution as the wild type. The red arrow denotes a cell likely co-transfected with β<sub>1</sub>, the white arrow denotes a cell likely not co-transfected with β<sub>1</sub>. D, only cells which express both subunits show homogenous subcellular distribution. The red arrow denotes a cell co-transfected with β<sub>1</sub>, the white arrow denotes a cell not co-transfected with β<sub>1</sub>. E, The subcellular localization of α<sub>1</sub> full-length is not affected through coexpression of β<sub>1</sub>. Bar, 20 µm. CFP, ECFP channel; YFP, EYFP channel.</p>", "links"=>[], "tags"=>["eyfp-marked", "full-length", "hek-293"], "article_id"=>400269, "categories"=>["Biochemistry", "Chemistry"], "users"=>["Jan R. Kraehling", "Mareike Busker", "Tobias Haase", "Nadine Haase", "Markus Koglin", "Monika Linnenbaum", "Soenke Behrends"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025772.g009", "stats"=>{"downloads"=>1, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Expression_of_EYFP_marked_1_full_length_A_and_C_945_1_B_in_HEK_293_cells_/400269", "title"=>"Expression of EYFP-marked α<sub>1</sub> full-length (A) and C-α<sub>1</sub> (B) in HEK-293 cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-30 00:04:29"}
  • {"files"=>["https://ndownloader.figshare.com/files/729135"], "description"=>"<p>The graphic is a modified version of the domain architecture model by <i>Derbyshire</i> and <i>Marletta </i><a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0025772#pone.0025772-Derbyshire1\" target=\"_blank\">[34]</a>.</p>", "links"=>[], "tags"=>["deletion", "splice", "variant", "guanylyl"], "article_id"=>399482, "categories"=>["Biochemistry", "Chemistry"], "users"=>["Jan R. Kraehling", "Mareike Busker", "Tobias Haase", "Nadine Haase", "Markus Koglin", "Monika Linnenbaum", "Soenke Behrends"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025772.g001", "stats"=>{"downloads"=>1, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Assumed_formation_of_1_916_N_259_deletion_through_C_945_1_splice_variant_of_guanylyl_cyclase_/399482", "title"=>"Assumed formation of α<sub>1</sub>ΔN<sub>259</sub> deletion through C-α<sub>1</sub> splice variant of guanylyl cyclase.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-30 02:38:02"}
  • {"files"=>["https://ndownloader.figshare.com/files/730076"], "description"=>"<p>According to the settings a higher value means a more oxidized state of the protein.</p>", "links"=>[], "tags"=>["full-length", "hek-293", "redox-sensor"], "article_id"=>400429, "categories"=>["Biochemistry", "Chemistry"], "users"=>["Jan R. Kraehling", "Mareike Busker", "Tobias Haase", "Nadine Haase", "Markus Koglin", "Monika Linnenbaum", "Soenke Behrends"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025772.g010", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Redox_state_analysis_of_the_1_full_length_and_C_945_1_in_HEK_293_cells_using_the_redox_sensor_Grx1_roGFP2_/400429", "title"=>"Redox-state analysis of the α<sub>1</sub> full-length and C-α<sub>1</sub> in HEK-293 cells, using the redox-sensor Grx1-roGFP2.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-30 00:07:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/729262"], "description"=>"<p>5 µg of each purified enzyme was electrophoretically separated by SDS-Page and stained with Coomassie Blue. The experiments were repeated at least three times and one representative result is shown. [molecular weights predicted from their amino acid sequences: α<sub>1</sub>WT, 77.6 kDa; C-α<sub>1</sub>, 48 kDa; β<sub>1</sub><i>S</i>, 72.2 kDa].</p>", "links"=>[], "tags"=>["nosgc"], "article_id"=>399619, "categories"=>["Biochemistry", "Chemistry"], "users"=>["Jan R. Kraehling", "Mareike Busker", "Tobias Haase", "Nadine Haase", "Markus Koglin", "Monika Linnenbaum", "Soenke Behrends"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025772.g003", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SDS_PAGE_analysis_of_NOsGC_variants_/399619", "title"=>"SDS-PAGE analysis of NOsGC variants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-30 02:40:19"}
  • {"files"=>["https://ndownloader.figshare.com/files/729393"], "description"=>"<p>For quantification of the dimerization the optical densities of the Coomassie-stained bands were measured. A: The values obtained for α<sub>1</sub> were normalized to β<sub>1</sub> in the same lane. Dimerization was calculated in percentage of α<sub>1</sub>WT/β<sub>1</sub><i>S</i>. Data are expressed as means ± SEM.</p>", "links"=>[], "tags"=>["chemistry", "Biochemistry"], "article_id"=>399746, "categories"=>["Biochemistry", "Chemistry"], "users"=>["Jan R. Kraehling", "Mareike Busker", "Tobias Haase", "Nadine Haase", "Markus Koglin", "Monika Linnenbaum", "Soenke Behrends"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025772.g004", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Densitometric_analysis_of_dimerization_/399746", "title"=>"Densitometric analysis of dimerization.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-30 02:42:26"}
  • {"files"=>["https://ndownloader.figshare.com/files/729719"], "description"=>"<p>Spectroscopic analysis shows absorption values at basal (<i>solid line</i>) or NO-stimulated (100 µM DEA/NO, <i>dotted line</i>) conditions. A: α<sub>1</sub>WT/β<sub>1</sub><i>S</i>. B: C-α<sub>1</sub>/β<sub>1</sub><i>S</i>.</p>", "links"=>[], "tags"=>["purified", "cgc", "enzyme"], "article_id"=>400078, "categories"=>["Biochemistry", "Chemistry"], "users"=>["Jan R. Kraehling", "Mareike Busker", "Tobias Haase", "Nadine Haase", "Markus Koglin", "Monika Linnenbaum", "Soenke Behrends"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025772.g007", "stats"=>{"downloads"=>2, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Spectroscopic_analysis_of_purified_cGC_enzyme_complexes_/400078", "title"=>"Spectroscopic analysis of purified cGC enzyme complexes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-30 00:01:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/729811"], "description"=>"<p>Mean fluorescence lifetimes of ECFP were measured in HEK-293 cells at 37°C, 48 h post transfection with the respective recombinant constructs. A: α<sub>1</sub>-variants as fluorescence-donor. B: α<sub>1</sub>-variants as fluorescence-acceptor. Data are presented in box and whiskers plots showing the 25<sup>th</sup> percentiles, 75<sup>th</sup> percentile and median as box with the mean value as dotted line. Whiskers represent the 5<sup>th</sup> and 95<sup>th</sup> percentile, dots are outliers. Fluorescent tagged NOsGC variants show significantly reduced fluorescent lifetimes due to FRET.</p>", "links"=>[], "tags"=>["lifetimes", "fret", "ecfp", "hek-293", "expressing", "fluorescent", "tagged", "heterodimeric", "nosgc"], "article_id"=>400156, "categories"=>["Biochemistry", "Chemistry"], "users"=>["Jan R. Kraehling", "Mareike Busker", "Tobias Haase", "Nadine Haase", "Markus Koglin", "Monika Linnenbaum", "Soenke Behrends"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025772.g008", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Fluorescence_lifetimes_of_the_FRET_donor_ECFP_in_HEK_293_cells_expressing_donor_only_and_fluorescent_tagged_heterodimeric_NOsGC_variants_/400156", "title"=>"Fluorescence lifetimes of the FRET donor ECFP in HEK-293 cells, expressing donor only, and fluorescent tagged heterodimeric NOsGC variants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-30 00:02:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/368392", "https://ndownloader.figshare.com/files/368445"], "description"=>"<div><h3>Background</h3><p>Nitric oxide sensitive guanylyl cyclase (NOsGC) is a heterodimeric enzyme formed by an α- and a β<sub>1</sub>-subunit. A splice variant (C-α<sub>1</sub>) of the α<sub>1</sub>-subunit, lacking at least the first 236 amino acids has been described by <em>Sharina</em> et al. 2008 and has been shown to be expressed in differentiating human embryonic cells. <em>Wagner</em> et al. 2005 have shown that the amino acids 61–128 of the α<sub>1</sub>-subunit are mandatory for quantitative heterodimerization implying that the C-α<sub>1</sub>-splice variant should lose its capacity to dimerize quantitatively.</p> <h3>Methodology/Principal Findings</h3><p>In the current study we demonstrate preserved quantitative dimerization of the C-α<sub>1</sub>-splice by co-purification with the β<sub>1</sub>-subunit. In addition we used fluorescence resonance energy transfer (FRET) based on fluorescence lifetime imaging (FLIM) using fusion proteins of the β<sub>1</sub>-subunit and the α<sub>1</sub>-subunit or the C-α<sub>1</sub> variant with ECFP or EYFP. Analysis of the respective combinations in HEK-293 cells showed that the fluorescence lifetime was significantly shorter (≈0.3 ns) for α<sub>1</sub>/β<sub>1</sub> and C-α<sub>1</sub>/β<sub>1</sub> than the negative control. In addition we show that lack of the amino-terminus in the α<sub>1</sub> splice variant directs it to a more oxidized subcellular compartment.</p> <h3>Conclusions/Significance</h3><p>We conclude that the amino-terminus of the α<sub>1</sub>-subunit is dispensable for dimerization <em>in-vivo</em> and <em>ex-vivo</em>, but influences the subcellular trafficking.</p> </div>", "links"=>[], "tags"=>["amino-terminus", "nitric", "oxide", "guanylyl", "cyclase", "dimerization", "influences", "subcellular", "localization"], "article_id"=>132791, "categories"=>["Biochemistry", "Chemistry"], "users"=>["Jan R. Kraehling", "Mareike Busker", "Tobias Haase", "Nadine Haase", "Markus Koglin", "Monika Linnenbaum", "Soenke Behrends"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0025772.s001", "https://dx.doi.org/10.1371/journal.pone.0025772.s002"], "stats"=>{"downloads"=>5, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/The_Amino_Terminus_of_Nitric_Oxide_Sensitive_Guanylyl_Cyclase_1_Does_Not_Affect_Dimerization_but_Influences_Subcellular_Localization/132791", "title"=>"The Amino-Terminus of Nitric Oxide Sensitive Guanylyl Cyclase α<sub>1</sub> Does Not Affect Dimerization but Influences Subcellular Localization", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2011-09-30 00:46:31"}
  • {"files"=>["https://ndownloader.figshare.com/files/729192"], "description"=>"<p>All lanes were loaded with 40 µg protein of the cytosolic fractions. The experiments were repeated at least three times and one representative result is shown. [molecular weights predicted from their amino acid sequences: α<sub>1</sub>WT, 77.6 kDa; α<sub>1</sub>ΔN<sub>236</sub>, 51.2 kDa; α<sub>1</sub>ΔN<sub>259</sub>, 48 kDa].</p>", "links"=>[], "tags"=>["western-blot", "cytosolic", "fractions", "cells", "infected", "respective", "variants"], "article_id"=>399538, "categories"=>["Biochemistry", "Chemistry"], "users"=>["Jan R. Kraehling", "Mareike Busker", "Tobias Haase", "Nadine Haase", "Markus Koglin", "Monika Linnenbaum", "Soenke Behrends"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025772.g002", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Characterization_of_expression_of_the_1_subunits_by_Western_blot_analysis_in_cytosolic_fractions_of_Sf_9_cells_infected_with_the_respective_variants_of_the_1_subunits_/399538", "title"=>"Characterization of expression of the α<sub>1</sub>-subunits by Western-blot analysis in cytosolic fractions of <i>Sf-</i>9 cells infected with the respective variants of the α<sub>1</sub>-subunits.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-30 02:38:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/729511"], "description"=>"<p>50 µg Cytosol of cytosolic fraction or 5 µg of purified enzyme was electrophoretically separated by SDS-PAGE and stained with Coomassie Blue (a representative gel is shown). Lane A, cytosolic fraction of C-α<sub>1</sub>/β<sub>1</sub><i>S</i> expressed <u>without</u> heme-supplement and <u>without</u> lipid medium supplement. Lane B, purified C-α<sub>1</sub>/β<sub>1</sub><i>S</i> expressed <u>without</u> heme-supplement and <u>without</u> lipid medium supplement. Lane C, cytosolic fraction of C-α<sub>1</sub>/β<sub>1</sub><i>S</i> expressed only <u>with</u> heme-supplement and <u>without</u> lipid medium supplement. Lane D, purified C-α<sub>1</sub>/β<sub>1</sub><i>S</i> expressed <u>with</u> heme-supplement and <u>without</u> lipid medium supplement. Lane E, cytosolic fraction of C-α<sub>1</sub>/β<sub>1</sub><i>S</i> expressed only <u>with</u> heme-supplement and <u>with</u> lipid medium supplement. Lane F, purified C-α<sub>1</sub>/β<sub>1</sub><i>S</i> expressed <u>with</u> heme-supplement and <u>with</u> lipid medium supplement.</p>", "links"=>[], "tags"=>["staining", "cytosolic", "fractions", "purified"], "article_id"=>399871, "categories"=>["Biochemistry", "Chemistry"], "users"=>["Jan R. Kraehling", "Mareike Busker", "Tobias Haase", "Nadine Haase", "Markus Koglin", "Monika Linnenbaum", "Soenke Behrends"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025772.g005", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Coomassie_staining_of_cytosolic_fractions_and_purified_proteins_/399871", "title"=>"Coomassie staining of cytosolic fractions and purified proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-09-30 02:44:31"}

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Relative Metric

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