Walter Lab

  • Walter Lab
  • Research
    • The Unfolded Protein Response and IRE1 Signaling in Health and Disease
    • Organellar quality control, dynamics, and inheritance
    • RNA processing in the unfolded protein response
    • The integrated stress response and its role in cognition
    • ATF6-branch signaling through regulated proteolysis
  • Lab Members
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    • Alumni
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Aditya Anand

Graduate Student

Aditya@walterlab.ucsf.edu

Scientific Interest:

Proteins execute a vast array of cellular functions from cell signaling to ion transport to structural support.  To carry out these tasks, proteins adopt unique shapes in a process called protein folding. When proteins lose their shape, or “unfold”, they fail to function correctly and can further cause other proteins to unfold. A signaling network known as the integrated stress response (ISR) protects cells under these conditions by triggering a shut down of global protein synthesis. This pause in the production of proteins allows cells time and resources to mitigate protein unfolding-induced stress and prevent plaque-like aggregation. While great strides have been made in characterizing the ISR, there is more to be learned about stress responses and translational control. I am interested in furthering our mechanistic knowledge of the ISR and parallel pathways that regulate the synthesis of new proteins.

Current research interest:

Recently a small molecule modulator of the ISR called ISRIB (integrated stress response inhibitor) was discovered in our lab. My work is focused on determining a mechanism of action for this compound that can explain its blunting effects on the ISR.

Former Lab Affiliations

2010-2013 Dr. John Tainer , Lawrence Berkeley National Laboratory

Education

2007-2011 BA Molecular and Cell Biology, University of California, Berkeley
2011-Present PhD Biochemistry, University of California, San Francisco

Selected Publications

Tsai JC, Miller-Vedam LE, Anand AA, Jaishankar P, Nguyen HC, Renslo AR, Frost A, Walter P. Structure of the nucleotide exchange factor eIF2B reveals mechanism of memory-enhancing molecule. Science 359, eaaq0939, 2018
( PMID : not available ) (PDF)

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