Judges’ Queries and Presenter’s Replies

  • Members may log in to read judges’ queries and presenters’ replies.

Presentation Discussion

  • Icon for: Lee McDavid

    Lee McDavid

    May 23, 2012 | 05:06 p.m.

    What are the implications of understanding apoptosis better for disease treatment?

  • Icon for: Scott Eron

    Scott Eron

    May 23, 2012 | 10:05 p.m.

    Great question! By understanding the regulation of caspases and how they control apoptosis we can better recognize the diseased state and ways to enhance treatment. To elaborate, I can think of two types of examples: (1) Imagine small molecules being able to control whether a cell lives or dies. In neurodegenerative diseases such as Alzheimer’s or Huntington’s disease, control of caspase activity could prevent the excess apoptosis that occurs as a result of these diseases. Conversely, many cancer cells overexpress certain kinases that phosphorylate caspases and make the cell immune to cell death. For example, PAK2 is overexpressed in a variety of cancer cell lines and inactivates caspase-7 via phosphorylation. This immunity to apoptosis poses a serious threat to cancer therapies that rely on cell death. However, if you administered a small molecule drug that activated caspase-7 it could enhance other therapeutic treatments. (2) Recently there have been a plethora of novel strategies to deliver proteins. Delivery of an executioner caspase, specifically to tumors, would result in apoptosis events in cancerous cells.

  • Further posting is closed as the competition has ended.

Icon for: Scott Eron


University of Massachusetts at Amherst
Years in Grad School: 2

Structural Insights into Programmed Cell Death

Caspases are the protein hitmen of the cell, cutting key protein substrates and causing a controlled and coordinated cell death. Their regulation is critical for proper development, inflammation responses, and differentiation. Malfunctions in caspase activity and the apoptotic pathway play a role in cancer and neurodegenerative diseases. This study dives into the regulation of a particular executioner caspase, caspase-7, and how phosphorylation of this protein regulates its function. By taking an interdisciplinary approach utilizing molecular biology, protein biochemistry, enzymology, and crystallography we have shown that an engineered caspase-7 phosphorylation mimic inactivates the protein by sterically preventing substrate binding.