Kindlin-1 Regulates Integrin Dynamics and Adhesion Turnover
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{"title"=>"Kindlin-1 Regulates Integrin Dynamics and Adhesion Turnover", "type"=>"journal", "authors"=>[{"first_name"=>"Coert", "last_name"=>"Margadant", "scopus_author_id"=>"9737505800"}, {"first_name"=>"Maaike", "last_name"=>"Kreft", "scopus_author_id"=>"7004901549"}, {"first_name"=>"Giovanna", "last_name"=>"Zambruno", "scopus_author_id"=>"7004942362"}, {"first_name"=>"Arnoud", "last_name"=>"Sonnenberg", "scopus_author_id"=>"7202880655"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "pui"=>"369102094", "doi"=>"10.1371/journal.pone.0065341", "sgr"=>"84878925241", "scopus"=>"2-s2.0-84878925241", "pmid"=>"23776470"}, "id"=>"b727abf3-0818-38ba-b5ef-19b64e4807c3", "abstract"=>"Loss-of-function mutations in the gene encoding the integrin co-activator kindlin-1 cause Kindler syndrome. We report a novel kindlin-1-deficient keratinocyte cell line derived from a Kindler syndrome patient. Despite the expression of kindlin-2, the patient's cells display several hallmarks related to reduced function of β1 integrins, including abnormal cell morphology, cell adhesion, cell spreading, focal adhesion assembly, and cell migration. Defective cell adhesion was aggravated by kindlin-2 depletion, indicating that kindlin-2 can compensate to a certain extent for the loss of kindlin-1. Intriguingly, β1 at the cell-surface was aberrantly glycosylated in the patient's cells, and its expression was considerably reduced, both in cells in vitro and in the patient's epidermis. Reconstitution with wild-type kindlin-1 but not with a β1-binding defective mutant restored the aberrant β1 expression and glycosylation, and normalized cell morphology, adhesion, spreading, and migration. Furthermore, the expression of wild-type kindlin-1, but not of the integrin-binding-defective mutant, increased the stability of integrin-mediated cell-matrix adhesions and enhanced the redistribution of internalized integrins to the cell surface. Thus, these data uncover a role for kindlin-1 in the regulation of integrin trafficking and adhesion turnover.", "link"=>"http://www.mendeley.com/research/kindlin1-regulates-integrin-dynamics-adhesion-turnover", "reader_count"=>31, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Librarian"=>1, "Researcher"=>6, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>10, "Other"=>1, "Student > Master"=>3, "Student > Bachelor"=>5, "Professor"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Librarian"=>1, "Researcher"=>6, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>10, "Other"=>1, "Student > Master"=>3, "Student > Bachelor"=>5, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>3, "Biochemistry, Genetics and Molecular Biology"=>6, "Agricultural and Biological Sciences"=>16, "Medicine and Dentistry"=>2, "Design"=>1, "Pharmacology, Toxicology and Pharmaceutical Science"=>1, "Chemistry"=>1, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Design"=>{"Design"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Chemistry"=>{"Chemistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>16}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>6}, "Unspecified"=>{"Unspecified"=>3}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>1}}, "reader_count_by_country"=>{"United States"=>1, "United Kingdom"=>2, "Germany"=>1}, "group_count"=>3}

Scopus | Further Information

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Figshare

  • {"files"=>["https://s3-eu-west-1.amazonaws.com/pstorage-plos-3567654/1082362/Figure_1.tif"], "description"=>"<p><b>A</b>) Schematic representation of the <i>KIND1</i> gene (top), indicating the position of the c.1161delA mutation, and kindlin-1 protein (bottom). Exons are represented by boxes, introns are not to scale. <b>B</b>) Western blot showing the expression of kindlin-1 and kindlin-2 in NHK and KS cells. <b>C</b>) Phase/contrast images of NHK and KS cells. Bar, 20 µm. <b>D</b>) Adhesion of KS cells to Col-1 and Ln-332, expressed relative to that of NHK. Shown are the averages ±SEM from 3 independent experiments. <b>E</b>) Cell spreading of NHK and KS cells on Col-1. Shown are the averages ±SEM from 3 independent experiments. <b>F</b>) Rose-plots depicting migration tracks of NHK and KS cells. <b>G</b>) Quantification of the velocity of cell migration (Bars represent averages ±SEM from ∼250 cells out of 3 experiments). <b>H</b>) Confocal images of FAs, visualized using an antibody against P(Y) (green), and F-actin (red). Scale bar, 10 µm.</p>", "links"=>[], "tags"=>["Biochemistry", "cytochemistry", "Extracellular matrix", "Extracellular matrix adhesions", "integrins", "developmental biology", "Molecular development", "Adhesion molecules", "histology", "Molecular cell biology", "cell adhesion", "dermatology", "ks"], "article_id"=>717007, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Coert Margadant", "Maaike Kreft", "Giovanna Zambruno", "Arnoud Sonnenberg"], "doi"=>["http://dx.doi.org/10.1371/journal.pone.0065341.g001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"http://figshare.com/articles/_Abnormalities_in_KS_cells_/717007", "title"=>"Abnormalities in KS cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-11 01:56:47"}
  • {"files"=>["https://s3-eu-west-1.amazonaws.com/pstorage-plos-3567654/1082363/Figure_2.tif"], "description"=>"<p><b>A</b>) FACS histograms (top) and quantification (bottom; average ±SEM from 3 independent experiments) of NHK and KS cells showing cell-surface expression of β1 (left) and active β1 (right), as measured by 9EG7 staining. AU, arbitrary units. <b>B</b>) Western blot showing the precursor β1 (110 kDa) and the mature form of β1 (130 kDa) in NHK and KS cells. <b>C</b>) Expression of β1 (green) and Ln-332 (red) in the skin of an unaffected individual (normal) and the KS patient. The upper border of the epidermis is indicated with a white line. Bar, 50 µm. d; dermis, e; epidermis. <b>D</b>) Depletion of kindlin-2 causes detachment of KS cells. The numbers above the blot indicate the normalized kindlin-2 expression in the remaining (attached) cells, relative to that in untreated cells. Bar, 20 µm. <b>E</b>) Expression of kindlin-1 (top) and kindlin-2 (bottom) in the skin. Bar, 50 µm. d; dermis, e; epidermis.</p>", "links"=>[], "tags"=>["Biochemistry", "cytochemistry", "Extracellular matrix", "Extracellular matrix adhesions", "integrins", "developmental biology", "Molecular development", "Adhesion molecules", "histology", "Molecular cell biology", "cell adhesion", "dermatology", "integrin"], "article_id"=>717008, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Coert Margadant", "Maaike Kreft", "Giovanna Zambruno", "Arnoud Sonnenberg"], "doi"=>["http://dx.doi.org/10.1371/journal.pone.0065341.g002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"http://figshare.com/articles/_Decreased_integrin_expression_in_the_absence_of_kindlin_1_/717008", "title"=>"Decreased integrin expression in the absence of kindlin-1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-11 01:56:48"}
  • {"files"=>["https://s3-eu-west-1.amazonaws.com/pstorage-plos-3567654/1082364/Figure_3.tif"], "description"=>"<p><b>A</b>) Western blot showing expression of eGFP-kindlin-1 in KS and KSK cells. <b>B</b>) Morphology of KS and KSK cells. Bar, 20 µm. <b>C</b>) Proliferation of KS and KSK cells. Shown are the averages ±SEM from 3 independent experiments. <b>D</b>) eGFP-kindlin-1 (green), FAs (blue) and F-actin (red) in KSK cells. Bar, 5 µm. <b>E</b>) Cell adhesion to Col-1 and Ln-332 in KS and KSK cells. Bars represent averages ±SEM of 3 independent experiments. AU, arbitrary units. <b>F</b>) Number of KS and KSK cells spread on Ln-332 and Col-1. Shown are the average values ±SEM from ∼500 cells out of a representative experiment. <b>G</b>) Surface area of KS and KSK cells on Ln-332 and Col-1. Shown are the averages ±SEM from ∼500 cells of a representative experiment. <b>H</b>) Rose-plots depicting migration tracks of KS and KSK cells generated by time-lapse video microscopy. <b>I</b>) Quantification of the velocity of cell migration (average ±SEM from ∼300 cells out of 3 experiments). <b>J</b>) FACS histograms of NHK and KS cells showing β1 cell-surface expression (left) and quantification (average ±SEM from 3 independent experiments) (right). AU, arbitrary units.</p>", "links"=>[], "tags"=>["Biochemistry", "cytochemistry", "Extracellular matrix", "Extracellular matrix adhesions", "integrins", "developmental biology", "Molecular development", "Adhesion molecules", "histology", "Molecular cell biology", "cell adhesion", "dermatology", "kindlin-1", "ks"], "article_id"=>717009, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Coert Margadant", "Maaike Kreft", "Giovanna Zambruno", "Arnoud Sonnenberg"], "doi"=>["http://dx.doi.org/10.1371/journal.pone.0065341.g003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"http://figshare.com/articles/_Re_expression_of_kindlin_1_in_KS_cells_/717009", "title"=>"Re-expression of kindlin-1 in KS cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-11 01:56:49"}
  • {"files"=>["https://s3-eu-west-1.amazonaws.com/pstorage-plos-3567654/1082365/Figure_4.tif"], "description"=>"<p><b>A</b>) Schematic representation of full-length kindlin-1 (top) and kindlin-1<sup>del581</sup> (bottom). <b>B</b>) Expression of full-length eGFP-kindlin-1 and eGFP-kindlin-1<sup>del581</sup> in KSK and KSK<sup>del581</sup> cells. <b>C</b>) Expression of precursor β1 (110 kDa) and mature β1 (130 kDa) in KS, KSK, and KSK<sup>del581</sup> cells. Expression of mature β1 was quantified by densitometry, normalized to actin, and expressed relative to the expression in KSK cells. Shown are the values acquired from a representative blot. <b>D</b>) Immunoprecipitated β1 was treated with neuraminidase (NANase) and analyzed by Western blotting. <b>E</b>) FACS histograms (left) and averages ±SEM quantified from 3 independent experiments (right) of β1 cell-surface expression in KS, KSK, KSK<sup>del581</sup>, and NHK, expressed relative to that in KS. <b>F</b>) Phase-contrast images of KS, KSK, KSK<sup>del581</sup> and NHK on Col-1 (left), and average surface area ±SEM of KS, KSK, KSK<sup>del581</sup> and NHK cells (quantified from ∼250 cells from a representative experiment) (right). Bar, 10 µm. <b>G</b>) Subcellular distribution of eGFP-kindlin-1 and eGFP-kindlin-1<sup>del581</sup> (green). FAs (blue), F-actin (red). Bar, 5 µm.</p>", "links"=>[], "tags"=>["Biochemistry", "cytochemistry", "Extracellular matrix", "Extracellular matrix adhesions", "integrins", "developmental biology", "Molecular development", "Adhesion molecules", "histology", "Molecular cell biology", "cell adhesion", "dermatology", "spreading", "kindlin-1", "f3"], "article_id"=>717010, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Coert Margadant", "Maaike Kreft", "Giovanna Zambruno", "Arnoud Sonnenberg"], "doi"=>["http://dx.doi.org/10.1371/journal.pone.0065341.g004"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"http://figshare.com/articles/_Regulation_of_946_1_expression_and_cell_spreading_by_kindlin_1_require_the_F3_domain_/717010", "title"=>"Regulation of β1 expression and cell spreading by kindlin-1 require the F3 domain.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-11 01:56:50"}
  • {"files"=>["https://s3-eu-west-1.amazonaws.com/pstorage-plos-3567654/1082367/Figure_5.tif"], "description"=>"<p><b>A</b>) Stills from a TIRF movie, showing the dynamics of mCherry-vinculin in KS cells. <b>B</b>) Dynamics of mCherry-vinculin (top), and eGFP-kindlin-1 (bottom) in KSK cells. <b>C</b>) Dynamics of mCherry-vinculin (top), and eGFP-kindlin-1 (bottom) in KSK<sup>del581</sup> cells. Look-up table ‘fire’ was used to enhance visibility of adhesions. Shown are images at 0, 7.5, 15, 22.5, and 30 min. Boxed regions are enlarged. Arrows indicate retraction fibers. Bar, 10 µm.</p>", "links"=>[], "tags"=>["Biochemistry", "cytochemistry", "Extracellular matrix", "Extracellular matrix adhesions", "integrins", "developmental biology", "Molecular development", "Adhesion molecules", "histology", "Molecular cell biology", "cell adhesion", "dermatology", "targeting", "adhesions", "adhesion", "f3"], "article_id"=>717011, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Coert Margadant", "Maaike Kreft", "Giovanna Zambruno", "Arnoud Sonnenberg"], "doi"=>["http://dx.doi.org/10.1371/journal.pone.0065341.g005"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"http://figshare.com/articles/_Kindlin_1_targeting_to_adhesions_and_adhesion_stability_depend_on_the_F3_domain_/717011", "title"=>"Kindlin-1 targeting to adhesions and adhesion stability depend on the F3 domain.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-11 01:56:51"}
  • {"files"=>["https://s3-eu-west-1.amazonaws.com/pstorage-plos-3567654/1082369/Figure_6.tif"], "description"=>"<p>Cell-surface β1 integrins on KS, KSK, and KSK<sup>del581</sup> cells were labelled with DyLight 649-conjugated K-20 at 4°C (top panel), after which they were allowed to internalize in serum-free medium at 37°C for 2 hrs (middle panel). Recycling of the internal pool was induced with 20% FCS for 7.5 min (bottom panel). Cells were then fixed and processed for confocal microscopy. β1 is pseudo-colored green, nuclei were counterstained with DAPI (pseudocolored red). Arrows indicate delivery of recycled β1 to adhesions. Percentages of cells with recycled integrins are shown (from ∼120 cells out of 3 independent experiments). Bar, 10 µm.</p>", "links"=>[], "tags"=>["Biochemistry", "cytochemistry", "Extracellular matrix", "Extracellular matrix adhesions", "integrins", "developmental biology", "Molecular development", "Adhesion molecules", "histology", "Molecular cell biology", "cell adhesion", "dermatology", "regulates", "integrin"], "article_id"=>717012, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Coert Margadant", "Maaike Kreft", "Giovanna Zambruno", "Arnoud Sonnenberg"], "doi"=>["http://dx.doi.org/10.1371/journal.pone.0065341.g006"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"http://figshare.com/articles/_Kindlin_1_interaction_with_946_1_regulates_integrin_trafficking_/717012", "title"=>"Kindlin-1 interaction with β1 regulates integrin trafficking.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-06-11 01:56:52"}
  • {"files"=>["https://s3-eu-west-1.amazonaws.com/pstorage-plos-3567654/1082372/Figure_S1.tif", "https://s3-eu-west-1.amazonaws.com/pstorage-plos-3567654/1082374/Figure_S2.tif", "https://s3-eu-west-1.amazonaws.com/pstorage-plos-3567654/1082375/Figure_S3.tif", "https://s3-eu-west-1.amazonaws.com/pstorage-plos-3567654/1082377/Movie_S1.avi", "https://s3-eu-west-1.amazonaws.com/pstorage-plos-3567654/1082378/Movie_S2.avi", "https://s3-eu-west-1.amazonaws.com/pstorage-plos-3567654/1082379/Movie_S3.avi"], "description"=>"<div><p>Loss-of-function mutations in the gene encoding the integrin co-activator kindlin-1 cause Kindler syndrome. We report a novel kindlin-1-deficient keratinocyte cell line derived from a Kindler syndrome patient. Despite the expression of kindlin-2, the patient’s cells display several hallmarks related to reduced function of β1 integrins, including abnormal cell morphology, cell adhesion, cell spreading, focal adhesion assembly, and cell migration. Defective cell adhesion was aggravated by kindlin-2 depletion, indicating that kindlin-2 can compensate to a certain extent for the loss of kindlin-1. Intriguingly, β1 at the cell-surface was aberrantly glycosylated in the patient’s cells, and its expression was considerably reduced, both in cells <i>in vitro</i> and in the patient’s epidermis. Reconstitution with wild-type kindlin-1 but not with a β1-binding defective mutant restored the aberrant β1 expression and glycosylation, and normalized cell morphology, adhesion, spreading, and migration. Furthermore, the expression of wild-type kindlin-1, but not of the integrin-binding-defective mutant, increased the stability of integrin-mediated cell-matrix adhesions and enhanced the redistribution of internalized integrins to the cell surface. Thus, these data uncover a role for kindlin-1 in the regulation of integrin trafficking and adhesion turnover.</p></div>", "links"=>[], "tags"=>["Biochemistry", "cytochemistry", "Extracellular matrix", "Extracellular matrix adhesions", "integrins", "developmental biology", "Molecular development", "Adhesion molecules", "histology", "Molecular cell biology", "cell adhesion", "dermatology", "regulates", "integrin", "adhesion"], "article_id"=>717013, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Coert Margadant", "Maaike Kreft", "Giovanna Zambruno", "Arnoud Sonnenberg"], "doi"=>["http://dx.doi.org/10.1371/journal.pone.0065341"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"http://figshare.com/articles/_Kindlin_1_Regulates_Integrin_Dynamics_and_Adhesion_Turnover_/717013", "title"=>"Kindlin-1 Regulates Integrin Dynamics and Adhesion Turnover", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2013-06-11 01:56:53"}

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Relative Metric

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