Lasp-1 Regulates Podosome Function
Publication Date
April 13, 2012
Journal
PLOS ONE
Authors
Miriam Stölting, Christiane Wiesner, Vanessa Van Vliet, Elke Butt, et al
Volume
7
Issue
4
Pages
e35340
DOI
https://dx.plos.org/10.1371/journal.pone.0035340
Publisher URL
http://journals.plos.org/plosone/article?id=10.1371%2Fjournal.pone.0035340
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/22514729
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3325968
Europe PMC
http://europepmc.org/abstract/MED/22514729
Web of Science
000305341600134
Scopus
84865595187
Mendeley
http://www.mendeley.com/research/lasp1-regulates-podosome-function
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Mendeley | Further Information

{"title"=>"Lasp-1 regulates podosome function", "type"=>"journal", "authors"=>[{"first_name"=>"Miriam", "last_name"=>"Stölting", "scopus_author_id"=>"26633329300"}, {"first_name"=>"Christiane", "last_name"=>"Wiesner", "scopus_author_id"=>"36571255100"}, {"first_name"=>"Vanessa", "last_name"=>"van Vliet", "scopus_author_id"=>"33768107600"}, {"first_name"=>"Elke", "last_name"=>"Butt", "scopus_author_id"=>"7003685904"}, {"first_name"=>"Hermann", "last_name"=>"Pavenstädt", "scopus_author_id"=>"7006903867"}, {"first_name"=>"Stefan", "last_name"=>"Linder", "scopus_author_id"=>"13605355500"}, {"first_name"=>"Joachim", "last_name"=>"Kremerskothen", "scopus_author_id"=>"6603093862"}], "year"=>2012, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "arxiv"=>"1203.2655", "scopus"=>"2-s2.0-84859712356", "sgr"=>"84859712356", "pui"=>"364617604", "isbn"=>"0011-3891", "pmid"=>"22514729", "doi"=>"10.1371/journal.pone.0035340"}, "id"=>"69accecb-ffc3-326c-88ae-c0e7e03919ca", "abstract"=>"Eukaryotic cells form a variety of adhesive structures to connect with their environment and to regulate cell motility. In contrast to classical focal adhesions, podosomes, highly dynamic structures of different cell types, are actively engaged in matrix remodelling and degradation. Podosomes are composed of an actin-rich core region surrounded by a ring-like structure containing signalling molecules, motor proteins as well as cytoskeleton-associated proteins. Lasp-1 is a ubiquitously expressed, actin-binding protein that is known to regulate cytoskeleton architecture and cell migration. This multidomain protein is predominantely present at focal adhesions, however, a second pool of Lasp-1 molecules is also found at lamellipodia and vesicle-like microdomains in the cytosol.In this report, we show that Lasp-1 is a novel component and regulator of podosomes. Immunofluorescence studies reveal a localization of Lasp-1 in the podosome ring structure, where it colocalizes with zyxin and vinculin. Life cell imaging experiments demonstrate that Lasp-1 is recruited in early steps of podosome assembly. A siRNA-mediated Lasp-1 knockdown in human macrophages affects podosome dynamics as well as their matrix degradation capacity. In summary, our data indicate that Lasp-1 is a novel component of podosomes and is involved in the regulation of podosomal function.", "link"=>"http://www.mendeley.com/research/lasp1-regulates-podosome-function", "reader_count"=>19, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>8, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>5, "Student > Postgraduate"=>2, "Student > Master"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>8, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>5, "Student > Postgraduate"=>2, "Student > Master"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>4, "Agricultural and Biological Sciences"=>9, "Medicine and Dentistry"=>1, "Neuroscience"=>1, "Physics and Astronomy"=>1, "Immunology and Microbiology"=>2}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Neuroscience"=>{"Neuroscience"=>1}, "Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>9}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>4}, "Unspecified"=>{"Unspecified"=>1}}, "reader_count_by_country"=>{"Netherlands"=>1, "Germany"=>1}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/654026"], "description"=>"<p>Primary human macrophages were treated with Lasp-1-specific siRNA (Oligo A or C) or control siRNA. (<b>A</b>) Examples for podosome dynamics included in the analysis. Shown are single podosomes of cells co-transfected with siRNA and Lifeact-TagGFP2. Podosome lifetime is defined as 1) appearance to dissolution, 2) appearance to fission, or 3) fusion to dissolution. (<b>B–D</b>) Measurement of podosome lifetime from cells treated with Lasp-1-specific siRNA, compared to controls. Double asterisks indicate values highly significant different from controls with <i>P</i><0.004 (means+SD, n = 3×4) (B). (C, D) Graph showing detailed podosome lifetime analysis, data from (B), of cells transfected with Lasp-1-specific siRNA (Oligo A (C; purple); Oligo C (D; brown), compared to controls (C, D; grey; (means+SE; n = 3×4;)).</p>", "links"=>[], "tags"=>["altered", "lasp-1", "knockdown"], "article_id"=>324512, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Miriam Stölting", "Christiane Wiesner", "Vanessa van Vliet", "Elke Butt", "Hermann Pavenstädt", "Stefan Linder", "Joachim Kremerskothen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0035340.g005", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Podosome_lifetime_is_altered_in_Lasp_1_knockdown_macrophages_/324512", "title"=>"Podosome lifetime is altered in Lasp-1 knockdown macrophages.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-04-13 01:15:12"}
  • {"files"=>["https://ndownloader.figshare.com/files/654200"], "description"=>"<p><b>A</b>) Confocal micrographs of macrophages transfected with control siRNA or siRNAs (Oligo A or C) specific for human Lasp-1, and seeded on rhodamine-labeled gelatin (red). Cells were fixed after 6 h and stained with Cy5-phalloidin for F-actin (blue). Matrix degradation is visible as dark areas by concomitant loss of the fluorescent label. White bars represent 10 µm. (<b>B</b>) Statistical quantification of matrix degradation in cells treated with control siRNA or siRNAs specific for Lasp-1. Measurement of the fluorescence intensity of the degraded area was used to evaluate the degree of degradation. Complete absence of signal was set as 100% degradation and the evaluated cells were scored into groups depending on the degree of matrix degradation (0%–25%; 26%–100%). Single asterisks indicate values significantly different from control with a <i>P</i> value<0.05 (means with n = 3×30).</p>", "links"=>[], "tags"=>["lasp-1", "impairs", "matrix", "degradation", "podosomes"], "article_id"=>324684, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Miriam Stölting", "Christiane Wiesner", "Vanessa van Vliet", "Elke Butt", "Hermann Pavenstädt", "Stefan Linder", "Joachim Kremerskothen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0035340.g006", "stats"=>{"downloads"=>1, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Knockdown_of_Lasp_1_impairs_the_matrix_degradation_capacity_of_podosomes_from_human_macrophages_/324684", "title"=>"Knockdown of Lasp-1 impairs the matrix degradation capacity of podosomes from human macrophages.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-04-13 01:18:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/653709"], "description"=>"<p>(<b>A</b>) Colocalization of recombinant EGFP-Lasp-1 and recombinant mRFP-actin at podosomes in PDBu-treated A7r5 cells. The white box marks the enlargement shown in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0035340#pone-0035340-g003\" target=\"_blank\">Fig. 3B</a>. Bar represents 25 µm. (<b>B</b>) Appearance of EGFP-Lasp-1 during assembly and disassembly of podosomes (white boxes) in PDBu-treated cells over a period of 4 min. Inserts in the pictures taken at 0 s, 2 min. and 4 min. show the merged EGFP-Lasp-1 (green) and mRFP-actin (red) signals in two individual podosomes. Bar represents 2 µm. (<b>C</b>) Colocalization of EGFP-Lasp-1 (upper row) and DsRed-cortactin (middle row, merged pictures in the lower row) during initial stages of podosome assembly in PDBu-treated A7r5 cells over a period of 2 min. An individual podosome is marked by a red circle. Bars represent 25 µm (left panel) or 2 µm (right panels), respectively.</p>", "links"=>[], "tags"=>["recruitment", "stages", "podosome"], "article_id"=>324195, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Miriam Stölting", "Christiane Wiesner", "Vanessa van Vliet", "Elke Butt", "Hermann Pavenstädt", "Stefan Linder", "Joachim Kremerskothen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0035340.g003", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Lasp_1_recruitment_is_associated_with_early_stages_of_podosome_biogenesis_/324195", "title"=>"Lasp-1 recruitment is associated with early stages of podosome biogenesis.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-04-13 01:09:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/653883"], "description"=>"<p>Primary human macrophages were treated with control siRNA or Lasp-1 specific siRNA (Oligo A or C). (<b>A–C</b>) Podosome-covered area was analyzed by life cell imaging, with example shown in (A). Pictures were taken every 30 sec. over 30 min. (n = 3×4 cells). Average area per cell was set at 100%. Values were plotted as box graphs, with whiskers from 1–99% (B). Note higher variability of podosome-covered areas in cells treated with Lasp-1-specific siRNA. (C) Measured cell size from cells used in (B). (means+SD; ns = not significant). (<b>D–G</b>) Diameter of the podosome cores (D, E) and number of podosomes per cell (F, G) were evaluated from cells treated with Lasp-1-specific siRNA (Oligo A (D, F; purple); Oligo C (E,G; brown)) or control siRNA (grey). Insets (d, e) show details taken from graph (means ±SE, n = 3×8 (D, E); means±SE n = 3×56 (F, G)).</p>", "links"=>[], "tags"=>["sirna-mediated", "knockdown", "lasp-1", "podosome", "numbers"], "article_id"=>324366, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Miriam Stölting", "Christiane Wiesner", "Vanessa van Vliet", "Elke Butt", "Hermann Pavenstädt", "Stefan Linder", "Joachim Kremerskothen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0035340.g004", "stats"=>{"downloads"=>1, "page_views"=>20, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Impact_of_a_siRNA_mediated_knockdown_of_Lasp_1_on_podosome_numbers_and_structure_in_macrophages_/324366", "title"=>"Impact of a siRNA-mediated knockdown of Lasp-1 on podosome numbers and structure in macrophages.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-04-13 01:12:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/336383", "https://ndownloader.figshare.com/files/336470", "https://ndownloader.figshare.com/files/336540", "https://ndownloader.figshare.com/files/336607", "https://ndownloader.figshare.com/files/336712", "https://ndownloader.figshare.com/files/336780"], "description"=>"<div><p>Eukaryotic cells form a variety of adhesive structures to connect with their environment and to regulate cell motility. In contrast to classical focal adhesions, podosomes, highly dynamic structures of different cell types, are actively engaged in matrix remodelling and degradation. Podosomes are composed of an actin-rich core region surrounded by a ring-like structure containing signalling molecules, motor proteins as well as cytoskeleton-associated proteins.</p> <p>Lasp-1 is a ubiquitously expressed, actin-binding protein that is known to regulate cytoskeleton architecture and cell migration. This multidomain protein is predominantely present at focal adhesions, however, a second pool of Lasp-1 molecules is also found at lamellipodia and vesicle-like microdomains in the cytosol.</p> <p>In this report, we show that Lasp-1 is a novel component and regulator of podosomes. Immunofluorescence studies reveal a localization of Lasp-1 in the podosome ring structure, where it colocalizes with zyxin and vinculin. Life cell imaging experiments demonstrate that Lasp-1 is recruited in early steps of podosome assembly. A siRNA-mediated Lasp-1 knockdown in human macrophages affects podosome dynamics as well as their matrix degradation capacity. In summary, our data indicate that Lasp-1 is a novel component of podosomes and is involved in the regulation of podosomal function.</p> </div>", "links"=>[], "tags"=>["lasp-1", "regulates", "podosome"], "article_id"=>126483, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Miriam Stölting", "Christiane Wiesner", "Vanessa van Vliet", "Elke Butt", "Hermann Pavenstädt", "Stefan Linder", "Joachim Kremerskothen"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0035340.s001", "https://dx.doi.org/10.1371/journal.pone.0035340.s002", "https://dx.doi.org/10.1371/journal.pone.0035340.s003", "https://dx.doi.org/10.1371/journal.pone.0035340.s004", "https://dx.doi.org/10.1371/journal.pone.0035340.s005", "https://dx.doi.org/10.1371/journal.pone.0035340.s006"], "stats"=>{"downloads"=>8, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Lasp_1_Regulates_Podosome_Function/126483", "title"=>"Lasp-1 Regulates Podosome Function", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-04-13 01:48:03"}
  • {"files"=>["https://ndownloader.figshare.com/files/653370"], "description"=>"<p>(<b>A, B</b>) Confocal micrographs of primary human macrophages transfected with constructs encoding (A) EGFP-Lasp-1 and (B) EYFP-Vinculin (green), respectively, and stained with vinculin- or Lasp-1-specific antibodies (with Alexa488- or Alexa 568-conjugated secondary antibody) for endogenous vinculin or Lasp-1, respectively, and Cy5-conjugated phalloidin for F-actin (blue). White box indicates detail images below. Bars represent 10 µm. (<b>C, D</b>) 3D reconstruction of single podosomes of primary human macrophages. Left panels: xyz mode, right panels: xzy mode for the same podosome. (C) Cells were transfected with EGFP-Lasp-1 and stained with Alexa568-phalloidin for F-actin (podosome core) or vinculin-specific antibody (with Alexa568-labeled secondary antibody) for vinculin (podosome ring structure; red). (D) Both untransfected cells (stained with Alexa488-phalloidin for F-actin; green) and cells transfected with EYFP-vinculin (green) were stained with Lasp-1-specific antibody (with Alexa568-labeled secondary antibody) for endogenous Lasp-1 (red). (<b>E</b>) Confocal micrographs of a rat smooth muscle cell (A7r5), stained with Alexa-594 phalloidin for F-actin (red, upper panel) or zyxin-specific antibody (with Alexa594-labeled secondary antibody) for endogenous zyxin (red, lower panel) and co-stained with Lasp-1-specific antibody (with Alexa488-labeled secondary antibody) for endogenous Lasp-1 (green). Lasp-1 and its binding partner zyxin colocalize at F-actin-rich podosomes (merge) in PDBu-treated A7r5 cells. Bars represent 25 µm.</p>", "links"=>[], "tags"=>["podosome"], "article_id"=>323858, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Miriam Stölting", "Christiane Wiesner", "Vanessa van Vliet", "Elke Butt", "Hermann Pavenstädt", "Stefan Linder", "Joachim Kremerskothen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0035340.g001", "stats"=>{"downloads"=>2, "page_views"=>26, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Lasp_1_is_a_component_of_the_podosome_ring_structure_/323858", "title"=>"Lasp-1 is a component of the podosome ring structure.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-04-13 01:04:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/653552"], "description"=>"<p>(<b>A</b>) Domain structure of Lasp-1 comprising an aminoterminal LIM domain, two nebulin (NEBU) repeats and an adjacent Linker region mediating actin binding, and a carboxyterminal SH3 (Src homology 3) domain that binds zyxin and palladin (N = aminoterminus, C = carboxyterminus). (<b>B</b>) Confocal micrographs of primary human macrophages transfected with EGFP-Lasp-1 deletion constructs (green) and stained with vinculin-specific antibody (with Alexa568-conjugated secondary antibody) for vinculin (red) and Cy5- phalloidin for F-actin. Constructs include EGFP-Lasp-1 wildtype (wt), EGFP-Lasp-1ΔLIM (lacking the LIM domain), EGFP-Lasp-1ΔSH3 (lacking the SH3 domain), and EGFP-Lasp-1ΔN-L (lacking the NEBU repeats and the Linker region). White boxes indicate detail images below. Bars represent 10 µm.</p>", "links"=>[], "tags"=>["mutants", "lacking", "lim", "nebu", "repeats", "linker", "sh3", "localized"], "article_id"=>324031, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Miriam Stölting", "Christiane Wiesner", "Vanessa van Vliet", "Elke Butt", "Hermann Pavenstädt", "Stefan Linder", "Joachim Kremerskothen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0035340.g002", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Lasp_1_mutants_lacking_either_the_LIM_domain_the_NEBU_repeats_and_the_Linker_region_or_the_SH3_domain_are_still_localized_at_podosomes_/324031", "title"=>"Lasp-1 mutants lacking either the LIM domain, the NEBU repeats and the Linker region, or the SH3 domain are still localized at podosomes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-04-13 01:07:11"}

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