The Bard Lab studies the cellular response to stress, with a particular focus on stress-induced translational reprogramming and stress-induced biomolecular condensation. We are interested in a wide range of fundamental questions about molecular specificity and cellular organization:

How do cells read out the molecular grammar of mRNA and turn that information into specific, reliable and regulatable protein production?

How do cells reorganize their cytoplasm during stress to form biomolecular condensates including stress granules?

What is the function of these transiently formed condensates and how are they regulated?

We use infection by human pathogenic viruses, such as Chikungunya virus, and stress-resistance in cancer cells as model systems to explore these topics. We hope to both identify potential therapeutic targets and take advantage of the unique characteristics of these diseases to better understand human biology. For instance, viruses, in addition to being public health menaces, are nature’s best cell biologists. When Chikungunya virus infects a cell, it first disperses host-induced stress granules, then co-opts the stress granule machinery to aid in its own replication. We will study the molecular mechanisms by which the virus accomplishes this, and how this reorganization affects host and viral translation. Similarly, some cancer cells are able to overcome chemotherapeutic treatment by upregulating the stress response and stress granules. We hope to understand how stress granules aid in resistance to treatment and how this resistance might be negated.

To address these questions, we take an integrative approach, combining biophysical, biochemical, and high-throughput tools to gain a deep understanding of molecular mechanisms and functions.

Kik SK, Christopher D, Glauninger H, Hickernell CW, Bard JAM, Ford M, Sosnick TR, and Drummond, DA (2023). An adaptive biomolecular condensation response is conserved across environmentally divergent species. bioRxiv, 2023.07.28.551061.

Ali A, Garde R, Schaffer OC, Bard JAM, Husain K, Kik SK, Davis KA, Luengo-Woods S, Igarashi MG, Drummond DA, Squires AH, Pincus D. Adaptive preservation of orphan ribosomal proteins in chaperone-dispersed condensates. Nat Cell Biol. 2023 Nov;25(11):1691–703. DOI: 10.1038/s41556-023-01253-2.

Jonsson E*, Htet ZM*, Bard JAM, Dong KC, Martin A. (2022). Ubiquitin modulates 26S proteasome conformational dynamics and promotes degradation. Science Advances. 8, eadd9520.

Glauninger H, Hickernell CJW, Bard JAM, Drummond, DA. (2022). Stressful steps: progress and challenges in understanding stress-induced mRNA condensation and stress granule coalescence. Molecular Cell. 82, 2544–2556.

Yoo H, Bard JAM, Pilipenko E, Drummond DA. (2022). Chaperones directly and efficiently disperse stress-triggered biomolecular condensates. Molecular Cell. 82, 741–755.e11.

Bard, JAM, Bashore C, Dong KC, Martin A. (2019). The 26S Proteasome Utilizes a Kinetic Gateway to Prioritize Substrate Degradation. Cell. 177, 286-298.e15.

Bard JAM*, Goodall EA*, Greene ER, Jonsson E, Dong KC, Martin A. (2018) Structure and Function of the 26S Proteasome. Annual Review of Biochemistry. 87: 697-724. *Authors contributed equally

Bard JAM, Martin A. (2018) Recombinant expression, unnatural amino-acid incorporation, and site-specific labeling of 26S proteasomal subcomplexes. Methods in Molecular Biology. vol 1844.