Janet Iwasa

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Janet Iwasa is an American data visualization expert and assistant professor of biochemistry at the University of Utah. [1]

Contents

Early life and education

In 1978, Janet Iwasa was born to parents Mikeko and Kuni Iwasa in Bloomington, Indiana. She was the youngest of three children. [2] Following her father joining the National Institutes of Health, she moved, with her family, to Maryland. [3] [4] She later went on to participate in an internship at the Institute for Genomic Research. [3]

In 1999, she graduated with great honor from Williams College with bachelor's degrees in Biology and Asian Studies. [5] In her junior year at Williams, she worked alongside Professor Robert Savage, studying the formation of segmented patterns in leeches on a cellular level. [6] In 2006, Iwasa obtained a PhD in cell biology at the University of California in San Francisco. She wrote her doctoral thesis on the topic of actin networks. [7]

After watching a molecular animation by Graham Johnson, she began to pursue 3D animation. She began taking animation classes at San Francisco State University. [3] [8] After graduation, she studied animation at the Gnomon School of Visual Effects in Hollywood, California; she was the only woman in her class. She applied her skills in animation to biology, using 3D animation as a means to visualize cellular functions and interactions. [3]

Career and research

In 2006, Iwasa began working as a postdoctoral fellow under Jack Szostak with Harvard University and the Massachusetts General Hospital. [5] [9] In 2007, Iwasa worked as a teaching assistant at Harvard Medical School, in the "Visualizing Molecular Processes with Maya" course. [5] She also worked with MASSIVE, adapting the visual effects software to depict processes of nucleation elongation. [4]

In 2008, Iwasa created illustrations and animations for a multimedia exhibit for the Boston Museum of Science titled Exploring Life's Origins. [10]

In 2008, she became a lecturer in Molecular Visualization for the Department of Cell Biology at Harvard Medical School. [5] Her work with Joan Brugge and Michael Overholtzer furthered her understanding of a newly discovered cellular process called endosis. Iwasa worked alongside researchers at the university to investigate the process. [4]

While working with Tomas Kirchausen, she created an animation on clathrin-mediated endocytosis, researching how clathrin triskelions operated and assembled on the inner surface of the plasma membrane to invaginate an extracellular particle. [4] [8]

In 2010, Iwasa organized and taught a course on visualizing molecular and cellular processes with 3D animation in Porto, Portugal. [11] In 2013, she joined the University of Utah School of Medicine as a research assistant professor for the Department of Cell Biology. She returned to Portugal in 2014 to teach a 3D animation workshop for scientific animation. [5] In 2014, she also completed a project called Molecular Flipbook, [12] a free, open-source software program designed to animate molecules. In 2016, Iwasa released a life-cycle animation on HIV. Her project used animation to illustrate the molecular mechanisms the virus utilizes to enter into and exit target cells. [13] [8]

Iwasa is a TED senior fellow, and has spoken about animation in molecular biology at both TED and TEDx conferences. She has also contributed to TED-Ed. [14] [15]

Publications

Iwasa's work has been published in scientific journals including Nature , Science , and Cell , as well as the New York Times . [16] [17]

Iwasa's knowledge of cellular animation has also led her to publish several different works of scientific literature. Her work with Robert Savage's Lab led to her first publication in 1999 in Development Genes and Evolution, "The leech hunchback protein is expressed in the epithelium and CNS but not in the segmental precursor lineages", with co-authors Suver and Savage. [18] Iwasa's work with Savage focused on identifying regulatory genes engaged in the formation of segment patterns in annelids, investigating a gene in leeches called Leech Zinc Finger II (LZF2), considered to be an orthologue of the hunchback (hb) gene in Drosophila . Iwasa, Savage, and Suver concluded that LZF2 likely plays an important part in the morphological progressions of gastrulation and the specification of the central nervous system in leeches but does not contribute to the formation of anteroposterior patterns. [18]

In 2007, she published an article on her research at the University of California with Mullins, "Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly." [19] Her study with Mullins focused on the lamellipodial network. They concluded that the lamellipodial network incorporates the Arp 2/3 complex and capping proteins during initial assembly, but dismisses these complexes long before the lamellipodial network is actually disassembled. They also reported that the network does not use cofilin, twinfilin, and tropomyosin in assembly. Instead, these factors play a role in the network's size. [19]

In 2010, she published "Animating the model figure" in Trends in Cell Biology. [20] In this article, she points out the importance of animations in revealing and teaching scientific concepts, explaining that students are shown to retain more information and show more interest in the material when animations are incorporated into the curriculum. She also pushed the invention of animation software engineered exclusively for the scientific research community. [20]

In 2015, Iwasa and Wallace Marshal co-authored Karp's Cell and Molecular Biology: Concepts and Experiments by Gerald Karp. [21]

In 2016, Iwasa published "The Scientist as Illustrator" in Trends in Immunology, in which she describes the role of animation in science and discusses the importance of visualization. [22]

Recognition and honors

From 1999 to 2004, Iwasa was honoured as a member of the NSF Graduate Fellowship. From 2006 to 2008, she was a member of the NSF Discpery Corps Postgraduate Fellowship. [5] In 2008, she earned an honourable mention for her entry into the AAAS International Science & Engineering Visualization Challenge. In 2012, she was listed as one of Fast Company 's "100 Most Creative People." [5] [23] In 2014, she was recognized as a TED Fellow, a FASEB BioArt Winner, and one of Foreign Policy Magazine 's "100 Leading Global Thinkers." [5] [24] [25] In 2016, the University of Utah credited Iwasa as an Entrepreneurial Faculty Scholar. In 2017, she was honoured as a TED Senior Fellow. [5]

Related Research Articles

<span class="mw-page-title-main">Microtubule</span> Polymer of tubulin that forms part of the cytoskeleton

Microtubules are polymers of tubulin that form part of the cytoskeleton and provide structure and shape to eukaryotic cells. Microtubules can be as long as 50 micrometres, as wide as 23 to 27 nm and have an inner diameter between 11 and 15 nm. They are formed by the polymerization of a dimer of two globular proteins, alpha and beta tubulin into protofilaments that can then associate laterally to form a hollow tube, the microtubule. The most common form of a microtubule consists of 13 protofilaments in the tubular arrangement.

<span class="mw-page-title-main">Microfilament</span> Filament in the cytoplasm of eukaryotic cells

Microfilaments, also called actin filaments, are protein filaments in the cytoplasm of eukaryotic cells that form part of the cytoskeleton. They are primarily composed of polymers of actin, but are modified by and interact with numerous other proteins in the cell. Microfilaments are usually about 7 nm in diameter and made up of two strands of actin. Microfilament functions include cytokinesis, amoeboid movement, cell motility, changes in cell shape, endocytosis and exocytosis, cell contractility, and mechanical stability. Microfilaments are flexible and relatively strong, resisting buckling by multi-piconewton compressive forces and filament fracture by nanonewton tensile forces. In inducing cell motility, one end of the actin filament elongates while the other end contracts, presumably by myosin II molecular motors. Additionally, they function as part of actomyosin-driven contractile molecular motors, wherein the thin filaments serve as tensile platforms for myosin's ATP-dependent pulling action in muscle contraction and pseudopod advancement. Microfilaments have a tough, flexible framework which helps the cell in movement.

<span class="mw-page-title-main">Actin</span> Family of proteins

Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm.

<span class="mw-page-title-main">Myosin</span> Superfamily of motor proteins

Myosins are a superfamily of motor proteins best known for their roles in muscle contraction and in a wide range of other motility processes in eukaryotes. They are ATP-dependent and responsible for actin-based motility.

<span class="mw-page-title-main">Wiskott–Aldrich syndrome protein</span> Mammalian protein found in humans

The Wiskott–Aldrich syndrome protein (WASp) is a 502-amino acid protein expressed in cells of the hematopoietic system that in humans is encoded by the WAS gene. In the inactive state, WASp exists in an autoinhibited conformation with sequences near its C-terminus binding to a region near its N-terminus. Its activation is dependent upon CDC42 and PIP2 acting to disrupt this interaction, causing the WASp protein to 'open'. This exposes a domain near the WASp C-terminus that binds to and activates the Arp2/3 complex. Activated Arp2/3 nucleates new F-actin.

<span class="mw-page-title-main">ADF/Cofilin family</span> Family of actin-binding proteins

ADF/cofilin is a family of actin-binding proteins associated with the rapid depolymerization of actin microfilaments that give actin its characteristic dynamic instability. This dynamic instability is central to actin's role in muscle contraction, cell motility and transcription regulation.

Cytochalasins are fungal metabolites that have the ability to bind to actin filaments and block polymerization and the elongation of actin. As a result of the inhibition of actin polymerization, cytochalasins can change cellular morphology, inhibit cellular processes such as cell division, and even cause cells to undergo apoptosis. Cytochalasins have the ability to permeate cell membranes, prevent cellular translocation and cause cells to enucleate. Cytochalasins can also have an effect on other aspects of biological processes unrelated to actin polymerization. For example, cytochalasin A and cytochalasin B can also inhibit the transport of monosaccharides across the cell membrane, cytochalasin H has been found to regulate plant growth, cytochalasin D inhibits protein synthesis and cytochalasin E prevents angiogenesis.

<span class="mw-page-title-main">Gelsolin</span> Mammalian protein found in Homo sapiens

Gelsolin is an actin-binding protein that is a key regulator of actin filament assembly and disassembly. Gelsolin is one of the most potent members of the actin-severing gelsolin/villin superfamily, as it severs with nearly 100% efficiency.

<span class="mw-page-title-main">Treadmilling</span> Simultaneous growth and breakdown on opposite ends of a protein filament

In molecular biology, treadmilling is a phenomenon observed within protein filaments of the cytoskeletons of many cells, especially in actin filaments and microtubules. It occurs when one end of a filament grows in length while the other end shrinks, resulting in a section of filament seemingly "moving" across a stratum or the cytosol. This is due to the constant removal of the protein subunits from these filaments at one end of the filament, while protein subunits are constantly added at the other end. Treadmilling was discovered by Wegner, who defined the thermodynamic and kinetic constraints. Wegner recognized that: “The equilibrium constant (K) for association of a monomer with a polymer is the same at both ends, since the addition of a monomer to each end leads to the same polymer.”; a simple reversible polymer can’t treadmill; ATP hydrolysis is required. GTP is hydrolyzed for microtubule treadmilling.

<span class="mw-page-title-main">Protein filament</span> Long chain of protein monomers

In biology, a protein filament is a long chain of protein monomers, such as those found in hair, muscle, or in flagella. Protein filaments form together to make the cytoskeleton of the cell. They are often bundled together to provide support, strength, and rigidity to the cell. When the filaments are packed up together, they are able to form three different cellular parts. The three major classes of protein filaments that make up the cytoskeleton include: actin filaments, microtubules and intermediate filaments.

CapZ, also known as CAPZ, CAZ1 and CAPPA1, is a capping protein that caps the barbed end of actin filaments in muscle cells.

<span class="mw-page-title-main">Beta-actin</span> Protein-coding gene in the species Homo sapiens

Actin beta is one of six different actin isoforms which have been identified in humans. This is one of the two nonmuscle cytoskeletal actins. Actins are highly conserved proteins that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.

<span class="mw-page-title-main">Rnd3</span> Protein-coding gene in the species Homo sapiens

Rnd3 is a small signaling G protein, and is a member of the Rnd subgroup of the Rho family of GTPases. It is encoded by the gene RND3.

<span class="mw-page-title-main">Cordon-bleu protein</span> Protein found in humans

Protein cordon-bleu is a protein that in humans is encoded by the COBL gene.

Actin remodeling is the biochemical process that allows for the dynamic alterations of cellular organization. The remodeling of actin filaments occurs in a cyclic pattern on cell surfaces and exists as a fundamental aspect to cellular life. During the remodeling process, actin monomers polymerize in response to signaling cascades that stem from environmental cues. The cell's signaling pathways cause actin to affect intracellular organization of the cytoskeleton and often consequently, the cell membrane. Again triggered by environmental conditions, actin filaments break back down into monomers and the cycle is completed. Actin-binding proteins (ABPs) aid in the transformation of actin filaments throughout the actin remodeling process. These proteins account for the diverse structure and changes in shape of Eukaryotic cells. Despite its complexity, actin remodeling may result in complete cytoskeletal reorganization in under a minute.

<span class="mw-page-title-main">INF2</span> Protein-coding gene in the species Homo sapiens

Inverted formin-2 is a protein that in humans is encoded by the INF2 gene. It belongs to the protein family called the formins. It has two splice isoforms, CAAX which localizes to the endoplasmic reticulum and non-CAAX which localizes to focal adhesions and the cytoplasm with enrichment at the Golgi. INF2 plays a role in mitochondrial fission and dorsal stress fiber formation. INF2 accelerates actin nucleation and elongation by interacting with barbed ends of actin filaments, but also accelerates disassembly of actin through encircling and severing filaments.

<span class="mw-page-title-main">Arp2/3 complex</span> Macromolecular complex

Arp2/3 complex is a seven-subunit protein complex that plays a major role in the regulation of the actin cytoskeleton. It is a major component of the actin cytoskeleton and is found in most actin cytoskeleton-containing eukaryotic cells. Two of its subunits, the Actin-Related Proteins ARP2 and ARP3, closely resemble the structure of monomeric actin and serve as nucleation sites for new actin filaments. The complex binds to the sides of existing ("mother") filaments and initiates growth of a new ("daughter") filament at a distinctive 70 degree angle from the mother. Branched actin networks are created as a result of this nucleation of new filaments. The regulation of rearrangements of the actin cytoskeleton is important for processes like cell locomotion, phagocytosis, and intracellular motility of lipid vesicles.

<span class="mw-page-title-main">Klaus Weber</span> German scientist (1936–2016)

Klaus Weber was a German scientist who made many fundamentally important contributions to biochemistry, cell biology, and molecular biology, and was for many years the director of the Laboratory of Biochemistry and Cell Biology at the Max Planck Institute for Biophysical Chemistry in Göttingen, Germany. This institute has been renamed the Max Planck Institute for Multidisciplinary Sciences.

<span class="mw-page-title-main">Mary Beckerle</span>

Mary C. Beckerle is an American cell biologist who studies cancer at the Huntsman Cancer Institute at the University of Utah School of Medicine. At Huntsman Cancer Institute, she serves as the CEO and also as Associate Vice President for Cancer Affairs at the University of Utah. Beckerle's research helped to define a novel molecular pathway for cell motility, and more recently, she has begun research into Ewing’s sarcoma, a pediatric bone cancer. Beckerle's lab made a ground breaking discovery in regards to Ewing's Sarcoma in relation to the EWS/FLI protein. Her lab discovered EWS/FLI to disrupt the internal cellular skeleton, which decreases the ability of cells to adhere to their proper environment. This can help explain the metastasis of tumors in patients with Ewing's sarcoma.

<span class="mw-page-title-main">Rong Li</span> American cell biologist (born 1967)

Rong Li is the Director of Mechanobiology Institute, a Singapore Research Center of Excellence, at the National University of Singapore. She is a Distinguished Professor at the National University of Singapore's Department of Biological Sciences and Bloomberg Distinguished Professor of Cell Biology and Chemical & Biomolecular Engineering at the Johns Hopkins School of Medicine and Whiting School of Engineering. She previously served as Director of Center for Cell Dynamics in the Johns Hopkins School of Medicine’s Institute for Basic Biomedical Sciences. She is a leader in understanding cellular asymmetry, division and evolution, and specifically, in how eukaryotic cells establish their distinct morphology and organization in order to carry out their specialized functions.

References

  1. ↑ "Janet Iwasa | School of Medicine". medicine.utah.edu. 2023-01-15. Retrieved 2024-01-06.
  2. ↑ Iwasa, Janet (2020). Karp's Cell and Molecular Biology. John Wiley & Sons. p. 5. ISBN   978-1119598244.
  3. 1 2 3 4 Reynolds, Sharon. "Meeting Janet Iwasa" . Retrieved 2017-12-08.
  4. 1 2 3 4 Fleichman, John (February 2009). "ASCB Profile: Janet Iwasa" (PDF). ASCB Newsletter: 39–41. Retrieved 10 December 2017.
  5. 1 2 3 4 5 6 7 8 9 Janet Iwasa, Ph.D., University of Utah, Curriculum Vita
  6. ↑ rpsci98 - BIOLOGY DEPARTMENT, https://science.williams.edu/wp-content/blogs.dir/72/files/RS98html/RepSci98Web-BIOLOGY.html.
  7. ↑ Iwasa, Janet (June 21, 2006). "Spatial and Temporal Relationships between Actin-Filament Nucleation, Capping, and Disassembly" (PDF). Cell. Retrieved October 28, 2021.
  8. 1 2 3 Iwasa, Janet H. "Crafting a Career in Molecular Animation." Molecular Biology of the Cell, vol. 25, no. 19, 29 Oct. 2014, pp. 2891–2893. NCBI, doi : 10.1091/mbc.e14-01-0699.
  9. ↑ "Szostak Lab: Former Post-Doctoral Fellows". Molecular Biology. Harvard Medical School. Retrieved 10 December 2017.
  10. ↑ "About the Exploring Origins Project". Exploring Life's Origins.
  11. ↑ "News — The Animation Lab". The Animation Lab. Retrieved October 28, 2021.
  12. ↑ "Molecular Flipbook".
  13. ↑ Iwasa, Janet. "Visualizing HIV Entry and Egress."
  14. ↑ Iwasa, Janet. "Janet Iwasa | Speaker | TED". www.ted.com. Retrieved 2024-02-05.
  15. ↑ Iwasa, Janet (2017-09-07), Why it's so hard to cure HIV/AIDS , retrieved 2024-02-05
  16. ↑ Olsen, Erik (15 November 2010). "Molecular Animation: Where Cinema and Biology Meet". The New York Times. Retrieved 10 December 2017.
  17. ↑ "Janet Iwasa". Secret Life of Scientists and Engineers. PBS. Retrieved 10 December 2017.
  18. 1 2 Iwasa, J. H, et al. "The Leech Hunchback Protein Is Expressed in the Epithelium and CNS but Not in the Segmental Precursor Lineages." Development Genes and Evolution, vol. 210, no. 6, 19 May 2000, pp. 277–288. Springer Nature , doi : 10.1007/s004270050315.
  19. 1 2 Iwasa JH, Mullins RD. Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly. Curr Biol. 2007 Mar 6; 17(5):395-406
  20. 1 2 Iwasa JH (2010). Animating the model figure. Trends Cell Biol, 20(12), 699-704.
  21. ↑ Iwasa, JH and Marshall, W (December 2015). Karp's Cell Biology: Concepts and Experiments (8). Hoboken, NJ: John Wiley and Sons, Inc.
  22. ↑ Iwasa JH (2016). "The Scientist as Illustrator". Trends Immunol, 37(4), 247-50.
  23. ↑ Cain, Patrick (27 April 2012). "100 Most Creative People: 25. Janet Iwasa". Fast Company. Retrieved 11 December 2017.
  24. ↑ "Janet Iwasa". TED Speakers. TED.com. Retrieved 11 December 2017.
  25. ↑ "Foreign Policy Unveils Sixth Annual "100 Leading Global Thinkers" Issue". Foreign Policy Group. 17 November 2014. Retrieved 11 December 2017.
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