Hard labor might be the very thing we try to avoid on Labor Day. But our cells and their components don’t have the luxury of taking a day off. Their non-stop work is what keeps us going and healthy.
Scientists often compare cells with small factories. Just like a factory, a cell contains specialized compartments and machines—including organelles and other structures—that each play their own roles in getting the job done. In the vignettes below, we give a shout out to some of these tireless cellular workers.
Mitochondria are the cell’s power plants. They convert energy from food into a molecule called ATP that fuels virtually every process in the cell. As shown here, mitochondria (brown) often have distinct, oblong shapes. Like most other organelles, mitochondria are encased in an outer membrane. But they also have an inner membrane that folds many times, increasing the area available for energy production. In addition, mitochondria store calcium ions, help make hemoglobin—the vital iron-containing protein that allows red blood cells to carry oxygen—and even take part in producing some hormones. Defects in mitochondria can lead to a host of rare but often incurable diseases that range from mild to devastating. Researchers are studying mitochondria to better understand their manifold jobs in the cell and to find treatments for mitochondrial diseases.
Continue reading “A Labor Day-Themed Collection: Hard-Working Cell Structures”
Credit: Jeff Foley, American Heart Association.
Enrique M. De La Cruz
Grew up in: Newark and Kearny, New Jersey
Job site: Yale University
Favorite food: His mom’s Spanish-style polenta (harina de maíz)
Alternative career: Managing a vinyl record shop
Favorite song: “Do Anything You Wanna Do” by Eddie & The Hot Rods
Enrique De La Cruz stood off to the side in a packed room. As he waited for his turn to speak, he stroked the beads of a necklace. Was he nervous? Quietly praying? When he took center stage, the purpose of the strand became clear.
Like a magician—and dressed all in black—De La Cruz held up the necklace with two hands so everyone, even those sitting in the back, could see it. It was made of snap-together beads. De La Cruz waved the strand. It wiggled in different directions. Then, with no sleight of hand, he popped off one of the beads. The necklace broke into two.
For the next hour, De La Cruz pulled out one prop after another: a piece of rope from his pocket, a pencil tucked behind his ear and even a fresh spear of asparagus stuffed in his backpack. At one point, De La Cruz assembled a conga line with people in the front row. Continue reading “Protein Paradox: Enrique De La Cruz Aims to Understand Actin”
Our cells are constantly removing and recycling molecular waste. On the occasion of Earth Day, we put together this narrated animation to show you one way cells process their trash. The video features the proteasome, a cellular machine that breaks down damaged or unwanted proteins into bits that the cell can re-use to make new proteins. For this reason, the proteasome is as much a recycling plant as it is a garbage disposal.
For more details about the proteasome and other cellular disposal systems, check out our article How Cells Take Out the Trash.
Animated structural model of TSPO. Credit: Michigan State University.
Mitochondria have proteins that span their membranes to control the flow of messages and materials moving into and out of the organelle. One way scientists can learn more about how membrane proteins function—and how medicines might interact with them—is to determine their structures. But for a variety of reasons, obtaining the structures has been notoriously difficult.
Two structural studies have now shed light on the mysterious mitochondrial membrane protein TSPO. This protein plays a key role in transporting cholesterol and drugs into the cell’s mitochondria. While here, the cholesterol is converted to steroid hormones that are essential for numerous bodily functions. Although many researchers have been studying TSPO since the 1990s, they’ve remained uncertain about its mechanisms and how it truly functions. Continue reading “Structural Studies Demystify Membrane Protein”
Many of the key players in regulating apoptosis were discovered in C. elegans. This tiny roundworm has more than 19,000 genes, and a vast number of them are very similar to genes in other organisms, including people. Credit: Ewa M. Davison.
Our cells come equipped with a self-destruct mechanism that’s activated during apoptosis, a carefully controlled process by which the body rids itself of unneeded or potentially harmful cells. Scientists have long known that a protein called PSR-1 helps clean up the cellular remains. Now they’ve found that PSR-1 also can repair broken nerve fibers.
Ding Xue of the University of Colorado, Boulder, and others made the finding in the tiny roundworm C. elegans, which scientists have used to study apoptosis and identify many of the genes that regulate the process. While apoptotic cells sent “eat me” signals to PSR-1, injured nerve cells sent “save me” signals to the protein. These SOS signals helped reconnect the broken nerve fibers, called axons, that would otherwise degenerate after an injury. Continue reading “Surprising Role for Protein Involved in Cell Death”
Researchers are developing a system to remotely control genes or cells in living animals with radio wave technology similar to that used to operate remote control car keys. Credit: Stock image.
One of the items on biomedical researchers’ “to-do” list is devising noninvasive ways to control the activity of specific genes or cells in order to study what those genes or cells do and, ultimately, to treat a range of human diseases and disorders.
A team of scientists recently reported progress on a new, noninvasive system that could remotely and rapidly control biological targets in living animals. The system can be activated remotely using either low-frequency radio waves or a magnetic field. Similar radio wave technology operates automatic garage-door openers and remote control car keys and is used in medicine to control electronic pacemakers noninvasively. Magnetic fields are used to activate sensors in burglar alarm systems and to turn your laptop to hibernate mode when the cover is closed. Continue reading “Remotely and Noninvasively Controlling Genes and Cells in Living Animals”
NIGMS’ Jean Chin answers questions about a new device for untangling proteins. Credit: National Institute of General Medical Sciences.
It’s not every day that we log into Facebook and Twitter to see conversations about denaturing proteins and the possibility of reducing biotechnology costs, but that changed last week when a story about “unboiling” eggs became a trending topic.
Since NIGMS partially funded the research advance that led to the media scramble, we asked our scientific expert Jean Chin to tell us more about it.
What’s the advance?
Gregory Weiss of the University of California, Irvine, and his collaborators have designed a device that basically unties proteins that have been tangled together. Continue reading “Untangling a Trending Topic”
Scientists have discovered a possible mechanism behind the bad taste and dry mouth caused by some drugs. Credit: Stock image.
The effects some medicines have on our salivary glands can at times extend beyond the fleeting flavor we experience upon ingesting them. Sometimes drugs cause a prolonged bad taste or dryness in the mouth, both of which can discourage people from taking medicines they need. Now, a research team led by Joanne Wang of the University of Washington has discovered a possible mechanism behind this phenomenon. Working primarily with mice and using a commonly prescribed antidiabetic drug known to impair taste, the scientists identified a protein in salivary gland cells that takes up the drug from the bloodstream and secretes it in saliva. Wang and her colleagues were also able to pinpoint a specific gene that, when removed, hindered this process. They hope their new insights will aid efforts to develop medicines that do not cause salivary issues.
This work also was funded by NIH’s Eunice Kennedy Shriver National Institute of Child Health and Human Development.
University of Washington News Release
Receptor proteins bind to bacterial cell wall fragments, initiating an immune response to remove bad gut bacteria. Credit: S. Melanie Lee, Caltech; Zbigniew Mikulski and Klaus Ley, La Jolla Institute for Allergy and Immunology.
Our bodies depend on a set of immune receptors to remove harmful bacteria and control the growth of helpful bacteria in our guts. Genetic changes that alter the function of the receptors can have an adverse effect and result in chronic inflammatory diseases like Crohn’s disease. Catherine Leimkuhler Grimes and Vishnu Mohanan of the University of Delaware researched a Crohn’s-associated immune receptor, NOD2, to figure out how it can lose the ability to respond properly to bacteria. In the process, they identified the involvement of a protective protein called HSP70. Increasing HSP70 levels in kidney, colon and white blood cells appeared to restore NOD2 function. This work represents a first step toward developing drugs to treat Crohn’s disease.
This work was funded in part by an Institutional Development Award (IDeA) Network of Biomedical Research Excellence (INBRE) grant.