{"id":7522,"date":"2021-01-26T10:56:26","date_gmt":"2021-01-26T10:56:26","guid":{"rendered":"http:\/\/www.sci.muni.cz\/ofiz\/?p=7522"},"modified":"2021-01-26T10:56:27","modified_gmt":"2021-01-26T10:56:27","slug":"phosphorylation-induced-changes-in-the-pdz-domain-of-dishevelled-3-2","status":"publish","type":"post","link":"https:\/\/ueb1.sci.muni.cz\/ofiz\/en\/phosphorylation-induced-changes-in-the-pdz-domain-of-dishevelled-3-2\/","title":{"rendered":"Phosphorylation-induced changes in the PDZ domain of Dishevelled 3"},"content":{"rendered":"\n<h5><strong>Abstract:<\/strong><\/h5>\n<p style=\"text-align: justify;\">The PDZ domain of Dishevelled 3 protein belongs to a highly abundant protein recognition motif which typically binds short C-terminal peptides. The affinity of the PDZ towards the peptides could be fine-tuned by a variety of post-translation modifications including phosphorylation. However, how phosphorylations affect the PDZ structure and its interactions with ligands remains elusive.<\/p>\n<p style=\"text-align: justify;\">Combining molecular dynamics simulations, NMR titration, and biological experiments, we explored the role of previously reported phosphorylation sites and their mimetics in the Dishevelled PDZ domain.<\/p>\n<p style=\"text-align: justify;\">Our observations suggest three major roles for phosphorylations:<\/p>\n<p style=\"text-align: justify;\">(1) acting as an on\/off PDZ binding switch,<\/p>\n<p style=\"text-align: justify;\">(2) allosterically affecting the binding groove, and<\/p>\n<p style=\"text-align: justify;\">(3) influencing the secondary binding site.<\/p>\n<p style=\"text-align: justify;\">Our simulations indicated that mimetics had similar but weaker effects, and the effects of distinct sites were non-additive. This study provides insight into the Dishevelled regulation by PDZ phosphorylation. Furthermore, the observed effects could be used to elucidate the regulation mechanisms in other PDZ domains.<\/p>\n\n\n\n<p style=\"text-align: right;\"><a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/33452274\/\"><strong>Sci Rep. 2021 Jan 15;11(1):1484. doi: 10.1038\/s41598-020-79398-5.<\/strong><\/a><\/p>\n\n\n\n<figure class=\"wp-block-image\"><img loading=\"lazy\" decoding=\"async\" width=\"1024\" height=\"313\" src=\"http:\/\/www.sci.muni.cz\/ofiz\/wp-content\/uploads\/2021\/01\/wnt_tko-1024x313.png\" alt=\"\" class=\"wp-image-7514\" srcset=\"https:\/\/ueb1.sci.muni.cz\/ofiz\/wp-content\/uploads\/2021\/01\/wnt_tko-1024x313.png 1024w, https:\/\/ueb1.sci.muni.cz\/ofiz\/wp-content\/uploads\/2021\/01\/wnt_tko-300x92.png 300w, https:\/\/ueb1.sci.muni.cz\/ofiz\/wp-content\/uploads\/2021\/01\/wnt_tko-768x235.png 768w, https:\/\/ueb1.sci.muni.cz\/ofiz\/wp-content\/uploads\/2021\/01\/wnt_tko.png 1967w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><figcaption> The illustration of the DVL3 rescue TopFlash assay where luciferase activity is measured after addition of Wnt3a ligand. If active DVL molecules are present in the cell a change of luminescence is measured. <\/figcaption><\/figure>\n\n\n\n<h5><strong>Authors:<\/strong><\/h5>\n<p>Miroslav Jur\u00e1sek<sup>1<\/sup>, Jitender Kumar<sup>2<\/sup> , <strong>Petra Pacl\u00edkov\u00e1<sup>3<\/sup><\/strong> , <strong>Alka Kumari<sup>3<\/sup><\/strong> , Konstantinos Tripsianes<sup>2<\/sup>, <strong>V\u00edt\u011bzslav Bryja<sup>3,4<\/sup><\/strong>, Robert V\u00e1cha<sup>5,6<\/sup><\/p>\n<p>    1     National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 753\/5, 625 00, Brno, Czech Republic.<\/p>\n<p>    2    CEITEC &#8211; Central European Institute of Technology, Masaryk University, Kamenice 753\/5, 625 00, Brno, Czech Republic.<\/p>\n<p>  <strong>  3    Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, 62500, Czech Republic.<\/strong><\/p>\n<p>    4    Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Brno, 612 65, Czech Republic.<\/p>\n<p>    5    National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 753\/5, 625 00, Brno, Czech Republic. robert.vacha@mail.muni.cz.<\/p>\n<p>    6    CEITEC &#8211; Central European Institute of Technology, Masaryk University, Kamenice 753\/5, 625 00, Brno, Czech Republic. robert.vacha@mail.muni.cz.<\/p>\n<p> <\/p>\n\n\n<style>.wp-block-kadence-advancedbtn.kb-btns_27e076-7b{gap:var(--global-kb-gap-xs, 0.5rem );justify-content:center;align-items:center;}.kt-btns_27e076-7b .kt-button{font-weight:normal;font-style:normal;}.kt-btns_27e076-7b .kt-btn-wrap-0{margin-right:5px;}.wp-block-kadence-advancedbtn.kt-btns_27e076-7b .kt-btn-wrap-0 .kt-button{color:#fff;background:#009900;border-color:#fff;box-shadow:1px 1px 2px 3px rgba(0, 0, 0, 0.2);}.wp-block-kadence-advancedbtn.kt-btns_27e076-7b .kt-btn-wrap-0 .kt-button:hover, .wp-block-kadence-advancedbtn.kt-btns_27e076-7b .kt-btn-wrap-0 .kt-button:focus{color:#ffffff;border-color:#444444;}.wp-block-kadence-advancedbtn.kt-btns_27e076-7b .kt-btn-wrap-0 .kt-button::before{display:none;}.wp-block-kadence-advancedbtn.kt-btns_27e076-7b .kt-btn-wrap-0 .kt-button:hover, .wp-block-kadence-advancedbtn.kt-btns_27e076-7b .kt-btn-wrap-0 .kt-button:focus{background:#444444;}<\/style>\n<div class=\"wp-block-kadence-advancedbtn kt-btn-align-center kt-btn-tablet-align-inherit kt-btn-mobile-align-inherit kt-btns-wrap kt-btns_27e076-7b\"><div class=\"kt-btn-wrap kt-btn-wrap-0\"><a class=\"kt-button kt-btn-0-action kt-btn-size-standard kt-btn-style-basic kt-btn-svg-show-always kt-btn-has-text-true kt-btn-has-svg-false\" href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/33452274\/\"><span class=\"kt-btn-inner-text\">Read the whole story<\/span><\/a><\/div><\/div>\n","protected":false},"excerpt":{"rendered":"<p>Abstract: The PDZ domain of Dishevelled 3 protein belongs to a highly abundant protein recognition motif which typically binds short C-terminal peptides. The affinity of the PDZ towards the peptides could be fine-tuned by a variety of post-translation modifications including &hellip; <a href=\"https:\/\/ueb1.sci.muni.cz\/ofiz\/en\/phosphorylation-induced-changes-in-the-pdz-domain-of-dishevelled-3-2\/\">Read More<\/a><\/p>\n","protected":false},"author":5,"featured_media":7520,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"kt_blocks_editor_width":"","_exactmetrics_skip_tracking":false,"_exactmetrics_sitenote_active":false,"_exactmetrics_sitenote_note":"","_exactmetrics_sitenote_category":0,"footnotes":""},"categories":[412,256],"tags":[304],"class_list":["post-7522","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-bryjalab","category-new-paper","tag-bryjalab"],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.1.1 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>Phosphorylation-induced changes in the PDZ domain of Dishevelled 3 - Department of Animal Physiology and Immunology<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/ueb1.sci.muni.cz\/ofiz\/en\/phosphorylation-induced-changes-in-the-pdz-domain-of-dishevelled-3-2\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Phosphorylation-induced changes in the PDZ domain of Dishevelled 3 - Department of Animal Physiology and Immunology\" \/>\n<meta property=\"og:description\" content=\"Abstract: The PDZ domain of Dishevelled 3 protein belongs to a highly abundant protein recognition motif which typically binds short C-terminal peptides. 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