{"id":27724,"date":"2020-08-10T00:00:23","date_gmt":"2020-08-10T07:00:23","guid":{"rendered":"https:\/\/vermont.salk.edu\/?post_type=disclosure&p=27724"},"modified":"2024-01-30T14:40:02","modified_gmt":"2024-01-30T22:40:02","slug":"imaging-method-highlights-new-role-for-cellular-skeleton-protein","status":"publish","type":"disclosure","link":"https:\/\/www.salk.edu\/zh\/news-release\/imaging-method-highlights-new-role-for-cellular-skeleton-protein\/","title":{"rendered":"Imaging method highlights new role for cellular \u201cskeleton\u201d protein"},"content":{"rendered":"

LA JOLLA\u2014While your skeleton helps your body to move, fine skeleton-like filaments within your cells likewise help cellular structures to move. Now, Salk researchers have developed a new imaging method that lets them monitor a small subset of these filaments, called actin.<\/p>\n

\u201cActin is the most abundant protein in the cell, so when you image it, it\u2019s all over the cell,\u201d says Uri Manor<\/a>, director of Salk\u2019s Biophotonics Core facility and corresponding author of the paper. \u201cUntil now, it\u2019s been really hard to tell where individual actin molecules of interest are, because it\u2019s difficult to separate the relevant signal from all the background.\u201d<\/p>\n

\"A<\/a>
A cancer cell labeled for actin (red) and mitochondria (cyan). The scientists designed novel probes that specifically monitor interactions between actin and mitochondria.<\/p>\n

Click here<\/a> for a high-resolution image.<\/p>\n

Credit: Salk Institute\/Waitt Advanced Biophotonics Center<\/figcaption><\/figure>\n

With the new imaging technique, the Salk team has been able to home in on how actin mediates an important function: helping the cellular \u201cpower stations\u201d known as mitochondria divide in two. The work, which appeared in the journal Nature Methods<\/em><\/a> on August 10, 2020, could provide a better understanding of mitochondrial dysfunction, which has been linked to cancer, aging, and neurodegenerative diseases.<\/p>\n

Mitochondrial fission is the process by which these energy-generating structures, or organelles, divide and multiply as part of normal cellular maintenance; the organelles divide not only when a cell itself is dividing, but also when cells are under high amounts of stress or mitochondria are damaged. However, the exact way in which one mitochondrion pinches off into two mitochondria has been poorly understood, particularly how the initial constriction happens. Studies have found that removing actin from a cell entirely, among many other effects, leads to less mitochondrial fission, suggesting a role for actin in the process. But destroying all the actin causes so many cellular defects that it\u2019s hard to study the protein\u2019s exact role in any one process, the researchers say.<\/p>\n

So, Manor and his colleagues developed a new way to image actin. Rather than tag all the actin in the cell with fluorescence, they created an actin probe targeted to the outer membrane of mitochondria. Only when actin is within 10 nanometers of the mitochondria does it attach to the sensor, causing the fluorescence signal to increase.<\/p>\n

Rather than see actin scattered haphazardly around all mitochondrial membranes, as they might if there were no discrete interactions between actin and the organelles, Manor\u2019s team saw bright hotspots of actin. And when they looked closely, the hotspots were located at the same locations where another organelle called the endoplasmic reticulum crosses the mitochondria, previously found to be fission sites. Indeed, as the team watched actin hotspots light up and disappear over time, they discovered that 97 percent of mitochondrial fission sites had actin fluorescing around them. (They speculate that there was also actin at the other 3 percent of fission sites, but that it wasn\u2019t visible).<\/p>\n

\u201cThis is the clearest evidence I\u2019ve ever seen that actin is accumulating at fission sites,\u201d says Cara Schiavon, co-first author of the paper and a joint postdoctoral fellow in the labs of Uri Manor and Salk Professor Gerald Shadel<\/a>. \u201cIt\u2019s much easier to see than when you use any other actin marker.\u201d<\/p>\n

By altering the actin probe so that it attached to the endoplasmic reticulum membrane rather than the mitochondria, the researchers were able to piece together the order in which different components join the mitochondrial fission process. The team\u2019s results suggest that the actin attaches to the mitochondria before it reaches the endoplasmic reticulum. This lends important insight towards how the endoplasmic reticulum and mitochondria work together to coordinate mitochondrial fission.<\/p>\n

\"Uri
From left: Uri Manor, Cara Schiavon and Tong Zhang.<\/p>\n

Click here<\/a> for a high-resolution image.<\/p>\n

Credit: Salk Institute<\/figcaption><\/figure>\n

In additional experiments described in a pre-print manuscript available on bioRxiv<\/a>, Manor\u2019s team also reports that the same accumulation of endoplasmic reticulum-associated actin is seen at the sites where other cellular organelles\u2014including endosomes, lysosomes and peroxisomes\u2014divide. This suggests a broad new role for a subset of actin in organelle dynamics and homeostasis (physiological equilibrium).<\/p>\n

In the future, the team hopes to look at how genetic mutations known to alter mitochondrial dynamics might also affect actin\u2019s interactions with the mitochondria. They also plan to adapt the actin probes to visualize actin that\u2019s close to other cellular membranes.<\/p>\n

\u201cThis is a universal tool that can now be used for many different applications,\u201d says Tong Zhang, a light microscopy specialist at Salk and co-first author of the paper. \u201cBy switching out the targeting sequence or the nanobody, you can address other fundamental questions in cell biology.\u201d<\/p>\n

\u201cWe\u2019re in a golden age of microscopy, where new instruments with ever higher resolution are always being invented; but in spite of that there are still major limitations to what you can see,\u201d says Manor. \u201cI think combining these powerful microscopes with new methods that select for exactly what you want to see is the next generation of imaging.\u201d<\/p>\n

Other researchers on the study were Pauline Wales, Leonardo Andrade, Melissa Wu, Tsung-Chang Sung, Yelena Dayn, and Gerald Shadel of Salk; Bing Zhao and Robert Grosse of the University of Freiburg; Andrew Moore of the Howard Hughes Medical Institute; and Jasmine Feng and Omar Quintero of the University of Richmond.<\/p>\n

The Waitt Advanced Biophotonics Center (home of Salk\u2019s Biophotonics Core facility) is funded by the Waitt Foundation and National Cancer Institute. The work and researchers involved were also supported by the Salk Transgenic Core Facility, National Institutes of Health, National Institute of General Medical Sciences, Human Frontier Science Program, Centre for Integrative Biological Signaling Studies, and the University of Richmond School of Arts & Sciences.<\/p>","protected":false},"featured_media":27834,"template":"","faculty":[405],"disease-research":[46,146,124],"class_list":["post-27724","disclosure","type-disclosure","status-publish","has-post-thumbnail","hentry","faculty-uri-manor","disease-research-cancer-biology","disease-research-aging-and-regenerative-medicine","disease-research-neuroscience-and-neurological-disorders"],"acf":[],"yoast_head":"\nImaging method highlights new role for cellular \u201cskeleton\u201d protein - Salk Institute for Biological Studies<\/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.salk.edu\/zh\/news-release\/imaging-method-highlights-new-role-for-cellular-skeleton-protein\/\" \/>\n<meta property=\"og:locale\" content=\"zh_CN\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Imaging method highlights new role for cellular \u201cskeleton\u201d protein - Salk Institute for Biological Studies\" \/>\n<meta property=\"og:description\" content=\"LA JOLLA\u2014While your skeleton helps your body to move, fine skeleton-like filaments within your cells likewise help cellular structures to move. 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