{"id":26600,"date":"2010-01-26T08:00:00","date_gmt":"2010-01-26T07:00:00","guid":{"rendered":"https:\/\/www.embl.org\/news\/?p=26600"},"modified":"2024-11-14T16:27:03","modified_gmt":"2024-11-14T15:27:03","slug":"how-to-shoot-the-messenger","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/how-to-shoot-the-messenger\/","title":{"rendered":"How to shoot the messenger"},"content":{"rendered":"\n

Cells rely on a range of signalling systems to communicate with each other and to control their own internal workings. Scientists from the European Molecular Biology Laboratory (EMBL) in Hamburg, Germany, have now found a way to hack into a vital communications system, raising the possibility of developing new drugs to tackle disorders like neurodegeneration, cancer and cardiovascular disease. In a study published today in Science Signaling<\/em>, they have pieced together the first snapshot of what two of the system\u2019s components look like while interacting.<\/p>\n\n\n\n

One way these signalling systems work is by triggering a flood of calcium ions inside the cell. These get picked up by a receiver, a protein called calmodulin which turns this calcium signal into action by switching various parts of the cell\u2019s machinery on or off. Calmodulin regulates a set of proteins called kinases, each of which controls the activity of specific parts of the cell, thus altering the cell\u2019s behaviour.<\/p>\n\n\n\n

Using high-energy X-rays produced by the European Synchrotron Radiation Facility (ESRF)<\/a> in Grenoble, France, and by the German Synchrotron Radiation Centre (DESY)<\/a>, in Hamburg, Germany, Matthias Wilmanns\u2019 team at EMBL revealed the molecular structure of one of these kinases, a protein called Death-Associated Protein Kinase DAPK, when bound to calmodulin. The structure showed how calmodulin binds to a particular section of DAPK, switching the kinase on so that it can go and change the function of its targets. The team then worked out which of DAPK\u2019s building blocks, or amino acids, were crucial for calmodulin to bind.<\/p>\n\n\n\n

\u201cFaulty versions of DAPK are involved in the development of some cancers,\u201d says Wilmanns, \u201cso we want to know more about how this protein functions to allow its better exploitation as an anti-cancer target.\u201d<\/p>\n\n\n\n

What\u2019s more, DAPK has physical similarities to many of the other kinases controlled by calmodulin, meaning many of them are likely to interact with calmodulin in the same, or similar ways. Being able to see the three-dimensional structures of these proteins, how they clip together and alter each other\u2019s behaviour means researchers can devise ways to manipulate this interaction with drugs.<\/p>\n\n\n\n

\u201cThat will provide a platform to get into drug discovery,\u201d says Wilmanns, adding, \u201cobviously, this is the beginning of the story.\u201d He is planning to do so in an ongoing collaboration with Adi Kimchi\u2019s team at the Weizmann Institute in Israel and other groups from EMBL.<\/p>\n","protected":false},"excerpt":{"rendered":"

Cells rely on a range of signalling systems to communicate with each other and to control their own internal workings. Scientists from the European Molecular Biology Laboratory (EMBL) in Hamburg, Germany, have now found a way to hack into a vital communications system, raising the possibility of…<\/p>\n","protected":false},"author":16,"featured_media":26604,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[2030,1774,37,53,1748,35,306,1714],"embl_taxonomy":[9596,19403],"class_list":["post-26600","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-desy","tag-esrf","tag-grenoble","tag-hamburg","tag-press-release","tag-structural-biology","tag-wilmanns","tag-x-ray-crystallography","embl_taxonomy-embl-hamburg","embl_taxonomy-wilmanns-group"],"acf":{"show_featured_image":false,"vf_locked":false,"featured":false,"article_intro":"

EMBL scientists shed light on cellular communication systems involved in neurodegeneration, cancer and cardiovascular disease<\/p>\n","article_sources":[{"source_description":"

De Diego, I., Kuper, J., Bakalova, N., Kursula, P., & Wilmanns, M. Molecular Basis of the Death Associated Protein Kinase \u2013 Calcium\/Calmodulin regulator complex. Science Signaling<\/em>, 26 January 2010. DOI: 10.1126\/scisignal.2000552<\/p>\n","source_link_url":"https:\/\/stke.sciencemag.org\/content\/3\/106\/ra6"}],"related_links":false,"in_this_article":false,"color":"#007B53","link_color":"#fff","youtube_url":"","mp4_url":"","video_caption":"","translations":false,"press_contact":"EMBL Generic"},"embl_taxonomy_terms":[{"uuid":"a:3:{i:0;s:36:\"b14d3f13-5670-44fb-8970-e54dfd9c921a\";i:1;s:36:\"89e00fee-87f4-482e-a801-4c3548bb6a58\";i:2;s:36:\"613c4de5-1775-447f-af71-4b07085318e9\";}","parents":[],"name":["EMBL Hamburg"],"slug":"embl-hamburg","description":"Where > All EMBL sites > EMBL Hamburg"},{"uuid":"a:3:{i:0;s:36:\"302cfdf7-365b-462a-be65-82c7b783ebf7\";i:1;s:36:\"2dc39890-6c01-47bf-ac78-d42abdb10079\";i:2;s:36:\"b7081976-e7c1-4678-ab00-3e02d20e9e87\";}","parents":[],"name":["Wilmanns Group"],"slug":"wilmanns-group","description":"What > Structural Biology (EMBL Hamburg) > Wilmanns Group"}],"yoast_head":"\nHow to shoot the messenger | EMBL<\/title>\n<meta name=\"description\" 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