Human Cataract Mutations in EPHA2 SAM Domain Alter Receptor Stability and Function
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{"title"=>"Human cataract mutations in EPHA2 SAM domain alter receptor stability and function", "type"=>"journal", "authors"=>[{"first_name"=>"Jeong Eun", "last_name"=>"Park", "scopus_author_id"=>"55204398300"}, {"first_name"=>"Alexander I.", "last_name"=>"Son", "scopus_author_id"=>"54996428600"}, {"first_name"=>"Rui", "last_name"=>"Hua", "scopus_author_id"=>"26643924500"}, {"first_name"=>"Lianqing", "last_name"=>"Wang", "scopus_author_id"=>"54964542600"}, {"first_name"=>"Xue", "last_name"=>"Zhang", "scopus_author_id"=>"20336388600"}, {"first_name"=>"Renping", "last_name"=>"Zhou", "scopus_author_id"=>"7401567180"}], "year"=>2012, "source"=>"PLoS ONE", "identifiers"=>{"scopus"=>"2-s2.0-84860531878", "sgr"=>"84860531878", "issn"=>"19326203", "doi"=>"10.1371/journal.pone.0036564", "pmid"=>"22570727", "pui"=>"364730453"}, "id"=>"1e586886-18ac-30bf-964d-365288fce2e6", "abstract"=>"The cellular and molecular mechanisms underlying the pathogenesis of cataracts leading to visual impairment remain poorly understood. In recent studies, several mutations in the cytoplasmic sterile-α-motif (SAM) domain of human EPHA2 on chromosome 1p36 have been associated with hereditary cataracts in several families. Here, we have investigated how these SAM domain mutations affect EPHA2 activity. We showed that the SAM domain mutations dramatically destabilized the EPHA2 protein in a proteasome-dependent pathway, as evidenced by the increase of EPHA2 receptor levels in the presence of the proteasome inhibitor MG132. In addition, the expression of wild-type EPHA2 promoted the migration of the mouse lens epithelial αTN4-1 cells in the absence of ligand stimulation, whereas the mutants exhibited significantly reduced activity. In contrast, stimulation of EPHA2 with its ligand ephrin-A5 eradicates the enhancement of cell migration accompanied by Akt activation. Taken together, our studies suggest that the SAM domain of the EPHA2 protein plays critical roles in enhancing the stability of EPHA2 by modulating the proteasome-dependent process. Furthermore, activation of Akt switches EPHA2 from promoting to inhibiting cell migration upon ephrin-A5 binding. Our results provide the first report of multiple EPHA2 cataract mutations contributing to the destabilization of the receptor and causing the loss of cell migration activity.", "link"=>"http://www.mendeley.com/research/human-cataract-mutations-epha2-sam-domain-alter-receptor-stability-function", "reader_count"=>12, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Student > Doctoral Student"=>2, "Researcher"=>3, "Student > Ph. D. Student"=>4, "Student > Master"=>1, "Lecturer"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Student > Doctoral Student"=>2, "Researcher"=>3, "Student > Ph. D. Student"=>4, "Student > Master"=>1, "Lecturer"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>2, "Agricultural and Biological Sciences"=>4, "Medicine and Dentistry"=>2, "Chemistry"=>3, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Chemistry"=>{"Chemistry"=>3}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>4}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}}, "reader_count_by_country"=>{"United Kingdom"=>1, "Germany"=>1}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/331765", "https://ndownloader.figshare.com/files/331839", "https://ndownloader.figshare.com/files/331906", "https://ndownloader.figshare.com/files/331951", "https://ndownloader.figshare.com/files/332014"], "description"=>"<div><p>The cellular and molecular mechanisms underlying the pathogenesis of cataracts leading to visual impairment remain poorly understood. In recent studies, several mutations in the cytoplasmic sterile-α-motif (SAM) domain of human EPHA2 on chromosome 1p36 have been associated with hereditary cataracts in several families. Here, we have investigated how these SAM domain mutations affect EPHA2 activity. We showed that the SAM domain mutations dramatically destabilized the EPHA2 protein in a proteasome-dependent pathway, as evidenced by the increase of EPHA2 receptor levels in the presence of the proteasome inhibitor MG132. In addition, the expression of wild-type EPHA2 promoted the migration of the mouse lens epithelial αTN4-1 cells in the absence of ligand stimulation, whereas the mutants exhibited significantly reduced activity. In contrast, stimulation of EPHA2 with its ligand ephrin-A5 eradicates the enhancement of cell migration accompanied by Akt activation. Taken together, our studies suggest that the SAM domain of the EPHA2 protein plays critical roles in enhancing the stability of EPHA2 by modulating the proteasome-dependent process. Furthermore, activation of Akt switches EPHA2 from promoting to inhibiting cell migration upon ephrin-A5 binding. Our results provide the first report of multiple EPHA2 cataract mutations contributing to the destabilization of the receptor and causing the loss of cell migration activity.</p> </div>", "links"=>[], "tags"=>["cataract", "mutations", "epha2", "sam", "receptor"], "article_id"=>125509, "categories"=>["Physics", "Developmental Biology", "Medicine", "Immunology", "Molecular Biology", "Biophysics"], "users"=>["Jeong Eun Park", "Alexander I. Son", "Rui Hua", "Lianqing Wang", "Xue Zhang", "Renping Zhou"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0036564.s001", "https://dx.doi.org/10.1371/journal.pone.0036564.s002", "https://dx.doi.org/10.1371/journal.pone.0036564.s003", "https://dx.doi.org/10.1371/journal.pone.0036564.s004", "https://dx.doi.org/10.1371/journal.pone.0036564.s005"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Human_Cataract_Mutations_in_EPHA2_SAM_Domain_Alter_Receptor_Stability_and_Function/125509", "title"=>"Human Cataract Mutations in EPHA2 SAM Domain Alter Receptor Stability and Function", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-05-03 01:31:49"}
  • {"files"=>["https://ndownloader.figshare.com/files/642913"], "description"=>"<p>(<b>A</b>) Schematic diagram showing the domains of EPHA2 receptor and the locations of four SAM domain mutations found in human cataracts (c.2819C>T; c.2915_2916delTG; c.2826-9G>A; and c.2842G>T) in the EPHA2 gene. FN-III: fibronectin type-III domain; TM: transmembrane domain; Kinase: protein tyrosine kinase domain; SAM: sterile-α-motif domain; P: PDZ-binding motif. The SAM domain comprises 5 α-hecices (H1–5). (<b>B</b>) Reduction of mutant EPHA2 protein levels in transfected cells expressing <i>EPHA2</i> mutants. Protein levels of <i>EPHA2</i> mutants are decreased in both HEK293T and αTN4-1 cells. The blot was reprobed with anti-α-tubulin as a loading control. The graphs represent the quantification of relative band intensity of EphA2 as connected by the levels of α-tubulin from three independent experiments. Total EphA2 protein band intensity was determined using ImageJ software. Mean values are presented with S.D as indicated. Statistical differences between multiple groups were analyzed using one-way analysis of variance (ANOVA). ***, <i>P</i><0.001; **, <i>P</i><0.01; *, <i>P</i><0.05; and ns, not significant. Values of <i>P</i><0.05 were considered to be statistically significant. (<b>C, D</b>) No difference between wild-type and mutant <i>EPHA2</i> genes in transcription levels. (<b>C</b>) Semi-quantitative RT-PCR and (<b>D</b>) Real-time PCR for wild-type and mutant <i>EPHA2</i> genes were performed using total RNA, isolated from transfected HEK293T cells. GAPDH transcript levels are used as controls. The graphs represent the quantification of western blots from three independent experiments.</p>", "links"=>[], "tags"=>["cataract", "mutations", "sam"], "article_id"=>313399, "categories"=>["Physics", "Developmental Biology", "Medicine", "Immunology", "Molecular Biology", "Biophysics"], "users"=>["Jeong Eun Park", "Alexander I. Son", "Rui Hua", "Lianqing Wang", "Xue Zhang", "Renping Zhou"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0036564.g001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_EPHA2_cataract_mutations_in_the_SAM_domain_/313399", "title"=>"<i>EPHA2</i> cataract mutations in the SAM domain.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-03 00:56:39"}
  • {"files"=>["https://ndownloader.figshare.com/files/643025"], "description"=>"<p>EphA2 knockout MEF cells expressing wild-type or mutant <i>EPHA2</i> were incubated with clustered ephrin-A5-Fc before fixation and treated with anti-Fc antibodies (red). After washing with PBS, cells were counterstained with anti-EphA2 antibody (green). Images were captured using a Nikon Eclipse C1 confocal microscope. Scale bar, 50 µm.</p>", "links"=>[], "tags"=>["localization", "wild-type", "mutant", "receptors", "transfected", "mef"], "article_id"=>313507, "categories"=>["Physics", "Developmental Biology", "Medicine", "Immunology", "Molecular Biology", "Biophysics"], "users"=>["Jeong Eun Park", "Alexander I. Son", "Rui Hua", "Lianqing Wang", "Xue Zhang", "Renping Zhou"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0036564.g002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Subcellular_localization_of_the_wild_type_and_mutant_EPHA2_receptors_on_transfected_EphA2_8722_8722_MEF_E13_5_cells_/313507", "title"=>"Subcellular localization of the wild-type and mutant <i>EPHA2</i> receptors on transfected EphA2<sup>−/−</sup> MEF (E13.5) cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-03 00:58:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/643141"], "description"=>"<p>(<b>A</b>) Mutant EPHA2 proteins have a reduced half-life. HEK293T cells were treated for indicated time with the protein biosynthesis inhibitor CHX (50 µg/mL) or the proteasome inhibitor MG132 (10 µM). Cell lysates were immunoblotted with anti-EphA2 antibody. Lysates were resolved by SDS-PAGE and western blot analysis was performed using indicated antibodies as described in the <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0036564#s4\" target=\"_blank\">Materials and Methods</a>. The blot was reprobed with anti-α-tubulin as a loading control. (<b>B</b>) Quantification of EphA2 protein levels over time. Mean values are presented with S.D as indicated. (<b>C</b>) EPHA2 mutants have increased ubiquitination. Cells transfected with <i>EPHA2</i> and HA-tagged ubiquitin were treated with 10 µM MG132 for 6 hours, and were then lysed. Immunoprecipitated EphA2 was further analyzed with western blotting using anti-HA antibodies to detect ubiquitinated EphA2 as described in the <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0036564#s4\" target=\"_blank\">Materials and Methods</a>. The smear band is characteristic ubiquitin immunoreactivity. The amount of total EphA2 is shown as a loading control.</p>", "links"=>[], "tags"=>["degradation", "mediated", "proteasomal"], "article_id"=>313633, "categories"=>["Physics", "Developmental Biology", "Medicine", "Immunology", "Molecular Biology", "Biophysics"], "users"=>["Jeong Eun Park", "Alexander I. Son", "Rui Hua", "Lianqing Wang", "Xue Zhang", "Renping Zhou"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0036564.g003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_EPHA2_degradation_is_mediated_by_proteasomal_pathway_/313633", "title"=>"EPHA2 degradation is mediated by proteasomal pathway.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-03 01:00:33"}
  • {"files"=>["https://ndownloader.figshare.com/files/643249"], "description"=>"<p>(<b>A, B</b>) Ephrin-A5 ligand stimulates EPHA2 phosphorylation. HEK293T (<b>A</b>) and αTN4-1 (<b>B</b>) cells were grown to confluence and growth factor-starved for 24 hours. 2 µg/mL cross-linked ephrin-A5-Fc was then added to the starvation media and cell lysates were immunoblotted with indicated antibodies. Western blot analysis was performed as described in the <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0036564#s4\" target=\"_blank\">Materials and Methods</a>. The blot was reprobed with anti-α-tubulin as a loading control. (<b>C</b>) The ratios of levels of phospho-EphA2 to total EphA2 are similar between the wild-type and mutant EPHA2 proteins. The graphs show total band intensity of anti-phospho-EphA2 immunoblot to total EphA2 and represent the average of three independent experiments. Quantification of phospho-EphA2 protein/total EphA2 protein levels was performed using ImageJ software. Mean values are presented with S.D as indicated. Statistical differences between multiple groups were analyzed using one-way analysis of variance (ANOVA). Values of <i>P</i><0.05 were considered to be statistically significant. ns: No statistically significant difference between the two groups.</p>", "links"=>[], "tags"=>["phosphorylation", "epha2", "receptor", "ephrin-a5", "affected", "sam"], "article_id"=>313735, "categories"=>["Physics", "Developmental Biology", "Medicine", "Immunology", "Molecular Biology", "Biophysics"], "users"=>["Jeong Eun Park", "Alexander I. Son", "Rui Hua", "Lianqing Wang", "Xue Zhang", "Renping Zhou"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0036564.g004"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Tyrosine_phosphorylation_of_EPHA2_receptor_by_ephrin_A5_is_not_affected_by_SAM_domain_mutations_/313735", "title"=>"Tyrosine phosphorylation of EPHA2 receptor by ephrin-A5 is not affected by SAM domain mutations.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-03 01:02:15"}
  • {"files"=>["https://ndownloader.figshare.com/files/643359"], "description"=>"<p>(<b>A</b>) Mutant <i>EPHA2</i> genes fail to promote αTN4-1 cell migration. αTN4-1 cells were grown to confluency and serum-starved for 24 hours. A scratch wound was made with a micropipette tip and the edge of cells was marked. 2 µg/mL cross-linked ephrin-A5-Fc was then added to the starvation media, and cells were allowed to migrate toward the center of the wound and photographed at the indicated times (representative figure of three independent experiments). The position of the initial scratch is indicated by dotted lines. Scale bar, 500 µm. (<b>B</b>) Quantification of the effects of <i>EPHA2</i> genes on αTN4-1 cell migration. The graphs represent the measurement of migration distance from three independent experiments. Mean values are presented with S.D as indicated. Statistical differences were analyzed using one-way analysis of variance (ANOVA) or calculated by a two-tailed student t-test. <b><i>Black asterisks</i></b><b>,</b> comparison between time 0 and 24 hours and time 0 and 48 hours; <b><i>Blue asterisks</i></b><b>,</b> comparison between the mock groups and the listed wild-type or mutant <i>EPHA2</i> genes at 24 or 48 hours; <b><i>Red asterisks</i></b><b>,</b> comparison between untreated and treated conditions at 24 or 48 hours. ***, <i>P</i><0.001; **, <i>P</i><0.01; *, <i>P</i><0.05; and ns, not significant. Values of <i>P</i><0.05 were considered to be statistically significant.</p>", "links"=>[], "tags"=>["ligand-independent"], "article_id"=>313850, "categories"=>["Physics", "Developmental Biology", "Medicine", "Immunology", "Molecular Biology", "Biophysics"], "users"=>["Jeong Eun Park", "Alexander I. Son", "Rui Hua", "Lianqing Wang", "Xue Zhang", "Renping Zhou"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0036564.g005"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SAM_domain_of_EPHA2_is_essential_for_ligand_independent_promotion_of_cell_migration_/313850", "title"=>"SAM domain of <i>EPHA2</i> is essential for ligand-independent promotion of cell migration.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-03 01:04:10"}
  • {"files"=>["https://ndownloader.figshare.com/files/643480"], "description"=>"<p>(<b>A, B</b>) Mutant EPHA2 proteins exhibit reduced activation of Akt and Erk by ephrin-A5. HEK293T cells were grown to confluence and serum-starved for 24 hours. 2 µg/mL cross-linked ephrin-A5-Fc was then added to the starvation media and cell lysates were immunoblotted with anti-phospho-Akt (Ser473) or anti-phospho-Erk (1/2), and then reprobed with anti-α-tubulin as a loading control. (<b>C</b>) Inactivation of EphA2 gene leads to reduction of Akt activity in mouse lenses. Each lens was prepared from 22 days old mice and extracted with lysis buffer. Total lens proteins were resolved by SDS-PAGE and western blot analysis was performed using indicated antibodies as described in the <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0036564#s4\" target=\"_blank\">Materials and Methods</a>. The blot was reprobed with anti-α-tubulin as a loading control.</p>", "links"=>[], "tags"=>["epha2", "activation", "regulates", "akt", "erk"], "article_id"=>313969, "categories"=>["Physics", "Developmental Biology", "Medicine", "Immunology", "Molecular Biology", "Biophysics"], "users"=>["Jeong Eun Park", "Alexander I. Son", "Rui Hua", "Lianqing Wang", "Xue Zhang", "Renping Zhou"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0036564.g006"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Ligand_stimulated_EPHA2_activation_regulates_Akt_and_Erk_activation_/313969", "title"=>"Ligand-stimulated EPHA2 activation regulates Akt and Erk activation.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-03 01:06:09"}

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Relative Metric

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