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The Burnham Buzz, February 2009
Date:2/3/2009

Ddk acts as a quality control protein and stops replication at the S-phase checkpoint of the cell cycle. Halting the cell cycle at the S-phase allows for DNA repair enzymes to repair the damaged DNA. Once the DNA damage has been repaired, Ddk re-initiates replication. Ddk has long been thought to be involved in DNA replication and the S-phase checkpoint. However, its exact role had not been elucidated until Jiang's study, which was published in the December 24, 2008 issue of Molecular Cell. The role of Ddk in controlling the DNA replication machinery for genome stability and fidelity may make it an excellent target for the development of new cancer treatments because these functions are often deregulated in cancerous cells.

Suicide Switch

Stefan Riedl, Ph.D., got the first look at the molecular structure of the protein complex that controls apoptosis (programmed cell death). Fas and Fas associated death domain protein (FADD) make up the death inducing signaling complex (DISC). The Fas-FADD DISC is a receptor platform, which once assembled, initiates the induction of programmed cell death. Dr. Riedl determined the X-ray crystal structure of the DISC to 2.7 Angstroms resolution and found that protein-protein interactions between Fas and FADD mechanistically control DISC formation. The structure showed that Fas undergoes a conformational change, creating an open structure that acts as a site for FADD binding, as well as bridging between the Fas molecules in the clustered complex. Dr. Riedl and colleagues propose that the bridging between Fas molecules in the complex acts as a control switch for DISC formation and initiation of apoptosis. Riedl's study was published December 31, 2008 in Nature.


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Contact: Josh Baxt
jbaxt@burnham.org
858-795-5236
Burnham Institute
Source:Eurekalert

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