{"id":68391,"date":"2024-06-06T13:57:15","date_gmt":"2024-06-06T11:57:15","guid":{"rendered":"https:\/\/www.embl.org\/news\/?p=68391"},"modified":"2024-06-06T13:57:21","modified_gmt":"2024-06-06T11:57:21","slug":"structure-and-function-of-new-lysosome-transporter-revealed","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science-technology\/structure-and-function-of-new-lysosome-transporter-revealed\/","title":{"rendered":"Structure and function of new lysosome transporter revealed"},"content":{"rendered":"\n<p>The groups of <a href=\"https:\/\/www.embl.org\/groups\/loew\/\">Christian L\u00f6w<\/a> (<a href=\"https:\/\/www.cssb-hamburg.de\/\">CSSB<\/a>, EMBL Hamburg), Markus Damme (Christian-Albrechts-University Kiel), and Bruno Gasnier (CNRS and Universit\u00e9 Paris Cit\u00e9) worked together to reveal the structure and function of a previously unknown lysosome transporter. Their findings have recently been published <a href=\"https:\/\/www.nature.com\/articles\/s41556-024-01436-5\">in <em>Nature Cell Biology<\/em><\/a>.<\/p>\n\n\n\n<p>Lysosomes are organelles that function as a waste disposal and recycling system within the cell. They break down larger macromolecules such as proteins and lipids into smaller, lighter compounds like amino acids, monosaccharides, or fatty acids. These smaller compounds, known as metabolites, are then transported into the cell\u2019s cytoplasm.<\/p>\n\n\n\n<p>The Damme group at Christian-Albrechts-University Kiel seeks to elucidate the function of specific proteins on the lysosome\u2019s membrane. <\/p>\n\n\n\n<p>\u201cSeveral years ago, we noticed that the Glycosylated Lysosomal Membrane Protein (GLMP) binds tightly with an orphan transporter named Major Facilitator Superfamily Domain Containing 1 (MFSD1),\u201d noted Markus Damme, one of the study\u2019s three corresponding authors. As the term \u2018orphan transporter\u2019 indicates, MSFD1\u2019s function and substrate were unknown.<\/p>\n\n\n\n<p>To help reveal MFSD1\u2019s function, Damme reached out to the L\u00f6w group at the Centre for Structural Systems Biology (CSSB) and EMBL Hamburg. The L\u00f6w Group\u2019s research focuses on understanding peptide transporters known as <a href=\"https:\/\/www.embl.org\/news\/embletc\/issue-101\/the-secret-of-molecular-promiscuity\/\">POTs (proton-coupled oligopeptide transporters)<\/a>. <\/p>\n\n\n\n<p>\u201cI was intrigued by MFSD1 and wanted to help figure out its role in the lysosome,\u201d explained L\u00f6w, currently a visiting group leader at EMBL Hamburg and another of the study\u2019s corresponding authors. \u201cI was also confident that the different technologies and methodologies available to us at CSSB would be essential in helping us unravel this mystery.\u201d<\/p>\n\n\n\n<p>The work was supported in part by the <a href=\"https:\/\/www.embl.org\/groups\/sample-preparation-characterisation\/\">EMBL Sample Preparation and Characterisation Facility<\/a>, <a href=\"https:\/\/www.cssb-hamburg.de\/facilities\/pp\/index_eng.html\">Protein Production Core Facility<\/a> and <a href=\"https:\/\/www.cssb-hamburg.de\/facilities\/cryo_em\/index_eng.html\">CSSB\u2019s cryo-EM multi-user facility<\/a> on-site.<\/p>\n\n\n\n<p>Using a combination of techniques, including fluorescence spectroscopy and differential scanning fluorimetry (nanoDSF), the researchers discovered that MFSD1 not only binds but also transports dipeptides, peptides comprised of just two amino acids. The researchers were then able to show how the MFSD1\/GLMP complex binds to dipeptides.<\/p>\n\n\n\n<p>\u201cWe were able to determine the complex\u2019s structure in an outward-open conformation,\u201d explained Katharina Jungnickel, an EMBL <a href=\"https:\/\/www.embl.org\/about\/info\/postdoctoral-programme\/eipod4-fellowship-programme\/\">EIPOD<\/a> Fellow and one of the first authors of the paper. \u201cWe additionally saw density of the dipeptide at the binding site. Together with molecular dynamics simulations (by Reza Mehdipour, Ghent University), we verified that dipeptide binding is mainly facilitated by the coordination of its N- and C-termini.\u201d<\/p>\n\n\n\n<p>The Gasnier group at the Universit\u00e9 Paris Cit\u00e9 performed some clever experiments which enabled the researchers to discover the mechanism used by MFSD1 to transport the dipeptides. <\/p>\n\n\n\n<p>\u201cWe discovered that MFSD1 is a passive uniporter that only transports dipeptides along its own gradient,\u201d stated Bruno Gasnier, the paper\u2019s third corresponding author. \u201cThis led us to develop a new assay which revealed that MFSD1 transports a much wider spectrum of dipeptides than initially thought.\u201d<\/p>\n\n\n\n<p>The insights gained by the researchers indicate that MFSD1 provides an alternative route to supply amino acids for biosynthetic pathways when other lysosomal amino acid exporters are overloaded. <\/p>\n\n\n\n<p>\u201cThis was an amazing collaborative effort which combined labs with different expertise that were driven by the need to answer biological questions,\u201d noted L\u00f6w. \u201cI am looking forward to finding out more about MFSD1 and its overall role in nutrition sensing.\u201d<\/p>\n\n\n\n<hr class=\"vf-divider\"\/>\n\n\n\n<p><em>This article has been adapted from a news article by the <a href=\"https:\/\/www.cssb-hamburg.de\/news_amp_events\/articles\/2024\/structure_and_function_of_new_lysosome_transporter_revealed\/index_eng.html\">Centre for Structural Systems Biology (CSSB)<\/a>. Find the original story at the CSSB website <a href=\"https:\/\/www.cssb-hamburg.de\/news_amp_events\/articles\/2024\/structure_and_function_of_new_lysosome_transporter_revealed\/index_eng.html\"><strong>here<\/strong><\/a>.<\/em><\/p>\n","protected":false},"excerpt":{"rendered":"<p>The group of Christian L\u00f6w at EMBL Hamburg and CSSB, and collaborators from the Christian-Albrechts-University Kiel and CNRS &#038; Universit\u00e9 Paris Cit\u00e9 worked together to reveal the structure and function of a previously unknown lysosome transporter, MFSD1.<\/p>\n","protected":false},"author":16,"featured_media":68397,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[17591],"tags":[64,775,53,461,35],"embl_taxonomy":[9596,19325],"class_list":["post-68391","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science-technology","tag-cell-biology","tag-cssb","tag-hamburg","tag-low","tag-structural-biology","embl_taxonomy-embl-hamburg","embl_taxonomy-low-group-visiting"],"acf":{"featured":true,"show_featured_image":false,"field_target_display":"embl","field_article_language":{"value":"english","label":"English"},"article_intro":"","related_links":[{"link_description":"L\u00f6w Group","link_url":"https:\/\/www.embl.org\/groups\/loew\/"},{"link_description":"The secret of molecular promiscuity ","link_url":"https:\/\/www.embl.org\/news\/embletc\/issue-101\/the-secret-of-molecular-promiscuity\/"},{"link_description":"Structure of a promiscuous protein will help scientists design better drugs","link_url":"https:\/\/www.embl.org\/news\/science\/structure-of-promiscuous-protein-will-help-scientists-design-better-drugs\/"}],"source_article":[{"publication_title":"MFSD1 with its accessory subunit GLMP functions as a general dipeptide uniporter in lysosomes","publication_link":{"title":"","url":"https:\/\/www.nature.com\/articles\/s41556-024-01436-5","target":"_blank"},"publication_authors":"Jungnickel, K.E.J., Guelle, O., Iguchi, M., et al.","publication_source":"Nature Cell Biology","publication_date":"5 June 2024","publication_doi":"10.1038\/s41556-024-01436-5"}],"in_this_article":false,"press_contact":"None","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; 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