Research Funding For Undergrads: MRSEC Summer Materials Undergraduate Research Fellowships

The Division of Science wishes to announce that, in 2017, we will offer seven MRSEC Summer  Materials Undergraduate Research Fellowships (SMURF) for Brandeis students doing undergraduate research, sponsored by the Brandeis Materials Research Science and Engineering Center.

The fellowship winners will receive $5,000 stipends (housing support is not included) to engage in an intensive and rewarding research and development program that consists of full-time research in a MRSEC lab, weekly activities (~1-2 hours/week) organized by the MRSEC Director of Education, and participation in SciFest VII on Aug 3, 2017.

The due date for applications is February 27, 2017, at 6:00 PM EST.

To apply, the application form is online and part of the Unified Application: (Brandeis login required).


Students are eligible if they will be rising Brandeis sophomores, juniors, or seniors in Summer 2017 (classes of ’18, ’19, and ’20). No prior lab experience is required. A commitment from a Brandeis MRSEC member to serve as your mentor in Summer 2017 is required though. The MRSEC faculty list is:

Conflicting Commitments
SMURF recipients are expected to be available to do full time laboratory research between May 30 – August 4, 2017. During that period, SMURF students are not allowed to take summer courses, work another job or participate in extensive volunteer/shadowing experiences in which they commit to being out of the lab for a significant amount of time during the summer. Additionally, students should not be paid for doing lab research during this period from other funding sources.

Application Resources
Interested students should apply online (Brandeis login required). Questions that are not answered in the online FAQ may be addressed to Steven Karel <divsci at>.

Yoshinori Ohsumi to Receive Rosenstiel Award Wednesday, April 6

ohsumi220Biologist Yoshinori Ohsumi will receive the 45th Rosenstiel Award for Distinguished Work in Biomedical Science this Wednesday, April 6th at 4:00 pm in Gerstenzang 123. At that time, he will present a lecture titled, “Lessons from yeast: Cellular recycling system, autophagy”.

Ohsumi is a cell biologist and professor at the Tokyo Institute of Technology’s Frontier Research Center in Japan. He is one of leading experts in the world on autophagy, a process that allows for the degradation and recycling of cellular components. The Rosenstiel Award is being given to Ohsumi in recognition of his pioneering discoveries in autophagy.

Learn more about Professor Ohsumi and his research at BrandeisNow.

Tissue-specific tagging of endogenous proteins in the fruit fly

Seeing is believing, and fluorescently tagged proteins have ushered in a major revolution in cell biology. Instead of observing the static components of dead cells fixed in plastic and reacted with dyes, tagged proteins fluorescing a variety of colors can be tracked in real time in live cells and organisms. We can peek at the previously only imaginable perpetual dynamism of life at the molecular level. In addition to turning us into spell-bound voyeurs, well-defined fluorescent tags also give us a hand-hold to isolate the binding partners of proteins of interest.

In a recent article by the Rodal lab reported in Biology Open, the authors report a new tagging methods designed to get rid of technological artifacts that can cause fluorescently tagged proteins to be expressed at the wrong time and place, and at the wrong levels. By using CRISPR mediated gene editing in fruit flies, they developed a novel approach to visualize any protein of choice in any tissue of choice at the level, localization and time that nature has intended. This method, dubbed T-STEP (for tissue-specific tagging of endogenous proteins), opens up novel experimental avenues to answer long-standing questions in several areas of neuroscience and cell biology, such as: how many different neurotransmitters are expressed in one neuronal circuit? Which tissue-type is a protein expressed in and when? What happens to a disease carrying mutant protein in a tissue of interest at endogenous levels?


As a proof of principle, two endosomal proteins, Vps35 (linked to Parkinson’s disease) and OCRL (linked to Lowe syndrome), which have never before been seen or localized in fruit flies, have now been visualized live at endogenous levels. Moreover, a Parkinson’s disease-specific mutation (D620N) in Vps35 has also been tagged with fluorescent proteins, opening up exciting new research avenues for interrogating binding partners and/or kinetics that may be altered during the diseased states.

In summary, T-STEP is an exciting novel tool that offers a simple and efficient method to tissue-specifically tag any protein at endogenous levels. Authors from the Rodal lab include Kate Koles (Research Scientist) and Anna Yeh ’16.

Lipids hit a “sweet spot” to direct cellular membrane remodeling.

Lipid membrane reshaping is critical to many common cellular processes, including cargo trafficking, cell motility, and organelle biogenesis. The Rodal lab studies how dynamic membrane remodeling is achieved by the active interplay between lipids and proteins. Recent results, published in Cell Reports, demonstrate that for the membrane remodeling protein Nervous Wreck (Nwk), intramolecular autoregulation and membrane charge work together in surprising ways to restrict remodeling to a limited range of lipid compositions.

F-BAR (Fes/Cip4 homology Bin/Amphiphysin/Rvs) domain family proteins are important mediators of membrane remodeling events. The F-BAR domain forms a crescent-shaped α-helical dimer that interacts with and deforms negatively charged membrane phospholipids by assembling into higher-order scaffolds. In this paper, Kelley et al. have shown that the neuronal F-BAR protein Nwk is autoregulated by its C-terminal SH3 domains, which interact directly with the F-BAR domain to inhibit membrane binding. Until now, the dogma in the field has been that increasing concentrations of negatively charged lipids would increase Nwk membrane binding, and thus would induce membrane deformation.

Surprisingly, Kelley et al. found that autoregulation does not mediate this kind of simple “on-off” switch for membrane remodeling. Instead, increasing the concentration of negatively charged lipids increases membrane binding, but inhibits F-BAR membrane deforming activities (see below). Using a combination of in vitro assays and single particle electron microscopy, they found that the Nwk F-BAR domain efficiently assembles into higher-order structures and deforms membranes only within “sweet spot” of negative membrane charge, and that autoregulation elevates this range. The implication of this work is that autoregulation could either reduce membrane binding or promote higher-order assembly, depending on local cellular membrane composition. This study suggests a significant role for the regulation of membrane composition in remodeling.

Brandeis authors on the study included Molecular and Cell Biology graduate students Charlotte Kelley and Shiyu Wang, staff member Tania Eskin, and undergraduate Emily Messelaar ’13 from the Rodal lab; postdoctoral fellow Kangkang Song, Associate Professor of Biology Daniela Nicastro (currently at UT Southwestern), and Associate Professor of Physics Michael Hagan.

Kelley CF, Messelaar EM, Eskin TL, Wang S, Song K, Vishnia K, Becalska AN, Shupliakov O, Hagan MF, Danino D, Sokolova OS, Nicastro D, Rodal AA. Membrane Charge Directs the Outcome of F-BAR Domain Lipid Binding and Autoregulation. Cell reports. 2015;13(11):2597-609.

Visualizing a protein decision complex in actin filament length control

Seen at the Gelles Lab Little Engine Shop blog this week, commentary on a new paper in Nature Communicationspublished in collaboration with the Goode Lab and researchers from New England Biolabs.

“Single-molecule visualization of a formin-capping protein ‘decision complex’ at the actin filament barbed end”

Regulation of actin filament length is a central process by which eukaryotic cells control the shape, architecture, and dynamics of their actin networks. This regulation plays a fundamental role in cell motility, morphogenesis, and a host of processes specific to particular cell types. This paper by recently graduated [Biophysics and Structural Biology] Ph.D. student Jeffrey Bombardier and collaborators resolves the long-standing mystery of how formins and capping protein work in concert and antagonistically to control actin filament length. Bombardier used the CoSMoS multi-wavelength single-molecule fluorescence microscopy technique to to discover and characterize a novel tripartite complex formed by a formin, capping protein, and the actin filament barbed end. Quantitative analysis of the kinetic mechanism showed that this complex is the essential intermediate and decision point in converting a growing formin-bound filament into a static capping protein-bound filament, and the reverse. Interestingly, the authors show that “mDia1 displaced from the barbed end by CP can randomly slide along the filament and later return to the barbed end to re-form the complex.” The results define the essential features of the molecular mechanism of filament length regulation by formin and capping protein; this mechanism predicts several new ways by which cells are likely to couple upstream regulatory inputs to filament length control.

Single-molecule visualization of a formin-capping protein ‘decision complex’ at the actin filament barbed end
Jeffrey P. Bombardier, Julian A. Eskin, Richa Jaiswal, Ivan R. Corrêa, Jr., Ming-Qun Xu, Bruce L. Goode, and Jeff Gelles
Nature Communications  6:8707 (2015)

The capping protein expression plasmid described in this article is available from Addgene.

Readers interested in this subject should also see a related article by Shekhar et al published simultaneously in the same journal.  We are grateful to the authors of that article for coordinating submission so that the two articles were published together.

Tenure-track positions in Biology (application deadline Oct 15)

The Biology Department at Brandeis University invites applications for up to two full-time, tenure-track appointments, beginning Fall 2016, from individuals who are conducting innovative research in the broad areas of molecular and cellular biology. Junior and more senior investigators will be considered, but preference will be given to hiring at the Assistant Professor level. Areas of interest range across molecular genetics, genomics and cell biology, including topics such as RNA biology, cytoskeleton, intracellular transport, development, signal transduction, transcriptional and post-transcriptional regulation, membrane biology, and epigenetics.

The research environment at Brandeis is highly collaborative, and we seek colleagues who will complement and extend existing strengths. Brandeis offers world-class research in the setting of a small liberal-arts university. Brandeis is located 7 miles from Boston, and is part of the vibrant research community of the greater Boston area.

Brandeis recognizes that diversity in its student body, staff and faculty is important to its primary mission of providing a quality education. The search committee is therefore particularly interested in candidates who, through their research, teaching and/or service experiences, will increase Brandeis’ reputation for academic excellence and better prepare its students for a pluralistic society.

To apply, please provide the following: a cover letter, a curriculum vitae, a summary of your research accomplishments to date, including a statement of your goals for future independent research (3-page limit), up to three publications, and at least three letters of reference. Applications will be accepted only through AcademicJobsOnline at

First consideration will be given to applications received by October 15, 2015. Following an initial evaluation by the search committee, finalists will be invited to visit the campus to discuss their research and to meet with faculty and students/postdocs. Additional inquiries may be directed to Leslie Griffith or to Paul Garrity.

Brandeis University is an equal opportunity employer, committed to supporting a culturally diverse intellectual community. Applications are particularly encouraged from applicants of groups underrepresented in the sciences.

Protected by Akismet
Blog with WordPress

Welcome Guest | Login (Brandeis Members Only)