Two University of Colorado at Boulder faculty members are among 33 researchers selected by the Howard Hughes Medical Institute of Chevy Chase, Md., to participate in a $40 million pilot program to pursue large, collaborative and potentially transformative biomedical research.
The Collaborative Innovation Awards to the eight teams of researchers represent a shift for the institute, the first time administrators there are providing direct funding for specific projects. The four-year pilot effort that includes researchers from 16 institutions in the United States and Chile is intended to encourage both HHMI investigators and outside scientists to undertake projects so new and large in scope that they require a team of collaborators with a range of expertise.
"We're excited about this program because of the quality of the projects, but also because it broadens the community of scientists supported by HHMI," said HHMI President and CU Distinguished Professor Tom Cech. "It incorporates people outside of the HHMI investigator program in solving important problems, and lets us do something really new."
A four-person research team led by HHMI Investigator Douglas Rees, which includes CU-Boulder faculty members Michael Stowell and Hang (Hubert) Yin and the California Institute of Technology's Rob Phillips, will be developing novel methods for analyzing the three-dimensional structures of membrane proteins. Located within the cell membranes, membrane proteins act as "gatekeepers" to control the two-way flow of nutrients, hormones and signaling molecules that regulate the permeability of the membranes and help cells stay healthy.
Rees and his team will build on earlier studies by Stowell of CU-Boulder's molecular, cellular and developmental biology department and his work on the structure of proteins found in neural synapses. Stowell has been targeting cell membrane lipids and their ability under some conditions to spontaneously assemble into "supramolecular" clusters in a laboratory dish.
Stowell has been able to take the lipid self-assembly a step further by adding membrane proteins to the lipids, coaxing them to form symmetrical, many-sided units called membrane protein polyhedra, or MPP. Team members hope the MPP research can help them to understand the structure of single proteins embedded in the MPP using x-ray crystallography.
Yin, of CU-Boulder's chemistry and biochemistry department, is a protein chemist who designs and studies peptides that interact with the membrane layers to pull them into a curved formation. Yin plans to use peptides to help the lipid system more easily form curved surfaces, creating a new method of studying membrane proteins packed inside MPPs.
Cech announced earlier this year that he will step down as HHMI president in spring 2009 and return to CU to resume his research and teaching. Cech has maintained his research lab at CU-Boulder during his tenure as HHMI president beginning in 2000 and has been returning to campus on a regular basis to collaborate with faculty, researchers and students studying the activity and regulation of telomerase, a key enzyme for replicating the ends of chromosomes.