{"id":68557,"date":"2024-06-19T18:18:59","date_gmt":"2024-06-19T16:18:59","guid":{"rendered":"https:\/\/www.embl.org\/news\/?p=68557"},"modified":"2024-06-19T18:19:05","modified_gmt":"2024-06-19T16:19:05","slug":"invisible-protein-keeps-cancer-at-bay","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science-technology\/invisible-protein-keeps-cancer-at-bay\/","title":{"rendered":"\u2018Invisible\u2019 protein keeps cancer at bay"},"content":{"rendered":"\n<article class=\"vf-card vf-card--brand vf-card--bordered vf-u-margin__bottom--800\" default>\n  <div class=\"vf-card__content | vf-stack vf-stack--400\">\n      <h3 class=\"vf-card__heading\">\n      Summary    <\/h3>\n                <p class=\"vf-card__text\"><ul>\r\n \t<li>EMBL Hamburg scientists and collaborators discovered a new molecular mechanism through which an unstructured protein disables cancer-promoting molecules by gluing them together into a stack.<\/li>\r\n \t<li>Unstructured proteins are essentially \u2018invisible\u2019 to structural biology techniques, which makes them challenging to study.<\/li>\r\n \t<li>Data from human patient samples support the role of this mechanism in cancer progression. While the study mostly focused on prostate cancer, the mechanism likely plays a role in other types of cancer as well.<\/li>\r\n<\/ul><\/p>\n      <\/div>\n<\/article>\n\n\n\n\n<p>Each second of our lives, cells in our body grow and divide to ensure we stay healthy. However, this process has a dark side: if cell growth and divisions become excessive, that may cause cancer. To keep a safe balance, our cells are equipped with several molecular mechanisms to limit their own growth and division.<\/p>\n\n\n\n<p>EMBL Hamburg\u2019s Wilmanns Group, in collaboration with research groups from the <a href=\"https:\/\/www.uke.de\/english\/departments-institutes\/centers\/experimental-medicine\/index.html\">Center for Experimental Medicine<\/a> <a href=\"https:\/\/www.uke.de\/english\/departments-institutes\/institutes\/tumor-biology\/index.html\">Institute of Tumor Biology <\/a>and <a href=\"https:\/\/www.martini-klinik.de\/en\/\">the Martini Clinic<\/a> at the <a href=\"https:\/\/www.uke.de\/english\/index.html\">University Medical Center Hamburg-Eppendorf (UKE)<\/a>, as well as the Leibniz Institute on Aging &#8211; <a href=\"https:\/\/www.leibniz-fli.de\/\">Fritz Lipmann Institute<\/a>, has revealed a new mechanism through which cells counteract one of the main cancer-promoting proteins by stacking and fixing its molecules in a pile. The findings shed light on how prostate cancer advances from treatable to aggressive, treatment-resistant stages.<\/p>\n\n\n\n<h2 class=\"wp-block-heading\" id=\"a1\"><strong>A villain and a hero<\/strong><\/h2>\n\n\n\n<p>Their discovery, like a good novel, has a villain and a hero.<\/p>\n\n\n\n<p>The \u2018villain\u2019 in this story is a group of proteins, called CtBPs (C-terminal binding proteins), which regulate the activity of several genes involved in cell growth and division. In various studies, CtBPs have been demonstrated to participate in promoting the development of cancer.<\/p>\n\n\n\n<p>But the cell has its ways to harness the \u2018villain\u2019 \u2013 that\u2019s where the \u2018hero\u2019 comes in: protein RAI2 (Retinoic Acid-Induced 2). RAI2 was only discovered recently, and even though it\u2019s present in the cell in small amounts, it has been shown to play a role in preventing cancer metastasis. However, until now, it has been unclear how it achieves this.<\/p>\n\n\n\n<p>The scientists have discovered that RAI2 has a remarkable ability to seize CtBP molecules and stack them together in a process called \u2018polymerisation\u2019. As they get piled up, the CtBP molecules form elongated aggregates in cancer cell lines, described as \u2018nuclear foci\u2019. Trapped and stacked by RAI2 in the aggregate, CtBP, the villain, becomes inactive.<\/p>\n\n\n\n<p>\u201cPolymerisation has become an emerging field of interest in the life sciences, but to our knowledge, it has not been described to date in the context of interfering with cancer progression,\u201d said Matthias Wilmanns, Group Leader at EMBL Hamburg. \u201cThe discovery of this new mechanism of powerful target inhibition could open up new anti-cancer therapy directions, such as developing small molecules with potential or cancer target polymerisation.\u201d<\/p>\n\n\n\n<h2 class=\"wp-block-heading\" id=\"a2\"><strong>An invisible hero<\/strong><\/h2>\n\n\n\n<p>To structural biologists like the Wilmanns Group, RAI2, the hero, is essentially an \u2018invisible\u2019 protein. While the majority of proteins, like origami, fold into 3D structures, RAI2 rather resembles a flexible band that keeps changing shape. Capturing such a wobbly protein in high resolution is impossible with the currently available structural biology techniques.<\/p>\n\n\n\n<p>\u201cYou could compare it to trying to take a photo of a moving object at night \u2013 what you\u2019ll get is a blurry image,\u201d said Wilmanns.<\/p>\n\n\n\n<p>In this study, the only parts of RAI2 that could be visualised in the molecular model were the only parts that would stand still \u2013 the \u2018sticky\u2019 fragments through which RAI2 binds CtBPs. Each RAI2 molecule has two such fragments (depicted in orange in the images), which enable it, akin to adhesive tape, to glue two CtBP molecules together.<\/p>\n\n\n\n<figure class=\"vf-figure wp-block-image size-full\"><img loading=\"lazy\" decoding=\"async\" width=\"1000\" height=\"600\" class=\"vf-figure__image\" src=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2024\/06\/StackingProteins_supplementary_final-1000x600-1.jpg\" alt=\"Illustration consisting of three panels. Upper left, a cyan granular oval shape (cell nucleus) with a brighter cyan spot in it. The middle panel: broad and narrow elements arranged alternatingly into a bright chain. On the right: molecular model, which shows the same chain of molecules as in the middle panel, but in more detail and in multiple colours.\" class=\"wp-image-68571\" srcset=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2024\/06\/StackingProteins_supplementary_final-1000x600-1.jpg 1000w, https:\/\/www.embl.org\/news\/wp-content\/uploads\/2024\/06\/StackingProteins_supplementary_final-1000x600-1-300x180.jpg 300w, https:\/\/www.embl.org\/news\/wp-content\/uploads\/2024\/06\/StackingProteins_supplementary_final-1000x600-1-768x461.jpg 768w\" sizes=\"auto, (max-width: 1000px) 100vw, 1000px\" \/><figcaption class=\"vf-figure__caption\">The scientists observed the CtBP-RAI2 polymers at different scales: at the cellular level, as aggregates, or \u2018foci\u2019, in the nucleus (upper left) and at the molecular level as a stack of molecules captured with cryo-electron microscopy (middle). The latter enabled them to create a detailed structural model (right). Credit: Isabel Romero Calvo\/EMBL<\/figcaption><\/figure>\n\n\n\n<p>\u201cWobbly proteins like RAI2 are challenging to work with, so this project took lots of hard work, focus, determination, and a \u2018never give up\u2019 attitude,\u201d said Nishit Goradia, previously a postdoc in the Wilmanns Group, currently a fellow at the UKE. \u201cWe\u2019ve revealed that RAI2 is a real dark horse: like other wobbly proteins, it\u2019s quite understudied, but it holds true potential for inactivating cancer-promoting proteins. For me, this has been a career-defining project and I\u2019m proud of this achievement.\u201d<\/p>\n\n\n\n<h2 class=\"wp-block-heading\" id=\"a3\"><strong>Wobbly protein in prostate cancer<\/strong><\/h2>\n\n\n\n<p>To check if the new mechanism plays a role in human cancer, the scientists analysed, in addition to cancer cell lines, cancer samples from a diverse cohort of more than 100 patients of the UKE\u2019s <a href=\"https:\/\/www.uke.de\/english\/departments-institutes\/centers\/university-cancer-center-hamburg-(ucch)%E2%80%94hubertus-wald-tumor-center\/index.html\">University Cancer Center Hamburg<\/a> and <a href=\"https:\/\/www.martini-klinik.de\/en\/\">Martini Clinic<\/a>. They focused on prostate cancer, the second most common type of cancer in men and the third leading cause of cancer related death.<\/p>\n\n\n\n<p>In the course of therapy, prostate cancer may develop resistance to treatment, resulting in very poor prognosis for the patients. However, it is not yet fully understood why some forms of prostate cancer develop into certain highly aggressive subtypes, and others don\u2019t. RAI2 could play a key role here.<\/p>\n\n\n\n<p>In both tumour cell lines and samples from patients, the scientists saw that the RAI2 levels were strongly reduced in more severe and treatment-resistant types of prostate cancer. In analyses <em>in vitro<\/em>, they saw that loss of RAI2 favours cellular processes that may lead to resistance to certain types of treatment.<\/p>\n\n\n\n<p>\u201cEven if we are not yet able to use this result therapeutically, it is a decisive step towards better understanding how a very aggressive subtype of prostate cancer develops,\u201d said Gunhild von Amsberg, Professor of Uro-oncology at the University Cancer Center Hamburg and the Martini Clinic. \u201cAn important next step will be to transfer our findings to the clinic and thus identify patients who may be at risk at an early stage.\u201d<\/p>\n\n\n\n<p>Although the analysis focused on prostate cancer, the scientists suspect that the significance of their discovery maybe be applicable to other cancers too.<\/p>\n\n\n\n<h2 class=\"wp-block-heading\" id=\"a4\"><strong>Molecular biology meets the clinics<\/strong><\/h2>\n\n\n\n<p>The study is part of the long-standing collaboration between EMBL and UKE and showcases the benefits of combining both institutions\u2019 complementary scientific approaches. While the UKE conducts a large spectrum of medical projects, in part based on patient data, EMBL contributes expertise in studying life across biological scales, including investigating disease mechanisms at the molecular and cellular levels.<\/p>\n\n\n\n<p>\u201cThis work demonstrates the future perspective of collaboration between molecular biology and the clinics to unlock research \u2018from molecules to patients\u2019,\u201d said Wilmanns.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>EMBL Hamburg scientists and collaborators discovered a new molecular mechanism in which an unstructured protein disables one of the main cancer-promoting proteins by gluing them into an elongated stack. Data from human patient samples support the role of this mechanism in prostate cancer&hellip;<\/p>\n","protected":false},"author":96,"featured_media":68569,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[17591],"tags":[38,474,17279,40,53,738,5752,35,653,17647,14311,306],"embl_taxonomy":[9596,5150,19403],"class_list":["post-68557","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science-technology","tag-cancer","tag-collaboration","tag-cryo-electron-microscopy","tag-gene-regulation","tag-hamburg","tag-prostate-cancer","tag-protein-structure","tag-structural-biology","tag-tumour","tag-uke","tag-unstructural-biology","tag-wilmanns","embl_taxonomy-embl-hamburg","embl_taxonomy-structural-biology-embl-hamburg","embl_taxonomy-wilmanns-group"],"acf":{"featured":true,"show_featured_image":false,"field_target_display":"embl","field_article_language":{"value":"english","label":"English"},"article_intro":"<p>EMBL Hamburg scientists have revealed how an unstructured protein traps cancer-promoting molecules<\/p>\n","related_links":[{"link_description":"Wilmanns Group","link_url":"https:\/\/www.embl.org\/groups\/wilmanns\/"},{"link_description":"Bringing research on disordered proteins to order","link_url":"https:\/\/www.embl.org\/news\/science\/bringing-research-on-disordered-proteins-to-order\/"}],"source_article":[{"publication_title":"Master corepressor inactivation through multivalent SLiM-induced polymerization mediated by the oncogene suppressor RAI2","publication_link":{"title":"","url":"https:\/\/www.nature.com\/articles\/s41467-024-49488-3","target":"_blank"},"publication_authors":"Goradia N., Werner S., et al. ","publication_source":"Nature Communications","publication_date":"19 June 2024","publication_doi":"10.1038\/s41467-024-49488-3"}],"in_this_article":[{"heading_description":"A villain and a hero","anchor":"#a1"},{"heading_description":"An invisible hero","anchor":"#a2"},{"heading_description":"Wobbly protein in prostate cancer","anchor":"#a3"},{"heading_description":"Molecular biology meets the clinics","anchor":"#a4"}],"press_contact":"EMBL Generic","article_translations":false,"languages":""},"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 &gt; All EMBL sites &gt; EMBL Hamburg"},{"uuid":"a:3:{i:0;s:36:\"302cfdf7-365b-462a-be65-82c7b783ebf7\";i:1;s:36:\"7ca3ce91-dc32-47ea-8d4b-7a53c3a3a9fd\";i:2;s:36:\"2dc39890-6c01-47bf-ac78-d42abdb10079\";}","parents":[],"name":["Structural Biology (EMBL Hamburg)"],"slug":"structural-biology-embl-hamburg","description":"What &gt; Research Units &gt; Structural Biology (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 &gt; Structural Biology (EMBL Hamburg) &gt; Wilmanns Group"}],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.2 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>\u2018Invisible\u2019 protein keeps cancer at bay | EMBL<\/title>\n<meta name=\"description\" content=\"EMBL Hamburg scientists and collaborators have revealed how an unstructured protein disables one of the main cancer-promoting molecules.\" \/>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.embl.org\/news\/science-technology\/invisible-protein-keeps-cancer-at-bay\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"\u2018Invisible\u2019 protein keeps cancer at bay | EMBL\" \/>\n<meta property=\"og:description\" content=\"EMBL Hamburg scientists and collaborators have revealed how an unstructured protein disables one of the main cancer-promoting molecules.\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.embl.org\/news\/science-technology\/invisible-protein-keeps-cancer-at-bay\/\" \/>\n<meta property=\"og:site_name\" content=\"EMBL\" \/>\n<meta property=\"article:publisher\" content=\"https:\/\/www.facebook.com\/embl.org\/\" \/>\n<meta property=\"article:published_time\" content=\"2024-06-19T16:18:59+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2024-06-19T16:19:05+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2024\/06\/StackingProteins_final-1000x600-1.jpg\" \/>\n\t<meta property=\"og:image:width\" content=\"1000\" \/>\n\t<meta property=\"og:image:height\" content=\"600\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/jpeg\" \/>\n<meta name=\"author\" content=\"Dorota Badowska\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:creator\" content=\"@d_badowska\" \/>\n<meta name=\"twitter:site\" content=\"@embl\" \/>\n<meta name=\"twitter:label1\" content=\"Written by\" \/>\n\t<meta name=\"twitter:data1\" content=\"Dorota Badowska\" \/>\n\t<meta name=\"twitter:label2\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data2\" content=\"5 minutes\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\/\/schema.org\",\"@graph\":[{\"@type\":\"NewsArticle\",\"@id\":\"https:\/\/www.embl.org\/news\/science-technology\/invisible-protein-keeps-cancer-at-bay\/#article\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/science-technology\/invisible-protein-keeps-cancer-at-bay\/\"},\"author\":{\"name\":\"Dorota Badowska\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/b8ae50efcd7533f0ab2ec368736b1d04\"},\"headline\":\"\u2018Invisible\u2019 protein keeps cancer at bay\",\"datePublished\":\"2024-06-19T16:18:59+00:00\",\"dateModified\":\"2024-06-19T16:19:05+00:00\",\"mainEntityOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science-technology\/invisible-protein-keeps-cancer-at-bay\/\"},\"wordCount\":1014,\"publisher\":{\"@id\":\"https:\/\/www.embl.org\/news\/#organization\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science-technology\/invisible-protein-keeps-cancer-at-bay\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2024\/06\/StackingProteins_final-1000x600-1.jpg\",\"keywords\":[\"cancer\",\"collaboration\",\"cryo-electron microscopy\",\"gene regulation\",\"hamburg\",\"prostate cancer\",\"protein structure\",\"structural biology\",\"tumour\",\"uke\",\"unstructural biology\",\"wilmanns\"],\"articleSection\":[\"Science &amp; 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