Exploring How a Cell Consumes Itself
The ability to capture and degrade specific cytoplasmic targets including protein aggregates, invading pathogens or even whole dysfunctional organelles forms the basis of the cell's response to disease ranging from neurodegeneration to cancer and heart disease. In each case, large cytoplasmic targets are identified and encapsulated in a newly-formed organelle, the autophagosome, which wraps portions of cytosol in a double-membraned compartment and eventually delivers it to the lysosome for degradation. How these targets are identified and how this organelle forms are the major foci of our laboratory.
Individual Recognitions
- Theodore Agbi and Yonas Takele were each awarded a STARS summer fellowship and will join the lab this summer. Welcome Theo and Yonas!
Recent Highlights
How autophagy proteins determine the unique structure of the autophagosome is just beginning to be understood. Our first efforts to study how the strident curvature present at the expanding rim of the growing phagophore might influence local biochemistry have just been published:
- Nath et al. 2014. Lipidation of the LC3/GABARAP family of autophagy proteins relies on a membrane curvature-sensing domain in Atg3. Nature Cell Biology , 16, 415-424.
- Dancourt and Melia, 2014. Lipidation of the autophagy proteins LC3 and GABARAP is a membrane-curvature dependent process. Autophagy, in press.
Principal Investigator
Thomas Melia, PhD
Professor of Cell Biology
Contact Information
- Office
- Fax
- Lab