{"id":29424,"date":"2020-09-03T11:00:00","date_gmt":"2020-09-03T09:00:00","guid":{"rendered":"https:\/\/www.embl.org\/news\/?p=29424"},"modified":"2024-08-29T14:11:57","modified_gmt":"2024-08-29T12:11:57","slug":"nuclear-pores-in-their-natural-context","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/nuclear-pores-in-their-natural-context\/","title":{"rendered":"Nuclear pores in their natural context"},"content":{"rendered":"\n

EMBL scientists study the 3D structure of nuclear pores in yeast cells<\/h2>\n\n\n\n

Scientists from the Beck group at EMBL Heidelberg<\/a>, in collaboration with the Kosinski group at EMBL Hamburg<\/a> and the Pfander group at the Max Planck Institute of Biochemistry in Martinsried<\/a>, have studied the 3D structure of nuclear pores in budding yeast (Saccharomyces cerevisiae<\/em>). Their findings, published in Nature<\/em>, show how the architecture of the nuclear pore complex differs inside cells compared to its form observed in vitro<\/em> studies, and increases our understanding of crucial processes of life.<\/p>\n\n\n\n

Nuclear pores are a highly complex assembly of proteins. Thousands of them are embedded in the double membrane that surrounds and protects the cell\u2019s nucleus. They act as a gateway that regulates the entry and exit of hundreds of thousands of molecules every minute. An important function of nuclear pores is to regulate the export of a molecule called messenger RNA (mRNA) from the nucleus into the surrounding cell \u2013 the cytoplasm \u2013 where it delivers instructions for the assembly of proteins.<\/p>\n\n\n\n

Revealing the architecture<\/h2>\n\n\n\n

\u201cWe now appreciate better how the nuclear pore works in its native context, and what happens to the pore during physiological, pathological, or starved conditions,\u201d says group leader Martin Beck, who led the structural work. The study provided a detailed structural description of the three protein rings that make up the nuclear pore, known as the cytoplasmic, nuclear, and inner rings. To show how these rings are arranged in cells, EMBL researchers used a combination of cell biology, computational modelling, and in-cell cryo-electron tomography: an imaging technique, under active development at EMBL<\/a>, that is used to produce high-resolution 3D views of the molecular landscape inside a cell.<\/p>\n\n\n\n

One of the study\u2019s goals was to find out if the architecture of the nuclear pore would differ inside the crowded environment of a cell, compared to in vitro<\/em> studies. Using cryo-electron tomography, the Beck group captured images of nuclear pores inside yeast cells. As they\u2019d expected, the scientists discovered that some parts of the nuclear pore complex, when observed in cells, had different spatial configurations in comparison to previous in vitro<\/em> studies. This led to fundamental new insights. \u201cWe found out that the 3D configuration of the cytoplasmic ring accommodates the path of mRNA export,\u201d says Matteo Allegretti, a postdoc in the Beck group and first author of the study.<\/p>\n\n\n\n

Understanding the life cycle<\/h2>\n\n\n\n

The structure of the cytoplasmic ring also serves another function \u2013 it exposes a certain domain of a protein to the cytoplasm. This domain interacts with proteins that facilitate the process by which nuclear pores are broken down by the cell and replaced with new ones \u2013 a process known as autophagic turnover. How exactly the architecture of nuclear pores facilitates the breakdown process \u2013 autophagy \u2013 and assembly of nuclear pores is largely unknown, but this study provides important first steps towards a better understanding of these mechanisms. \u201cWith knowledge coming from many different structures, we\u2019re closer to understanding how nuclear pores assemble and how the pore evolved from the first cells with a nucleus up to now,\u201d says group leader Jan Kosinski, who led the computational modelling.<\/p>\n\n\n\n

To better understand the assembly of nuclear pores, the researchers grew a yeast strain missing a protein called nucleoporin 116, which plays an important role in the assembly process. The resulting structure was missing the cytoplasmic ring and part of the inner ring. The scientists conclude that these incomplete structures show intermediate states of nuclear pore assembly. Studying this process is important, as failures in the assembly of nuclear pores lead to the death of the cell and have been linked to neurodegenerative diseases. The study yielded detailed structures that scientists from other institutions can use in various ways, for example to study nuclear pore function, how molecules are transported into or out of the nucleus, or how viruses enter the nucleus. Many viruses, such as influenza and SARS\u2011CoV\u20112, need to get their genetic information past the nuclear pore complex to infect a cell. \u201cIt also shows the scientific community that we need to shift scientific efforts towards the investigation of the structure\u2013function relationship of macromolecules directly inside the cell,\u201d says Matteo. Fundamental processes of life, such as nuclear transport and autophagy, can be understood by combining technologies like cryo-electron tomography with structural modelling, light microscopy, and biochemistry.<\/p>\n","protected":false},"excerpt":{"rendered":"

Scientists from the Beck group have studied the 3D structure of nuclear pores in budding yeast. They show how the architecture of the nuclear pore complex differs inside cells compared to its form observed in vitro studies.<\/p>\n","protected":false},"author":69,"featured_media":29430,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[350,712,53,43,876,540,1790,4686,35,768],"embl_taxonomy":[9796,5152],"class_list":["post-29424","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-beck","tag-cryo-electron-tomography","tag-hamburg","tag-heidelberg","tag-integrative-modelling","tag-kosinski","tag-nuclear-pore","tag-nucleus","tag-structural-biology","tag-yeast","embl_taxonomy-embl-heidelberg","embl_taxonomy-molecular-systems-biology"],"acf":{"featured":true,"color":"#007B53","show_featured_image":false,"article_intro":"

The architecture of the nuclear pore complex differs inside cells compared to its form observed in vitro<\/em> studies, and increases our understanding of crucial processes of life.<\/p>\n","article_sources":[{"source_description":"

Matteo Allegretti, et al. In-cell architecture of the nuclear pore and snapshots of its turnover. Nature<\/em>, published on 2 September 2020, DOI: 10.1038\/s41586-020-2670-5<\/p>\n","source_link_url":"https:\/\/www.nature.com\/articles\/s41586-020-2670-5"}],"related_links":[{"link_description":"New perspectives on nuclear pores","link_url":"https:\/\/www.embl.org\/news\/science\/new-perspectives-on-nuclear-pores\/"},{"link_description":"Watching nuclear pores in growing nuclei","link_url":"https:\/\/www.embl.org\/news\/science\/160923-watching-nuclear-pores-grow\/"},{"link_description":"Revealing structure of nuclear pore\u2019s inner ring","link_url":"https:\/\/www.embl.org\/news\/science\/1604-nuclear-pore\/"},{"link_description":"Centre for Structural Systems Biology in Hamburg","link_url":"https:\/\/www.cssb-hamburg.de\/"},{"link_description":"Max Planck Institute of Biochemistry (MPIB) in Martinsried","link_url":"https:\/\/www.biochem.mpg.de\/"}],"in_this_article":false,"youtube_url":"","mp4_url":"","video_caption":"","press_contact":"EMBL 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