{"id":4498,"date":"2013-04-12T17:50:00","date_gmt":"2013-04-12T21:50:00","guid":{"rendered":"https:\/\/www.med.unc.edu\/biochem\/unc-researchers-engineer-protein-switch-to-dissect-role-of-cancer2019s-key-players\/"},"modified":"2018-08-01T10:41:19","modified_gmt":"2018-08-01T14:41:19","slug":"unc-researchers-engineer-protein-switch-to-dissect-role-of-cancer2019s-key-players","status":"publish","type":"post","link":"https:\/\/www.med.unc.edu\/biochem\/news\/unc-researchers-engineer-protein-switch-to-dissect-role-of-cancer2019s-key-players\/","title":{"rendered":"UNC researchers engineer &#8216;protein switch&#8217; to dissect role of cancer\u2019s key players"},"content":{"rendered":"<div>\n<p class=\"lead\">In the first application of this approach, the UNC researchers showed how a protein called Src kinase influences the way cells extend and move, a previously unknown role that is consistent with the protein\u2019s ties to tumor progression and metastasis.<\/p>\n<div class=\"image-section\">\n<figure class=\"thumbnail wp-caption alignright\">\n    <img loading=\"lazy\" decoding=\"async\" class=\"size-medium wp-image-4499\" src=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2018\/07\/unc-researchers-engineer-protein-switch-to-dissect-role-of-cancer2019s-key-players-image2-264x300.jpeg\" width=\"300\" height=\"200\" alt=\"image2\"\/><figcaption class=\"caption wp-caption-text\">At top is a structural model of uniRapR domain which binds small molecule rapamycin. The bottom left depicts inactive state of the protein of interest modified with uniRapR domain. Binding of rapamycin and uniRapR reactivates the protein (bottom right).<br \/>\n    <\/figcaption><\/figure>\n<\/div>\n<div>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \"><b>Media contact: <\/b>Les Lang, (919) 966-9366, <a class=\"mail-link\" href=\"mailto:llang@med.unc.edu\" style=\"color: rgb(51, 102, 153); border-bottom-color: rgb(108, 112, 120); border-bottom-style: dotted; \">llang@med.unc.edu<\/a><\/p>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \">Wednesday, April 10, 2013<\/p>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \">CHAPEL HILL, N.C. \u2013 Researchers at the University of North Carolina at Chapel Hill School of Medicine have \u201crationally rewired\u201d some of the cell\u2019s smallest components to create proteins that can be switched on or off by command. These \u201cprotein switches\u201d can be used to interrogate the inner workings of each cell, helping scientists uncover the molecular mechanisms of human health and disease.<\/p>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \">In the first application of this approach, the UNC researchers showed how a protein called Src kinase influences the way cells extend and move, a previously unknown role that is consistent with the protein\u2019s ties to tumor progression and metastasis.<\/p>\n<p><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2018\/07\/image7_7-300x225.jpeg\" alt=\"Dokh_2012pic\" title=\"Dokh_2012pic\" height=\"150\" width=\"120\" class=\"size-medium wp-image-3094\"\/><\/p>\n<p>\u201cThis rationally designed control of protein conformations represents a breakthrough in computational protein design,\u201d said senior study author <a class=\"external-link\" href=\"http:\/\/www.med.unc.edu\/biochem\/dokholyan\" style=\"color: rgb(51, 102, 153); border-bottom-color: rgb(108, 112, 120); border-bottom-style: dotted; \">Nikolay Dokholyan, PhD<\/a>, a professor of biochemistry and biophysics. \u201cWe now have a new tool for delineating the activities of various proteins in living cells in a way that was never before possible.\u201d <\/p>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \">The research was <a class=\"external-link\" href=\"http:\/\/www.pnas.org\/content\/early\/2013\/04\/05\/1218319110.abstract\" style=\"color: rgb(51, 102, 153); border-bottom-color: rgb(108, 112, 120); border-bottom-style: dotted; \">published online<\/a> ahead of print in the <a class=\"external-link\" href=\"http:\/\/www.pnas.org\/\" style=\"color: rgb(51, 102, 153); border-bottom-color: rgb(108, 112, 120); border-bottom-style: dotted; \">Proceedings of the National Academy of Sciences<\/a>. In the study, Dokholyan created a \u201cswitch\u201d that would make a protein wobbly and unable to do its job unless it was flipped \u201con\u201d by a drug called rapamycin, which would stabilize the protein and let it perform its function.<\/p>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \">The approach is a simpler and more reliable version of a protein engineering system pioneered three years ago by Dokholyan and Klaus Hahn, professor of pharmacology at UNC, called rapamycin regulated or RapR.  In the old approach, the switching mechanism depended on two proteins and the drug. The first protein \u2013 the one the researchers wanted to study \u2013 was given the RapR modification and put in cells in tissue culture. The second protein was placed in the cells as well, but simply floated around until the addition of drug caused it to latch on to the modification in the first protein and turn it on. The problem with the approach was that some cells would have a lot of the first protein and less of the second, or vice versa.<\/p>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \">\u201cIt became the Achilles heel of the technique, because there was variability in the results due to the different ratios between the proteins,\u201d said Hahn. \u201cWhat Dokholyan was able to do, which was extremely challenging from a protein engineering standpoint, was to combine the two parts into one.\u201d Dokholyan and Hahn are members of the UNC Lineberger Comprehensive Cancer Center.<\/p>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \">Dokholyan and his colleagues took the two proteins and broke them apart into their individual components, structures called alpha helices and beta sheets. They then rewired them together to make a whole new protein where the parts could interact with each other. When researchers compared this system, called uniRapR, with the previous approach, they found the new one gave cleaner, more reliable and more consistent results.<\/p>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \">They then applied the technique to study Src kinase, a protein involved in the metastasis or spread of tumor cells. Scientists had postulated that Src kinase plays a role in cell motility, but previous methods have not allowed them to isolate its activity from other similar proteins.<\/p>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \">Working both in cultured human cells and in the model organism zebrafish, the researchers showed that turning on Src causes the cell to extend its edges as part of cell movement. Now that they have dissected the role of one protein, the researchers plan to look at a variety of other kinases to understand their roles in the development, progression, and spread of cancer.<\/p>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \">The research was funded in by the National Institutes of Health, the National Institute of Environmental Health Sciences, and the National Cancer Institute. Study co-authors from UNC were Onur Dagliyan; David Shirvanyants, PhD; Andrei V. Karginov, PhD; Feng Deng, PhD; Lanette Fee; and Srinivas N. Chandrasekaran. Co-authors from the University of Wisconsin, Madison, were Christina M. Freisinger, Gromoslaw A. Smolen, and Anna Huttenlocher.<\/p>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \"><a class=\"external-link\" href=\"http:\/\/danger.med.unc.edu\/index.php\" target=\"_blank\" title=\"\">Doklolyan Lab<\/a><\/p>\n<p style=\"margin: 0.25em 0pt 0.85em; line-height: 1.5em; color: rgb(51, 51, 51); background-color: rgb(255, 255, 255); \"><a class=\"external-link\" href=\"http:\/\/unclineberger.org\/news\/dokholyan-lab-engineers-protein-switch-to-dissect-role-of-cancers-key-players-1\" target=\"_blank\" title=\"\">Lineburger News<\/a> by William Davis<\/p>\n<\/div>\n<\/div>\n","protected":false},"excerpt":{"rendered":"<p><!-- description --> <\/p>\n<p class='lead'>In the first application of this approach, the UNC researchers showed how a protein called Src kinase influences the way cells extend and move, a previously unknown role that is consistent with the protein\u2019s ties to tumor progression and metastasis.<\/p>\n","protected":false},"author":12066,"featured_media":4499,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"layout":"","cellInformation":"","apiCallInformation":"","footnotes":"","_links_to":"","_links_to_target":""},"categories":[2],"tags":[10,19,4],"class_list":["post-4498","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-news","tag-news_faculty","tag-news_2013","tag-recent-news","odd"],"acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.8 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>UNC researchers engineer &#039;protein switch&#039; 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