Two models for how material passes through the Golgi apparatus: the vesicular shuttle model and the cisternae maturation model.

Network diagram showing a map of protein-protein interactions in a yeast (Saccharomyces cerevisiae) cell. This cluster includes 78 percent of the proteins in the yeast proteome. The color of a node represents the phenotypic effect of removing the corresponding protein (red, lethal; green, nonlethal; orange, slow growth; yellow, unknown).

Mosquito larvae with genes edited by CRISPR. This species of mosquito, Culex quinquefasciatus, can transmit West Nile virus, Japanese encephalitis virus, and avian malaria, among other diseases. The researchers who took this image developed a gene-editing toolkit for Culex quinquefasciatus that could ultimately help stop the mosquitoes from spreading pathogens. The work is described in the Nature Communications paper "Optimized CRISPR tools and site-directed transgenesis towards gene drive development in Culex quinquefasciatus mosquitoes" by Feng et al. Related to image 6769 and video 6771.

A computer model of the cell membrane, where the plasma membrane is red, endoplasmic reticulum is yellow, and mitochondria are blue. This image relates to a July 27, 2009 article in Computing Life.

The proteasome is a critical multiprotein complex in the cell that breaks down and recycles proteins that have become damaged or are no longer needed. This movie shows how a protein substrate (red) is bound through its ubiquitin chain (blue) to one of the ubiquitin receptors of the proteasome (Rpn10, yellow). The substrate's flexible engagement region then gets engaged by the AAA+ motor of the proteasome (cyan), which initiates mechanical pulling, unfolding and movement of the protein into the proteasome's interior for cleavage into shorter protein pieces called peptides. During movement of the substrate, its ubiquitin modification gets cleaved off by the deubiquitinase Rpn11 (green), which sits directly above the entrance to the AAA+ motor pore and acts as a gatekeeper to ensure efficient ubiquitin removal, a prerequisite for fast protein breakdown by the 26S proteasome. Related to image 3763.

Each point in these colorful patchworks represents the correlation between two sleep-associated genes in fruit flies. Vibrant reds and oranges represent high and intermediate degrees of association between the genes, respectively. Genes in these areas show similar activity patterns in different fly lines. Cool blues represent gene pairs where one partner's activity is high and the other's is low. The green areas show pairs with activities that are not correlated. These quilt-like depictions help illustrate a recent finding that genes act in teams to influence sleep patterns.

A model of a Geobacter sulfurreducens nanowire created from cryo-electron microscopy images. The bacterium conducts electricity through these nanowires, which are made up of protein and iron-containing molecules.

The TRPA1 protein is responsible for the burn you feel when you taste a bite of sushi topped with wasabi. Known therefore informally as the "wasabi receptor," this protein forms pores in the membranes of nerve cells that sense tastes or odors. Pungent chemicals like wasabi or mustard oil cause the pores to open, which then triggers a tingling or burn on our tongue. This receptor also produces feelings of pain in response to chemicals produced within our own bodies when our tissues are damaged or inflamed. Researchers used cryo-EM to reveal the structure of the wasabi receptor at a resolution of about 4 angstroms (a credit card is about 8 million angstroms thick). This detailed structure can help scientists understand both how we feel pain and how we can limit it by developing therapies to block the receptor. For more on cryo-EM see the blog post Cryo-Electron Microscopy Reveals Molecules in Ever Greater Detail.

Many disease-causing microbes manipulate their host’s metabolism and cells for their own ends. Microsporidia—which are parasites closely related to fungi—infect and multiply inside animal cells, and take the rearranging of cells’ interiors to a new level. They reprogram animal cells such that the cells start to fuse, causing them to form long, continuous tubes. As shown in this image of the roundworm Caenorhabditis elegans, microsporidia (shown in red) have invaded the worm’s gut cells (the large blue dots are the cells' nuclei) and have instructed the cells to merge. The cell fusion enables the microsporidia to thrive and propagate in the expanded space. Scientists study microsporidia in worms to gain more insight into how these parasites manipulate their host cells. This knowledge might help researchers devise strategies to prevent or treat infections with microsporidia.

For more on the research into microsporidia, see this news release from the University of California San Diego. Related to images 5777 and 5778.

The microtubule severing protein, katanin, localizes to chromosomes and regulates anaphase A in mitosis. The movement of chromosomes on the mitotic spindle requires the depolymerization of microtubule ends. The figure shows the mitotic localization of the microtubule severing protein katanin (green) relative to spindle microtubules (red) and kinetochores/chromosomes (blue). Katanin targets to chromosomes during both metaphase (top) and anaphase (bottom) and is responsible for inducing the depolymerization of attached microtubule plus-ends. This image was a finalist in the 2008 Drosophila Image Award.

Researchers have learned much of what they know about membranes by constructing artificial membranes in the laboratory. In artificial membranes, different lipids separate from each other based on their physical properties, forming small islands called lipid rafts.

Model of the mandelate racemase enzyme from Bacillus subtilis, a bacterium commonly found in soil.

Cytoplasmic linker protein (CLIP)-170 is a microtubule plus-end-tracking protein that regulates microtubule dynamics and links microtubule ends to different intracellular structures. In this movie, the gene for CLIP-170 has been fused with green fluorescent protein (GFP). When the protein is expressed in cells, the activities can be monitored in real time. Here, you can see CLIP-170 streaming towards the edges of the cell.

Learn how curiosity about the world and our cells is key to scientific discoveries. Discover more resources from NIGMS’ Pathways collaboration with Scholastic. View the video on YouTube for closed captioning.

Microarrays, also called gene chips, are tools that let scientists track the activity of hundreds or thousands of genes simultaneously. For example, researchers can compare the activities of genes in healthy and diseased cells, allowing the scientists to pinpoint which genes and cell processes might be involved in the development of a disease.

Both instruments shown were developed by CellFree Sciences of Yokohama, Japan. The instrument on the left, the GeneDecoder 1000, can generate 384 proteins from their corresponding genes, or gene fragments, overnight. It is used to screen for properties such as level of protein production and degree of solubility. The instrument on the right, the Protemist Protein Synthesizer, is used to generate the larger amounts of protein needed for protein structure determinations.

The research organism Arabidopsis thaliana forms a large molecular machine called a resistosome to fight off infections. This illustration shows the top and side views of the fully-formed resistosome assembly (PDB entry 6J5T), composed of different proteins including one the plant uses as a decoy, PBL2 (dark blue), that gets uridylylated to begin the process of building the resistosome (uridylyl groups in magenta). Other proteins include RSK1 (turquoise) and ZAR1 (green) subunits. The ends of the ZAR1 subunits (yellow) form a funnel-like protrusion on one side of the assembly (seen in the side view). The funnel can carry out the critical protective function of the resistosome by inserting itself into the cell membrane to form a pore, which leads to a localized programmed cell death. The death of the infected cell helps protect the rest of the plant.

The glial cells (black dots) and nerve cells (brown bands) in this developing fruit fly nerve cord formed normally despite the absence of the SPITZ protein, which blocks their impending suicide. The HID protein, which triggers suicide, is also lacking in this embryo.

This illustration shows, in simplified terms, how the CRISPR-Cas9 system can be used as a gene-editing tool. The CRISPR system has two components joined together: a finely tuned targeting device (a small strand of RNA programmed to look for a specific DNA sequence) and a strong cutting device (an enzyme called Cas9 that can cut through a double strand of DNA). This frame (4 out of 4) shows a repaired DNA strand with new genetic material that researchers can introduce, which the cell automatically incorporates into the gap when it repairs the broken DNA.

For an explanation and overview of the CRISPR-Cas9 system, see the iBiology video, and find the full CRIPSR illustration here.

Myelinated axons in a rat spinal root. Myelin is a type of fat that forms a sheath around and thus insulates the axon to protect it from losing the electrical current needed to transmit signals along the axon. The axoplasm inside the axon is shown in pink. Related to 3397.

PETase enzyme degrades polyester plastic (polyethylene terephthalate, or PET) into monohydroxyethyl terephthalate (MHET). Then, MHETase enzyme degrades MHET into its constituents ethylene glycol (EG) and terephthalic acid (TPA).

Find these in the RCSB Protein Data Bank: PET hydrolase (PDB entry 5XH3) and MHETase (PDB entry 6QGA).

This Petri dish contains microscopic roundworms called Caenorhabditis elegans. Researchers used these particular worms to study how C. elegans senses the color of light in its environment.

Shortly after a pregnant woman gives birth, her breasts start to secrete milk. This process is triggered by hormonal and genetic cues, including the protein Elf5. Scientists discovered that Elf5 also has another job--it staves off cancer. Early in the development of breast cancer, human breast cells often lose Elf5 proteins. Cells without Elf5 change shape and spread readily--properties associated with metastasis. This image shows cells in the mouse mammary gland that are lacking Elf5, leading to the overproduction of other proteins (red) that increase the likelihood of metastasis.

This image shows a cell in two stages of division: prometaphase (top) and metaphase (bottom). To form identical daughter cells, chromosome pairs (blue) separate via the attachment of microtubules made up of tubulin proteins (pink) to specialized structures on centromeres (green).

Normal mice, like the B6 breed pictured on the left, develop scars when their ears are pierced. The Murphy Roths Large (MRL) mice pictured on the right can grow back lost ear tissue thanks to an inactive version of the p21 gene. When researchers knocked out that same gene in other mouse breeds, their ears also healed completely without scarring. Journal Article: Clark, L.D., Clark, R.K. and Heber-Katz, E. 1998. A new murine model for mammalian wound repair and regeneration. Clin Immunol Immunopathol 88: 35-45.

Ecteinascidin 743 (ET-743, brand name Yondelis), was discovered and isolated from a sea squirt, Ecteinascidia turbinata, by NIGMS grantee Kenneth Rinehart at the University of Illinois. It was synthesized by NIGMS grantees E.J. Corey and later by Samuel Danishefsky. Multiple versions of this structure are available as entries 2790-2797.

Telophase during mitosis: Nuclear membranes form around each of the two sets of chromosomes, the chromosomes begin to spread out, and the spindle begins to break down. Mitosis is responsible for growth and development, as well as for replacing injured or worn out cells throughout the body. For simplicity, mitosis is illustrated here with only six chromosomes.

Opioid receptors on the surfaces of brain cells are involved in pleasure, pain, addiction, depression, psychosis, and other conditions. The receptors bind to both innate opioids and drugs ranging from hospital anesthetics to opium. Researchers at The Scripps Research Institute, supported by the NIGMS Protein Structure Initiative, determined the first three-dimensional structure of a human opioid receptor, a kappa-opioid receptor. In this illustration, the submicroscopic receptor structure is shown while bound to an agonist (or activator). The structure is superimposed on a poppy flower, the source of opium.

Arranging exons in different patterns, called alternative splicing, enables cells to make different proteins from a single gene. See image 2553 for a labeled version of this illustration. Featured in The New Genetics.

Time lapse series shows short dynamin assemblies (not visible) constricting a lipid tube to make a "beads on a string" appearance, then cutting off one of the beads i.e., catalyzing membrane fission). The lipids are fluorescent (artificially colored). Ramachandran R, Pucadyil T.J., Liu Y.W., Acharya S., Leonard M., Lukiyanchuk V., Schmid S.L. 2009. Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission. Mol Biol Cell. 2009 20:4630-9.

The nucleolus is a small but very important protein complex located in the cell's nucleus. It forms on the chromosomes at the location where the genes for the RNAs are that make up the structure of the ribosome, the indispensable cellular machine that makes proteins from messenger RNAs.

However, how the nucleolus grows and maintains its structure has puzzled scientists for some time. It turns out that even though it looks like a simple liquid blob, it's rather well-organized, consisting of three distinct layers: the fibrillar center, where the RNA polymerase is active; the dense fibrillar component, which is enriched in the protein fibrillarin; and the granular component, which contains a protein called nucleophosmin. Researchers have now discovered that this multilayer structure of the nucleolus arises from differences in how the proteins in each compartment mix with water and with each other. These differences let the proteins readily separate from each other into the three nucleolus compartments.

This video of nucleoli in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows how each of the compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue) spontaneously fuse with each other on encounter without mixing with the other compartments.

For more details on this research, see this press release from Princeton. Related to video 3789, image 3792 and image 3793.

This image is a computer-generated model of the approximately 4.2 million atoms of the HIV capsid, the shell that contains the virus' genetic material. Scientists determined the exact structure of the capsid and the proteins that it's made of using a variety of imaging techniques and analyses. They then entered these data into a supercomputer that produced the atomic-level image of the capsid. This structural information could be used for developing drugs that target the capsid, possibly leading to more effective therapies. Related to image 6601.

A protein called tubulin (green) accumulates in the center of a nucleus (outlined in pink) from an aging cell. Normally, this protein is kept out of the nucleus with the help of gatekeepers known as nuclear pore complexes. But NIGMS-funded researchers found that wear and tear to long-lived components of the complexes eventually lowers the gatekeepers' guard. As a result, cytoplasmic proteins like tubulin gain entry to the nucleus while proteins normally confined to the nucleus seep out. The work suggests that finding ways to stop the leakage could slow the cellular aging process and possibly lead to new therapies for age-related diseases.

Floral pattern emerging as two bacterial species, motile Acinetobacter baylyi and non-motile Escherichia coli (green), are grown together for 72 hours on 0.5% agar surface from a small inoculum in the center of a Petri dish.

See 6557 for a photo of this process at 24 hours on 0.75% agar surface.
See 6553 for a photo of this process at 48 hours on 1% agar surface.
See 6555 for another photo of this process at 48 hours on 1% agar surface.
See 6550 for a video of this process.

A three-dimensional representation of the structure of E2, a key antigen protein involved with hepatitis C virus infection.

Cdc42, a member of the Rho family of small guanosine triphosphatase (GTPase) proteins, regulates multiple cell functions, including motility, proliferation, apoptosis, and cell morphology. In order to fulfill these diverse roles, the timing and location of Cdc42 activation must be tightly controlled. Klaus Hahn and his research group use special dyes designed to report protein conformational changes and interactions, here in living neutrophil cells. Warmer colors in this image indicate higher levels of activation. Cdc42 looks to be activated at cell protrusions.

Related to images 2451, 2452, and 2453.

Yeast cells with the protein Fimbrin Fim1 shown in magenta. This protein plays a role in cell division. This image was captured using wide-field microscopy with deconvolution.

Related to images 6791, 6792, 6793, 6797, 6798, and videos 6795 and 6796.

Two fruit fly (Drosophila melanogaster) egg cells, one on each side of the central black line. The colorful swirls show the circular movement of cytoplasm—called ooplasmic streaming—that occurs in late egg cell development in wild-type (right) and mutant (left) oocytes. This image was captured using confocal microscopy.

More information on the research that produced this image can be found in the Journal of Cell Biology paper “Ooplasmic flow cooperates with transport and anchorage in Drosophila oocyte posterior determination” by Lu et al.

A biofilm is a highly organized community of microorganisms that develops naturally on certain surfaces. These communities are common in natural environments and generally do not pose any danger to humans. Many microbes in biofilms have a positive impact on the planet and our societies. Biofilms can be helpful in treatment of wastewater, for example. This dime-sized biofilm, however, was formed by the opportunistic pathogen Pseudomonas aeruginosa. Under some conditions, this bacterium can infect wounds that are caused by severe burns. The bacterial cells release a variety of materials to form an extracellular matrix, which is stained red in this photograph. The matrix holds the biofilm together and protects the bacteria from antibiotics and the immune system.

A light microscope image of a cell from the endosperm of an African globe lily (Scadoxus katherinae). This is one frame of a time-lapse sequence that shows cell division in action. The lily is considered a good organism for studying cell division because its chromosomes are much thicker and easier to see than human ones. Staining shows microtubules in red and chromosomes in blue. Here, condensed chromosomes are clearly visible and are starting to separate to form two new cells.

Ribonucleic acid (RNA) has a sugar-phosphate backbone and the bases adenine (A), cytosine (C), guanine (G), and uracil (U). See image 2555 for a labeled version of this illustration. Featured in The New Genetics.

Although they are tiny, microbes that are growing in confined spaces can generate a lot of pressure. In this video, yeast cells grow in a small chamber called a microfluidic bioreactor. As the cells multiply, they begin to bump into and squeeze each other, resulting in periodic bursts of cells moving into different parts of the chamber. The continually growing cells also generate a lot of pressure--the researchers conducting these experiments found that the pressure generated by the cells can be almost five times higher than that in a car tire--about 150 psi, or 10 times the atmospheric pressure. Occasionally, this pressure even caused the small reactor to burst. By tracking the growth of the yeast or other cells and measuring the mechanical forces generated, scientists can simulate microbial growth in various places such as water pumps, sewage lines or catheters to learn how damage to these devices can be prevented. To learn more how researchers used small bioreactors to gauge the pressure generated by growing microbes, see this press release from UC Berkeley.

The human immunodeficiency virus (HIV), shown here as tiny purple spheres, causes the disease known as AIDS (for acquired immunodeficiency syndrome). HIV can infect multiple cells in your body, including brain cells, but its main target is a cell in the immune system called the CD4 lymphocyte (also called a T-cell or CD4 cell).

Real-time footage of Caenorhabditis elegans, a tiny roundworm, trapped by a carnivorous fungus, Arthrobotrys dactyloides. This fungus makes ring traps in response to the presence of C. elegans. When a worm enters a ring, the trap rapidly constricts so that the worm cannot move away, and the fungus then consumes the worm. The size of the imaged area is 0.7mm x 0.9mm.

This video was obtained with a polychromatic polarizing microscope (PPM) in white light that shows the polychromatic birefringent image with hue corresponding to the slow axis orientation. More information about PPM can be found in the Scientific Reports paper “Polychromatic Polarization Microscope: Bringing Colors to a Colorless World” by Shribak.

A scanning electron microscope picture of a nerve ending. It has been broken open to reveal vesicles (orange and blue) containing chemicals used to pass messages in the nervous system.

The Golgi complex, also called the Golgi apparatus or, simply, the Golgi. This organelle receives newly made proteins and lipids from the ER, puts the finishing touches on them, addresses them, and sends them to their final destinations.

Like a pulsing blue shower, E. coli cells flash in synchrony. Genes inserted into each cell turn a fluorescent protein on and off at regular intervals. When enough cells grow in the colony, a phenomenon called quorum sensing allows them to switch from blinking independently to blinking in unison. Researchers can watch waves of light propagate across the colony. Adjusting the temperature, chemical composition or other conditions can change the frequency and amplitude of the waves. Because the blinks react to subtle changes in the environment, synchronized oscillators like this one could one day allow biologists to build cellular sensors that detect pollutants or help deliver drugs.

Bacteria engineered to act as genetic clocks flash in synchrony. Here, a "supernova" burst in a colony of coupled genetic clocks just after reaching critical cell density. Superimposed: A diagram from the notebook of Christiaan Huygens, who first characterized synchronized oscillators in the 17th century.

The cerebellum is the brain's locomotion control center. Found at the base of your brain, the cerebellum is a single layer of tissue with deep folds like an accordion. People with damage to this region of the brain often have difficulty with balance, coordination and fine motor skills.

This image of a mouse cerebellum is part of a collection of such images in different colors and at different levels of magnification from the National Center for Microscopy and Imaging Research (NCMIR). Related to image 5795.

The cone cell of the eye allows you to see in color. Appears in the NIGMS booklet Inside the Cell.