We use the power of C. elegans genetics to understand cellular stress responses. Our specific interests lie in understanding the stress responses in the protein secretory pathway (endoplasmic reticulum (ER) and Golgi apparatus). Because cellular stress responses integrate with the innate immunity, aging, and cellular-death pathways, the ultimate goal of our laboratory is to understand how cellular stress responses affect the health and lifespan of an organism.

Our lab is also interested in understanding the mechanisms involved in controlling innate immune responses against microbial pathogens. Our previous studies demonstrated that C. elegans intestinal infection activates transcriptional programs to induce immune effectors and protective behavioral responses. Our current efforts involve understanding how intestinal infection brings about these changes.

Finally, to understand how organismal homeostasis is maintained, our lab is interested in studying the endocrinal (signaling between different tissues) and neuroendocrinal (endocrine signals from the nervous tissue to another tissue) regulation of cellular stress responses and innate immunity.

 

Please check out the Group website for more information.

1. Singh, J. (2020).Harnessing the power of genetics: fast forward genetics in Caenorhabditis elegans. Mol. Genet. Genomics, https://doi.org/10.1007/s00438-020-01721-6
2. Gokul, G., and Singh, J. (2020). Extracellular Proteostasis: Laying Siege to Pathogens. Curr. Biol. 30, R1085-R1087.
3. Singh, J., and Aballay, A. (2019). Intestinal infection regulates behavior and learning via neuroendocrine signaling. eLife 8, e50033.
4. Singh, J., and Aballay, A. (2019). Microbial Colonization Activates an Immune Fight-and-Flight Response via Neuroendocrine Signaling. Dev. Cell 49, 89-99.
5. Singh, J., and Aballay, A. (2017). Endoplasmic reticulum stress caused by lipoprotein accumulation suppresses immunity against bacterial pathogens and contributes to immunosenescence. mBio 8, e00778–17.
6. Singh, J., and Udgaonkar, J. B. (2015). Structural Effects of Multiple Pathogenic Mutations Suggest a Model for the Initiation of Misfolding of the Prion Protein. Angew. Chem., Int. Ed. 54, 7529−7533.
7. Singh, J., Kumar, H., Sabareesan, A. T., and Udgaonkar, J. B. (2014). Rational stabilization of helix 2 of the prion protein prevents its misfolding and oligomerization. J. Am. Chem. Soc. 136, 16704−16707.

Please check out the Group website for more information.