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Computer Science, Biology & Chemistry have opened faculty searches

August 23, 2018 By

Brandeis has open searches for tenure-track faculty in three departments within the Division of Science for this fall.  We are looking forward to a busy season of intriguing seminars from candidates this winter.

  1. Assistant Professor of Computational Linguistics. Computer Science invites applications for a full-time, tenure-track assistant professor, beginning Fall 2019, in the area of Computational Linguistics including, but not limited to Statistical and Neural Machine Translation, Question Answering, Information Extraction, Text Summarization, Syntactic and Semantic Parsing, Dialogue Systems, etc.
  2. Assistant Professor(s) of Biology Biology invites applications for up to two full-time tenure-track positions at the level of Assistant Professor, beginning Fall 2019. Ideal candidates will be conducting innovative research in the broad area of cell biology using any organismal, cellular or in vitro system. Areas of emphasis include, but are not limited to, cell architecture, cell motility, cell division and morphogenesis, organelle function, intracellular trafficking, and compartmentalization.
  3. Assistant Professor of Chemistry. Chemistry is seeking a creative individual at the assistant professor level for a tenure-track faculty position in organic chemistry or chemical biology.  Exceptional senior candidates in all areas of chemistry will also be considered at the appropriate rank.

Brandeis University is an equal opportunity employer, committed to building a culturally diverse intellectual community, and strongly encourages applications from women and minorities.  Diversity in its student body, staff and faculty is important to Brandeis’ primary mission of providing a quality education.  The search committees are therefore particularly interested in candidates who, through their creative endeavors, teaching and/or service experiences, will increase Brandeis’ reputation for academic excellence and better prepare its students for a pluralistic society.

Filed Under: Biology, chemistry, Computer Science, labs Tagged With: , , , ,

Research Funding For Undergrads: MRSEC Summer Materials Undergraduate Research Fellowships

January 30, 2017 By

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: https://goo.gl/9LcSpG (Brandeis login required).


Eligibility
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: http://www.brandeis.edu/mrsec/people/index.html

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 brandeis.edu>.

Filed Under: awards, Biochemistry, Biology, chemistry, labs, Physics, Undergrads Tagged With: , , , , , , , , , , , , , , , , , , ,

Yoshinori Ohsumi to Receive Rosenstiel Award Wednesday, April 6

April 4, 2016 By

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.

Filed Under: awards, Biology Tagged With: , , , , , ,

Tissue-specific tagging of endogenous proteins in the fruit fly

February 28, 2016 By

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?

tstep

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.

Filed Under: Biology, Neuroscience Tagged With: , , , , , ,

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

February 14, 2016 By

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.

Filed Under: Biology, grad students, Physics Tagged With: , , , , , ,

Visualizing a protein decision complex in actin filament length control

November 17, 2015 By

Seen at the Gelles Lab Little Engine Shop blog this week, commentary on a new paper in Nature Communications, published 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.

Filed Under: Biochemistry, Biology, grad students, labs Tagged With: , , , , , , , ,

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