{"id":21908,"date":"2022-04-01T14:04:15","date_gmt":"2022-04-01T18:04:15","guid":{"rendered":"https:\/\/www.med.unc.edu\/biochem\/?p=21908"},"modified":"2022-04-01T14:53:51","modified_gmt":"2022-04-01T18:53:51","slug":"scientists-unravel-new-details-for-entry-into-cells","status":"publish","type":"post","link":"https:\/\/www.med.unc.edu\/biochem\/news\/scientists-unravel-new-details-for-entry-into-cells\/","title":{"rendered":"Scientists unravel new details for entry into cells"},"content":{"rendered":"<p>Researchers at the University of North Carolina at Chapel Hill and the UNC Lineberger Comprehensive Cancer Center have uncovered a new checkpoint that cells use to control what molecules they internalize. Understanding the determinants for entry into cells could lead to the design of better therapeutics that must enter through this gatekeeping mechanism.<\/p>\n<p>Every cell in the body relies on a process called endocytosis to control what molecules are allowed inside and is often broken or misregulated in cancers and heart disease. UNC researchers now show that endocytosis has a \u201ccheckpoint\u201d that allows for precise control of what molecules, or \u201ccargo\u201d, are allowed inside cells.<\/p>\n<p>To understand this checkpoint at the molecular scale, they teamed with a team of geneticists at the Cornell University College of Veterinary Medicine who had previously shown that a family of proteins called Muniscins are important regulators of endocytosis. Using a cutting-edge technique called cryo-electron microscopy (cryo-EM), the team showed that Muniscins alter the conformation of a key endocytic protein complex called AP2.<\/p>\n<p><a href=\"https:\/\/www.nature.com\/articles\/s41594-022-00749-z\">Their findings were published<\/a> online on March 28<sup>th<\/sup>, 2022 in Nature Structure and Molecular Biology. A free PDF version of the manuscript is available here: <a href=\"https:\/\/rdcu.be\/cJ0ur\">https:\/\/rdcu.be\/cJ0ur<\/a>.<\/p>\n<p>\u201cAP2 is an important protein complex and is required for controlling how many medically-relevant molecules, like viruses and cholesterol, enter cells,\u201d said UNC Lineberger\u2019s\u00a0<a href=\"https:\/\/unclineberger.org\/directory\/rick-baker\/\">Rick Baker, PhD<\/a>, assistant professor of Biochemistry and Biophysics at the UNC School of Medicine and co-lead author of this research article. \u201cWe were really surprised that Muniscins could drastically alter the shape of AP2 and that this would have profound effects on AP2 function.\u201d<\/p>\n<figure id=\"attachment_21909\" class=\"thumbnail wp-caption alignleft\" style=\"width: 427px\"><img loading=\"lazy\" decoding=\"async\" class=\"wp-image-21909\" src=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Baker-Figure-1.-Model-for-interplay-between-Muniscins-and-AP2-300x140.png\" alt=\"Figure 1. Model for interplay between Muniscins and AP2. Muniscins promote a specific conformation of AP2, which has not been described previously. This AP2 conformation selects for specific cargo that need to be internalized during endocytosis. \" width=\"417\" height=\"195\" srcset=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Baker-Figure-1.-Model-for-interplay-between-Muniscins-and-AP2-300x140.png 300w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Baker-Figure-1.-Model-for-interplay-between-Muniscins-and-AP2-1024x478.png 1024w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Baker-Figure-1.-Model-for-interplay-between-Muniscins-and-AP2-768x359.png 768w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Baker-Figure-1.-Model-for-interplay-between-Muniscins-and-AP2-1536x717.png 1536w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Baker-Figure-1.-Model-for-interplay-between-Muniscins-and-AP2-2048x957.png 2048w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Baker-Figure-1.-Model-for-interplay-between-Muniscins-and-AP2-600x280.png 600w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Baker-Figure-1.-Model-for-interplay-between-Muniscins-and-AP2-560x262.png 560w\" sizes=\"auto, (max-width: 417px) 100vw, 417px\" \/><figcaption class=\"caption wp-caption-text\"><strong>Figure 1. Model for interplay between Muniscins and AP2.<\/strong><br \/><em>Muniscins promote a specific conformation of AP2, which has not been described previously. This AP2 conformation selects for specific cargo that needs to be internalized during endocytosis.<\/em><\/figcaption><\/figure>\n<p>AP2 can readily change its shape and adopt multiple conformations. The researchers found that Muniscins bind to AP2 and promote a new conformation that had not been described previously. This new Muniscin-bound conformation makes AP2 more likely to select one particular type of cargo for internalization. Once AP2 finds this cargo, the Muniscin releases the AP2-cargo complex and finds another copy of AP2 to start the process over again (Figure 1). \u201cMuniscins seem to make AP2 fall in love with one specific type of cargo. AP2 needs to select from hundreds of possible cargo and controlling AP2 conformation seems to be one way that cells decide which cargo they want to bring inside,\u201d said Kevin Cannon, PhD, a postdoctoral researcher in the UNC Biochemistry and Biophysics department and second author of the work.<\/p>\n<figure id=\"attachment_21911\" class=\"thumbnail wp-caption alignright\" style=\"width: 310px\"><img loading=\"lazy\" decoding=\"async\" class=\"size-medium wp-image-21911\" src=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Rick-Baker-PhD-and-Kevin-Cannon-PhD-300x163.png\" alt=\"Rick Baker PhD and Kevin Cannon PhD shown in a lab\" width=\"300\" height=\"163\" srcset=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Rick-Baker-PhD-and-Kevin-Cannon-PhD-300x163.png 300w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Rick-Baker-PhD-and-Kevin-Cannon-PhD-600x325.png 600w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Rick-Baker-PhD-and-Kevin-Cannon-PhD-560x303.png 560w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Rick-Baker-PhD-and-Kevin-Cannon-PhD.png 681w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><figcaption class=\"caption wp-caption-text\">Rick Baker Ph.D. and Kevin Cannon Ph.D.<\/figcaption><\/figure>\n<p>Previous research has suggested that endocytosis operates in a less controlled manner. \u201cResearchers often like to think of endocytosis as a cellular process that runs more or less on autopilot.\u201d Rick Baker said. \u201cOur work suggests that this process is more tightly controlled than we had previously appreciated and provides new insight into diseases like cancer where entry of one particular protein, like receptor tyrosine kinases, directly underpins the disease state.\u201d<\/p>\n<p><strong>Authors and disclosures<\/strong><\/p>\n<p>In addition to Rick Baker Ph.D. and Kevin Cannon Ph.D., the study\u2019s authors are graduate student Ed Partlow and co-lead investigator Gunther Hollopeter, both of Cornell University College of Veterinary Medicine.<\/p>\n<p><em>This work was supported in part by grants from the National Institutes of Health, R01GM127548. The authors declare no competing interests.<\/em><\/p>\n<p>&nbsp;<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Researchers in Biochemistry and Biophysics (Rick Baker and Kevin Cannon) and collaborators have uncovered a new checkpoint that cells use to control what molecules they internalize. Understanding the determinants for entry into cells could lead to the design of better therapeutics that must enter through this gatekeeping mechanism.<\/p>\n","protected":false},"author":41619,"featured_media":21911,"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":[10,378,179],"class_list":["post-21908","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-news","tag-news_faculty","tag-news_2022","tag-news_postdoc-scholars","odd"],"acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.8 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>Scientists unravel new details for entry into cells | Biochemistry and Biophysics<\/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:\/\/www.med.unc.edu\/biochem\/news\/scientists-unravel-new-details-for-entry-into-cells\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Scientists unravel new details for entry into cells | Biochemistry and Biophysics\" \/>\n<meta property=\"og:description\" content=\"Researchers in Biochemistry and Biophysics (Rick Baker and Kevin Cannon) and collaborators have uncovered a new checkpoint that cells use to control what molecules they internalize. Understanding the determinants for entry into cells could lead to the design of better therapeutics that must enter through this gatekeeping mechanism.\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.med.unc.edu\/biochem\/news\/scientists-unravel-new-details-for-entry-into-cells\/\" \/>\n<meta property=\"og:site_name\" content=\"Biochemistry and Biophysics\" \/>\n<meta property=\"article:publisher\" content=\"https:\/\/www.facebook.com\/uncbiochemistryandbiophysics\/\" \/>\n<meta property=\"article:published_time\" content=\"2022-04-01T18:04:15+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2022-04-01T18:53:51+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Rick-Baker-PhD-and-Kevin-Cannon-PhD.png\" \/>\n\t<meta property=\"og:image:width\" content=\"681\" \/>\n\t<meta property=\"og:image:height\" content=\"369\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/png\" \/>\n<meta name=\"author\" content=\"Carolyn Clabo\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:creator\" content=\"@UNC_BCBP\" \/>\n<meta name=\"twitter:site\" content=\"@UNC_BCBP\" \/>\n<meta name=\"twitter:label1\" content=\"Written by\" \/>\n\t<meta name=\"twitter:data1\" content=\"Carolyn Clabo\" \/>\n\t<meta name=\"twitter:label2\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data2\" content=\"3 minutes\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\/\/schema.org\",\"@graph\":[{\"@type\":\"Article\",\"@id\":\"https:\/\/www.med.unc.edu\/biochem\/news\/scientists-unravel-new-details-for-entry-into-cells\/#article\",\"isPartOf\":{\"@id\":\"https:\/\/www.med.unc.edu\/biochem\/news\/scientists-unravel-new-details-for-entry-into-cells\/\"},\"author\":{\"name\":\"Carolyn Clabo\",\"@id\":\"https:\/\/www.med.unc.edu\/biochem\/#\/schema\/person\/9693a4e0a76e8208ca2105ae25587332\"},\"headline\":\"Scientists unravel new details for entry into cells\",\"datePublished\":\"2022-04-01T18:04:15+00:00\",\"dateModified\":\"2022-04-01T18:53:51+00:00\",\"mainEntityOfPage\":{\"@id\":\"https:\/\/www.med.unc.edu\/biochem\/news\/scientists-unravel-new-details-for-entry-into-cells\/\"},\"wordCount\":597,\"publisher\":{\"@id\":\"https:\/\/www.med.unc.edu\/biochem\/#organization\"},\"image\":{\"@id\":\"https:\/\/www.med.unc.edu\/biochem\/news\/scientists-unravel-new-details-for-entry-into-cells\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2022\/04\/Rick-Baker-PhD-and-Kevin-Cannon-PhD.png\",\"keywords\":[\"Faculty &amp; 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