Team of Proteins Works Together to Turn on T Cells

The fates of various cells in our bodies—whether they become skin or another type of tissue—are controlled by genetic switches. In a new study, Caltech scientists investigate the switch for T cells, which are immune cells produced in the thymus that destroy virus-infected cells and cancers. The researchers wanted to know how cells make the choice to become T cells.

"We already know which genetic switch directs cells to commit to becoming T cells, but we wanted to figure out what enables that switch to be turned on," says Hao Yuan Kueh, a postdoctoral scholar at Caltech and lead author of a Nature Immunology report about the work, published on July 4.

The study found that a group of four proteins, specifically DNA-binding proteins known as transcription factors, work in a multi-tiered fashion to control the T-cell genetic switch in a series of steps. This was a surprise because transcription factors are widely assumed to work in a simultaneous, all-at-once fashion when collaborating to regulate genes.

The results may ultimately allow doctors to boost a person's T-cell population. This has potential applications in fighting various diseases, including AIDS, which infects mature T cells.

"In the past, combinatorial gene regulation was thought to involve all the transcription factors being required at the same time," says Kueh, who works in the lab of  Ellen Rothenberg, Caltech's Albert Billings Ruddock Professor of Biology. "This was particularly true in the case of the genetic switch for T-cell commitment, where it was thought that a quorum of the factors working simultaneously was needed to ensure that the gene would only be expressed in the right cell type."

The authors report that a key to their finding was the ability to image live cells in real-time. They genetically engineered mouse cells so that a gene called Bcl11b—the key switch for T cells—would express a fluorescent protein in addition to its own Bcl11b protein. This caused the mouse cells to glow when the Bcl11b gene was turn on. By monitoring how different transcription factors, or proteins, affected the activation of this genetic switch in individual cells, the researchers were able to isolate the distinct roles of the proteins.

The results showed that four proteins work together in three distinct steps to flip the switch for T cells. Kueh says to think of the process as a team of people working together to get a light turned on. He says first two proteins in the chain (TCF1 and GATA3) open a door where the main light switch is housed, while the next protein (Notch) essentially switches the light on. A fourth protein (Runx1) controls the amplitude of the signal, like sliding a light dimmer.

"We identify the contributions of four regulators of Bcl11b, which are all needed for its activation but carry out surprisingly different functions in enabling the gene to be turned on," says Rothenberg. "It's interesting—the gene still needs the full quorum of transcription factors, but we now find that it also needs them to work in the right order. This makes the gene respond not only to the cell's current state, but also to the cell's recent developmental history."

Team member Kenneth Ng, a visiting student from California Polytechnic State University, says he was surprised by how much detail they could learn about gene regulation using live imaging of cells.

"I had read about this process in textbooks, but here in this study we could pinpoint what the proteins are really doing," he says.

The next step in the research is to get a closer look at precisely how the T cell genetic switch itself works. Kueh says he wants to "unscrew the panels" of the switch and understand what is physically going on in the chromosomal material around the Bcl11b gene.

The Nature Immunology paper, titled, "Asynchronous combinatorial action of four regulatory factors activates Bcl11b for T cell commitment," includes seven additional Caltech coauthors: Mary Yui, Shirley Pease, Jingli Zhang, Sagar Damle, George Freedman, Sharmayne Siu, and Michael Elowitz; as well as a collaborator at the Fred Hutchinson Cancer Research Center, Irwin Bernstein. The work at Caltech was funded by a CRI/Irvington Postdoctoral Fellowship, the National Institutes of Health, the California Institute for Regenerative Medicine, the Al Sherman Foundation, and the Louis A. Garfinkle Memorial Laboratory Fund.

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Proteins Work Together to Turn on T Cells
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Scientists Transform Lower-Body Cells into Facial Cartilage

Caltech scientists have converted cells of the lower-body region into facial tissue that makes cartilage, in new experiments using bird embryos. The researchers discovered a "gene circuit," composed of just three genes, that can alter the fate of cells destined for the lower bodies of birds, turning them instead into cells that produce cartilage and bones in the head.

The results, published in the June 24 issue of the journal Science, could eventually lead to therapies for conditions where facial bone or cartilage is lost. For example, cartilage destroyed in the nose due to cancer is particularly hard to replace. Understanding the genetic pathways that lead to the development of facial cartilage may help in future stem-cell therapies, where a patient's own skin cells could be transformed and used to repair the nose.

"When facial cartilage and bone is lost, from cancer or an accident, it has been difficult to replace," says Marianne Bronner, the Albert Billings Ruddock Professor of Biology at Caltech, and senior author of the Science report. "Our long term hope is that uncovering this gene circuit may be useful in reprogramming a patient's own stem cells to make facial cartilage."

The bones below our necks, referred to by scientists as the "long" bones, originate from a different source of tissue than the bones in our head. As embryos, we are born with a type of early tissue called the neural crest that forms along the entire body, from the head to the end of the spinal cord. Those neural crest cells which originate in the head, called cranial neural crest, differentiate into the cartilage and bone of our faces, including the jaws and skull. In contrast, the so-called trunk neural crest cells, forming below the neck, do not make cartilage or bone but instead turn into nerve cells and pigment cells elsewhere in our bodies. Bronner and her colleagues want to understand what genes regulate the development of cranial neural crest cells and enable them to make cartilage and bones in the head.

To this end, they divided the trunk and cranial neural crest cells of bird embryos into separate groups, and looked for differences in gene activity. Fifteen genes were initially identified as being turned on in only the cranial cells. The researchers chose six of these genes for further study. All six code for transcription factors—molecules that bind to DNA to turn on and off the expression of other genes. After studying how these factors interact with each other, the scientists focused on three, called Sox8, Tfap2b and Ets, that are part of the cranial neural crest circuit.

These three genes were then inserted into the bodies of developing bird embryos, in particular the trunk neural crest, using a technique called electroporation. In this method, electric current is applied to cells to open up pores through which molecules such as DNA may pass. Next, the researchers transplanted the altered trunk cells to the cranial region of the embryos. Five days later, the trunk cells were doing something entirely new: producing cartilage.

"Normally, these trunk cells will not make cartilage," says Bronner. "Introducing just three genes into these cells reprogrammed them to acquire the ability to do so."

Bronner said that she hopes other researchers will use this information for experiments in cell culture. By adding the new-found gene circuit, perhaps with other known factors, to skin cells in a petri dish it may be possible to turn them into cartilage-producing cells—a key next step in creating future therapies for facial bone and cartilage loss.

The first author of the Science paper, titled, "Reprogramming of avian neural crest axial identity and cell fate," is Marcos Simoes-Costa of Caltech. The research is funded by the National Institutes of Health and the Pew Fellows Program in Biomedical Sciences.

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Creating Facial Cartilage in the Lab
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Wednesday, August 24, 2016
Center for Student Services 360 (Workshop Space) – Center for Student Services

CTLO's Summer Short Course for Faculty: (Re)Designing Your Class

Wednesday, September 21, 2016

SAVE THE DATE - 4th Annual Caltech Teaching Conference -- Details Coming Soon!

Wednesday, July 13, 2016
Noyes 147 (J. Holmes Sturdivant Lecture Hall) – Arthur Amos Noyes Laboratory of Chemical Physics

Teaching Statement Workshop

Dietary Fiber and Microbes Change the Gel That Lines Our Gut

In the ongoing hustle and bustle of our intestines, where bacteria and food regularly intermingle, there is another substance that, to the surprise of researchers, has been found to rapidly change: the gel that lines the gut. A new Caltech study is the first to show how the structure of this gut gel, or mucus, can change in the presence of certain substances, such as bacteria and polymers—a class of long-chained molecules that includes dietary fiber.

The work, to be published online the week of June 13 in the Proceedings of the National Academy of Sciences, could lead to the development of new drugs or diets for intestinal conditions such as irritable bowel disease.

Our intestinal tracts are lined with a mucus gel that acts as a protective barrier between the insides of our bodies and the outside world. The gel lets in nutrients and largely blocks out bacteria, preventing infections. It also regulates how some drugs are delivered elsewhere in our bodies.

Researchers had previously studied how the gel can be damaged, for instance when bacteria feed on the gut's lining. The Caltech study is the first to look at the structure of the gel and how it morphs in the presence of other substances naturally found in the gut.

Performing their experiments in mice, the team tested the effects of polymers, which include dietary fiber as well as therapeutics such as medicines for constipation. The researchers fed some mice a diet rich in polymers and others (the controls) a polymer-free diet. Using a technique called confocal reflectance microscopy they measured the thickness of the gut gel and the degree to which the gel was compressed as a result of the consumed polymers. Mice given a high-polymer diet, they found, had a more compressed gel layer.

"The gel is like a sponge with holes that let material through," says the paper's lead author, Sujit Datta, a postdoctoral scholar in the laboratory of Rustem Ismagilov, Ethel Wilson Bowles and Robert Bowles Professor of Chemistry and Chemical Engineering. "We are seeing that polymers, including dietary fiber, can compress the gel, potentially making the holes smaller, and we think that this might offer protective benefits," Datta adds.

In addition, the researchers applied different kinds of polymers—including dietary fibers like pectin, found in apples—directly to the gel lining to test its response. All of the polymers tested compressed the gel layer.

"It's too early to draw any conclusions, but it may be that eating an apple a day will affect the shape of the lining in your gut," says Asher Preska Steinberg, a Caltech graduate student and coauthor of the study.

The researchers also found that dietary fiber and gut bacteria—which are part of a community of microorganisms collectively known as gut microbiota—can work together to influence how the gut gel changes shape. They performed the same polymer/fiber experiments in germ-free mice, which are mice carefully raised to not have any bacteria in their gut. The results showed that the polymers compressed the gut gels of these germ-free mice to a greater degree. This implies that species of bacteria in our gut that are known to break down polymers can weaken the compressing effect.

"We previously thought of the gel as a static structure, so it was unexpected to find an interplay between diet and gut microbiota that rapidly and dynamically changes the biological structures that protect a host," says Ismagilov.

Both dietary fiber and certain gut microbes have been linked to good health. Fiber has been shown to lower cholesterol and regulate blood sugar levels—factors in heart disease and diabetes, respectively. Meanwhile, some bacteria, including the good "probiotics," can help treat digestive disorders and may even play a beneficial role in mental health. For instance, a separate Caltech-led study found that probiotics can alleviate autism-like behaviors in mice—a finding that could potentially lead to new therapies for the disorder in humans.

The entire collection of bacteria in our gut can include 1,000 different species or more and weigh a total of three pounds. Exactly how these microscopic organisms influence our health, for good and bad, is an area of active research with many unanswered questions. The White House recently announced the National Microbiome Initiative, with federal funding worth $121 million, to investigate the mysteries of microbes not only living in our bodies but all over the planet. In addition, more than 100 nonfederal agencies have pledged money and support toward researching microbial communities.

"Our study gives biologists and scientists studying diseases of the gut something else to think about," says Datta. "Now they can take the structure of the gut mucus, and how it responds to its environment, into account."

This research was funded by the Defense Advanced Research Projects Agency (DARPA) and National Science Foundation.

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Microbes & Dietary Fiber Change the Gut Lining
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The study is the first to look at the structure of the gut's mucus gel lining and how it morphs in the presence of other substances naturally found in the gut.

The Next Big Thing

To get a glimpse into the future, what better place is there to look than the minds of those about to become Caltech's newest alumni? After all, our 2016 graduates have been at the forefront of research in vastly different fields for the past few years. Their unique perspectives have informed their ideas of the future, and their work will reach far beyond the confines of a lab.

With that in mind, in the Summer 2016 issue of E&S magazine, we talked to a handful of undergraduate and graduate students prior to commencement to find out what they think will be the next big thing in science and engineering and how their plans after graduation reflect those ideas.

 

I believe that the future of science, technology, engineering, and mathematics (STEM) will place a greater emphasis on implementation and impact of research. While rapid economic growth and globalization have introduced numerous difficult challenges, society has acquired powerful new tools and technology to develop and implement solutions for these issues.

I will be working as a management consultant after graduating to expose myself to business and strategy. That way, I can perhaps one day help new discoveries and ideas produce a tangible impact on people's lives."

Aditya Bhagavathi
BS in Computer Science

 

I believe the future of planetary and space exploration will follow two paths—one, the search for life beyond Earth within the solar system, and two, the characterization of exoplanets.

For the solar system, the initial survey of its major worlds was just completed with the New Horizons flyby of Pluto, and therefore a new focus will likely emerge. That initial survey has revealed several worlds to be potentially habitable, including Mars, Europa, and Enceladus, with the former two already targets for future missions. These new missions will not only reveal more about these worlds but also force us to reevaluate what life is, how it arises, and how it endures.

For exoplanets, the diversity of worlds is immense. From giant planets that orbit their host stars in less than a day to habitable planets with permanent daysides and nightsides, exoplanets offer a tremendous opportunity to understand the planets in our own solar system. With the rapid development of technologies, instruments, and observing techniques, the flood of data regarding exoplanets will only continue. I plan to be among the scientists who will analyze this data and combine their results with theoretical models to investigate what these distant worlds are like. By doing this, we will be exploring our place in the universe and whether we are alone within it."

Peter Gao
PhD in Planetary Science

 

When asked what he would do with his degree in philosophy during a routine dentist appointment, David Silbersweig, MD at Brigham and Women's Hospital and Academic Dean at Harvard Medical School, responded with a single word that spoke volumes: 'Think.' Simply put, I too want to think.

I want to learn how to think at a complex level such that my ability to think and subsequently solve problems allows me to change lives. The history and philosophy of science degree at Caltech has given me exactly this. According to Silbersweig, 'If you can get through a one-sentence paragraph of Kant, holding all of its ideas and clauses in juxtaposition in your mind, you can think through most anything.' In my first History and Philosophy of Science class, I read Kant. I also find immense happiness in working with and helping other individuals, a sense of euphoria matched by little else in life. I learned this lesson through tutoring students and coaching younger athletes. And finally, as a collegiate athlete myself, I have undergone multiple orthopedic surgeries that ignited an interest in the musculoskeletal system and its ability to suffer injury yet recover remarkably. Together, these three aspects of life are central to my vision of the future. Becoming an orthopedic surgeon is the perfect combination—the career that will give me these components and a lot more.

One of the major developments in medicine will be 3-D printing, primarily in order to provide individuals with replacement bones and organs. Combining new progress in computer science will facilitate immense progress in 3-D printing, which also aligns well with the use of robotics in surgery. As an athlete who has torn my ACL and had bone spurs in the past year, I'm excited to be a part of this field in the future and hopefully help other athletes succeed in pursuing their passions."

Harinee Maiyuran
BS in History and Philosophy of Science

 

My personal hunch, and perhaps a somewhat common one, is that all disciplines—and not just STEM ones—are moving toward being increasingly data driven, a phenomenon rooted in freer dissemination and greater influx of research data. Correspondingly, computers and programming drive data processing in all disciplines; a common joke is that every scientist is automatically a software engineer. Statistical and machine learning techniques that are designed to tackle vast quantities of data are increasingly common in academic papers and will probably continue to climb in popularity.

I am planning to go into computational astrophysics research because I believe that the recent influx of data from new detectors will drive a huge surge of research questions to be investigated. And as a physics/computerscience double major, I'm uniquely equipped to analyze big data and extract scientific meaning from it."

Yubo Su
BS in Physics and Computer Science

 

Many aspects about future climate are unclear, such as how cloudiness, precipitation, and extreme events will change under global warming. But recent progress in observational and computational technology has provided great potential for clarifying these uncertainties. I plan to continue my research and utilize new data and models to develop theoretical understanding of these problems. I hope that such new insight will be helpful for assessing climate change impacts and designing effective adaptation and mitigation strategies."

Zhihong Tan
PhD in Environmental Science and Engineering

 

The future of science and engineering depends on closing the huge gap between the general public and scientists and engineers. I think this stems from a good deal of ignorance about what it is we do and hope to achieve, which leads to misconceptions about our work and community, and the separation between 'us' and 'them.' But if we're trying to understand and solve problems that affect everyone, shouldn't everyone be more involved?

When I graduate, I'm going to take a year off to try and bridge this gap in my own life. I don't know what I'll do yet, but it will be decidedly nonacademic. I want to travel, work odd jobs, and pursue hobbies I've set aside to finish my education. If I want to help people understand why I do what I do, I need to be certain that I understand first. After only four years surrounded almost exclusively by scientists and engineers, I want to get away a little. That way, when I inevitably return, I'll have a bit more perspective."

Valerie Pietrasz
BS in Mechanical Engineering and Planetary Science

 

Driven by the goal of reducing fossil fuel use and pollution, clean energy research plays and will play a pivotal role in America's energy future. Clean energy research spans disciplines such as biological and environmental sciences, advanced materials, nuclear sciences, and chemistry. Therefore, multidisciplinary efforts are not only necessary but also crucial to develop and deploy real-world solutions for energy security and protecting the environment.

As a graduate student, I have focused on understanding nanoscale energy transport in novel energy-efficient materials. In the future, I plan to further advance and apply my expertise to solve real-world problems in an integrated and multidisciplinary approach. I hope this effort will eventually lead to developing advanced clean energy technologies that could not only ease today's energy crisis but also improve our quality of life."

Chengyun Hua
PhD in Mechanical Engineering

 

I believe that in the next decade, the behavioral and computational subfields of neuroscience will work together seamlessly. I think this change will be primarily fueled by the development of new tools that allow us to measure the activity of large populations of neurons more precisely.

A prominent behavioral method of research, in mice at least, is to activate large structures in the brain and observe the aggregate behavioral effect. However, it is unlikely that all of these neurons are responsible for the same signal, so this approach may be too crude. I think new measurement techniques will enable behavioralists to collect large-scale population activity that computationalists can use in order to find subtle differences of function within these structures. Hopefully this collaboration will lead to generating and validating fundamental theories underlying how the brain works.

Currently, I am in the process of developing a method to measure the activity from over 10,000 neurons simultaneously. I hope to validate this technique before I graduate and then apply it to studying large-scale population activity during various behaviors. My future aim is to work closely with computationalists with the hope of discovering fundamental theories of brain function."

Gregory Stevens
BS in Biology

 

I think the future of planetary science is to discover and characterize more and more extra-solar planets, including their orbital configurations, atmospheres, and habitability. This is a challenging task because it requires a solid understanding of how chemistry and physics work on a planetary scale. Learning more about the planets closest to us paves a way toward the understanding of exoplanets that are far beyond our reach, since we can send missions to them. So after graduation, I will join the team for Juno—the spacecraft that will arrive at Jupiter in summer 2016—at JPL. New discoveries about Jupiter will also tell us more about what other planets beyond our solar system could look like."

Cheng Li
PhD in Planetary Science

 

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The Next Big Thing
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We hear from a handful of graduating students to learn what they think will be the next big thing in science and engineering and how their plans reflect those ideas.

Solving Molecular Structures

Determining the chemical formula of a protein is fairly straightforward, because all proteins are essentially long chains of molecules called amino acids. Each chain, however, folds into a unique three-dimensional shape that helps produce the characteristic properties and function of the protein. These shapes are more difficult to determine (or "solve"); scientists traditionally do so using a technique called X-ray crystallography, in which X-rays are shot through a crystallized sample and scatter off the atoms in a distinctive pattern.

This spring, Caltech students had the opportunity to use the technique to solve protein structures themselves in a new course taught by Professor of Chemistry André Hoelz.

Although the Institute has a long history in the fields of structural biology and X-ray crystallography, the chance to get hands-on experience with the technique is rare at most universities, Caltech included. Indeed, the method is more commonly performed at specialized facilities with high-energy X-ray beam lines, including the Stanford Synchrotron Radiation Laboratory (SSRL). However, in 2007, thanks to a gift from the Gordon and Betty Moore Foundation, Caltech opened the Molecular Observatory—a dedicated, completely automated radiation beam line at SSRL.

"The Molecular Observatory gives us lots of beam time," notes Hoelz. "Recently, I also received a grant from the Innovation in Education Fund from the Provost's Office that was matched by the Division of Chemistry and Chemical Engineering, and this allowed me the opportunity to develop this course and train students in a way not commonly found at universities."

In the new course, "Macromolecular Structure Determination with Modern X-ray Crystallography Methods" (BMB/Ch 230), Hoelz's students have been using the Molecular Observatory and other on-campus crystallization resources to solve the structures of various proteins, in particular, variants of green fluorescent proteins (GFPs)—proteins that exhibit bright green fluorescence under certain wavelengths of light. "These proteins are crucial tools in biology because they can be visualized by fluorescence techniques. It's important to know their physical structure, because it affects the intensity and wavelength at which the protein fluoresces," says Anders Knight, a first-year graduate student studying protein engineering with Frances Arnold, the Dick and Barbara Dickinson Professor of Chemical Engineering, Bioengineering and Biochemistry, and one of nine students—including two undergraduates—in the inaugural class.

During the first few weeks of the course, students determined the proper conditions—the pH levels and the mix of salts and buffer solutions—that are required to get a protein to crystallize. These conditions vary from protein to protein, making it tricky to "grow" perfect single crystals of the proteins. "Most of the ones we are working with have known 3-D structures, and they crystallize relatively easily, so they are a great place to start learning about the technique of X-ray crystallography," Knight says. "But some of us were also given protein variants that had never been crystallized before."

Once the students crystallized their proteins, single crystals were mounted in tiny nylon loops that are attached to small metal bases, frozen in liquid nitrogen, and loaded into pucks that were shipped to SSRL. There, the pucks were loaded into a robotic machine—remotely controllable from Caltech and operated by the students—that placed them, one by one, into a powerful X-ray beam. X-rays are scattered at characteristic angles by the electrons within the crystallized samples, generating a diffraction pattern that can be converted into a so-called electron-density map, which is then used to determine the 3-D location of all of the atoms.

"The electron density map doesn't exactly show you what the protein's structure is," Knight says. "You do have to correctly interpret the electron density map to determine where the protein's atoms will go. It's difficult, but this class is designed to give us practice doing that. Collecting data at SSRL was a great learning experience. It was interesting to be able to accurately mount and position the crystals—each smaller than a millimeter—on the beamline from hundreds of miles away. The data collection went fairly quickly, taking around eight minutes."

For their final assignment, students will write a mock journal paper about their methods and the final protein structure. Most of the structures had been determined previously, but one student did solve a previously unknown GFP structure, a bright red fluorescent protein called dTomato.

"dTomato is a product of directed evolution in protein engineering, created by subjecting its parent, DsRed, through several rounds of random genetic mutations," says Phong Nguyen, a graduate student in the lab of Doug Rees, Roscoe Gilkey Dickinson Professor of Chemistry and Howard Hughes Medical Institute Investigator, and the student who solved the structure of dTomato in Hoelz's class. "By solving its structure, we can see how directed evolution—a method developed by Frances Arnold to create new proteins using the principles of evolution—changed the protein from its parent. Specifically, we are able to explain how individual mutations contributed to the structural outcome of the protein and consequently to differing chemical and physical properties from the parent. We all are so excited to solve a new structure and contribute knowledge to the field of GFP protein engineering."

"Having the Molecular Observatory at Caltech allows us to train students with very sophisticated technology," says Hoelz, who is now envisioning a second, related course. "Students would learn recombinant protein expression and purification, directly prior to this course, so they can purify the proteins themselves with cutting-edge technology and then go on to determine their 3D structure by X-ray crystallography," he says.

"In my opinion, learning by doing is the best way to master how to determine crystal structures and this new course will solidify the strong roots Caltech has in X-ray crystallography," Hoelz adds. "Not only will this new course accelerate the otherwise slow learning process for this technique, but it will also allow non-structural biology laboratories on campus to determine crystal structures of their favorite proteins using Molecular Observatory, a unique and spectacular facility at Caltech."

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Solving Molecular Structures
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Solving Molecular Structures
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At Caltech, students have the opportunity to learn X‑ray crystallography, a technique that reveals the three-dimensional structure of molecules like proteins.

Gilmartin Named Dean of Undergraduate Students

On July 1, 2016, Kevin Gilmartin, professor of English, will begin serving as Caltech's dean of undergraduate students.

In announcing Gilmartin's appointment, Joseph E. Shepherd, vice president for student affairs and the C. L. Kelly Johnson Professor of Aeronautics and Mechanical Engineering, described him as "an accomplished scholar and author who brings to this position twenty-five years of experience in teaching and mentoring our students, and who has shown a keen interest in the welfare of our undergraduate students in and outside of the classroom."

In his new role as dean of undergraduate students, Gilmartin will work on fostering academic and personal growth through counseling and support for student activities as well as acting as a liaison between students and faculty, says Shepherd.

A recipient the Feynman Prize, Caltech's highest teaching award, Gilmartin says he was attracted to the job of dean because "I have always found our students to be so interesting, and engaging. They are extraordinarily optimistic. They seem to have a positive attitude toward the world—they're curious, and they're open to new things. What more could you ask for?"

He says he sees his role as helping undergraduates develop and thrive. "I'm excited to work with students to help foster their intellectual and academic growth and their development as individuals," he says. "Our students are remarkably diverse and they have diverse interests. The Caltech curriculum is demanding, and focused, no doubt. But within it, and through it, our students do find so many opportunities."

He adds, "The dean's office provides essential support. But we can also encourage our students to do more than they are inclined to do, to challenge themselves, to try new things."

Gilmartin received his undergraduate degree in English from Oberlin College in 1985. He received both his MS ('86) and PhD ('91) in English from the University of Chicago, joining the faculty of Caltech in 1991.

Barbara Green, who has served as the interim dean over the past year will return to her regular position as associate dean in July. In his announcement, Shepherd thanked Green "for her work with our students and service to the Institute [and for] being so willing and committed to the success of our undergraduate student body."

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On July 1, 2016, Kevin Gilmartin, professor of English, will begin serving as Caltech's dean of undergraduate students.

Ditch Day? It’s Today, Frosh!

Today we celebrate Ditch Day, one of Caltech's oldest traditions. During this annual spring rite—the timing of which is kept secret until the last minute—seniors ditch their classes and vanish from campus. Before they go, however, they leave behind complex, carefully planned out puzzles and challenges—known as "stacks"—designed to occupy the underclassmen and prevent them from wreaking havoc on the seniors' unoccupied rooms.

Follow the action on Caltech's Facebook, Twitter, and Instagram pages as the undergraduates tackle the puzzles left for them to solve around campus. Join the conversation by sharing your favorite Ditch Day memories and using #CaltechDitchDay in your tweets and postings.

          

 

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