Institute for Soft Matter Synthesis and Metrology

ISMSM Image(s) of the Month!

Nuclear Speckle Protein SRRM2 Dissolves During Anaphase in Ewing Sarcoma Cells

This study aims to investigate the role of the nuclear speckle protein SRRM2 (Serine/Arginine Repetitive Matrix 2) in Ewing Sarcoma (ES) by tagging the protein with moxGFP using CRISPR-Cas9 system delivered via transfection. ES cells (A4573) underwent puromycin selection and were then used for imaging experiments. Nuclear condensates formed by EWS::FLI1, the oncogene in ES, play a key role in oncogenesis by altering gene expression. The panels, from left to right, display: SRRM2 condensates dissolving in the dividing cell (both moxGFP-tagged and antibody-tagged, shown in orange), and the merged image including condensed chromatin stained with DAPI. Validating this fluorescent system was necessary in order to be able to study mRNA and SRRM2 in live cells. Studying nuclear bodies provides valuable insights into the mobility of soft matter and how their structural organization influences cellular function and the development of oncogenesis.

Credit: Dr. Jeff Toretsky, Olivia Oakley, David Allegakoen, and Emma McGuire

Read more: HERE

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Institute for Soft Matter News

Nuclear Speckle Protein SRRM2 Dissolves During Anaphase in Ewing Sarcoma Cells

April 3rd, 2025

A new study led by Dr. Jeffrey Toretsky and his team at Georgetown University investigates the role of the nuclear speckle protein SRRM2 in Ewing Sarcoma (ES), offering fresh insights into how oncogenic condensates influence gene regulation. The research, conducted in collaboration with Julie Forman-Kay’s lab at the Hospital for Sick Children in Toronto, uses advanced imaging techniques to track SRRM2 dynamics in live and fixed ES cells.…

This study focuses on the differential allosteric regulation by the ubiquitous signaling molecule, cAMP, in the cAMP receptor protein from Escherichia coli (CRPEcoli) and from Mycobacterium tuberculosis (CRPMTB). By introducing structurally homologous mutations from allosteric hotspots previously identified in CRPEcoli into CRPMTB and examining their effects on protein solution structure, stability, and function, we aimed to determine the factors contributing to their differential allosteric regulation. Results from this study indicate that the structural similarity between two allosteric proteins from distantly related bacteria does not reliably predict their allosteric behavior nor identify allosteric hotspots involved in the response to molecular signals.

Georgetown Researchers Uncover Key Differences in Bacterial Protein Regulation

February 11th, 2025

A new study led by Dr. Rodrigo Maillard at Georgetown University, “Identifying Allosteric Hotspots in Mycobacterium tuberculosis cAMP Receptor Protein through Structural Homology,” published in Biochemistry sheds light on how bacteria regulate their genes, challenging long-held assumptions about protein behavior. Published in Biochemistry, the research compares how two bacterial species—Escherichia coli and Mycobacterium tuberculosis—use a signaling molecule called cyclic AMP (cAMP) to control important cellular functions.…

Advancing Biomimetic Materials at Georgetown University

January 29th, 2025

Researchers within the Institute for Soft Matter Synthesis and Metrology (ISMSM) at Georgetown University, in collaboration with TU Eindhoven, have developed groundbreaking synthetic gel materials that mimic the dynamic properties of biological extracellular matrices. …

Unveiling the Sticky Secrets of Giardia: How a Parasitic Cell Masters Attachment

December 16th, 2024

Recent developments from Prof. Van Keuren and his students. An interdisciplinary team of researchers, led by Georgetown faculty members Biology Professor Heidi Elmendorf and Physics Professor Jeff Urbach used a combination of high-resolution imaging, computational modeling, theoretical analysis, innovative experimentation, to conclusively demonstrate that a version of the flow-based model accurately captures the biophysics of Giardia attachment.…

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