Research in the Gingras lab deciphers the intricacies of protein interactions
Dr. Anne-Claude Gingras is renowned for her studies of protein interactions that play a role in the development of cancer, drug resistance and immunity.
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Research in the lab of Dr. Anne-Claude Gingras
is focused on understanding how a specific class of enzymes called
phosphatases recognize their cellular targets. “Phosphatases control
key cellular processes, and their deregulation is associated with
diseases including cancer,” says Dr. Gingras. She explains that,
despite their importance to human health, phosphatases have been
relatively understudied. “Because proteins such as phosphatases rarely
work alone in the cell, but rather associate with other proteins to
exert their functions, identifying which proteins these molecules
associate with is key to understanding their biological
roles.”
For
example, Dr. Gingras and her colleagues have developed an innovative
computational approach—the first of its kind worldwide—designed to
analyze interaction proteomics data generated by mass spectrometry. The
software, called SAINT (Significance Analysis of INTeractome), will
allow researchers globally to quickly assess the reliability and
accuracy of protein binding data, helping to further their studies of
cancer and other illnesses. Dr. Gingras has encouraged many other
scientists to use SAINT, and the software is being implemented at a
number of research institutions.
Dr.
Gingras and other Lunenfeld researchers including Drs. Tony Pawson and
Mike Tyers have also created the first global ‘road map’ of important
protein interactions implicated in cell signaling—an achievement that
will help lead to better design of experiments that will accelerate
identification of new therapeutics approaches. The findings were
reported in the prestigious international journal Science.
By
using the Lunenfeld’s leading-edge mass spectrometry laboratory, the
researchers studied the interactions of two key classes of enzymes
known as protein kinases and phosphatases, referred to as the ‘kinome,’
in cells of the common baker’s yeast, Saccharomyces cerevisiae. Dr.
Gingras and her team analyzed the entire collection of kinases and
phosphatases in yeast, and uncovered a dense network of thousands of
protein interactions, including many previously uncharacterized
proteins.
“This was the first time that a kinome had been mapped to this extent,” says Dr. Gingras. “Our findings suggest that cells are able to integrate many different signals through the global network, and this has implications for how we might design drugs to control networks in health and disease.” Cells
coordinate many of their activities through the actions of protein
kinases and phosphatases. To date, only a fraction of these proteins in
the human genome has been explored by interaction proteomics. “When
these proteins malfunction, as occurs in genetic mutation or viral
infection, cellular function is disturbed,” says Dr. Gingras. Blocking
a protein kinase or phosphatase implicated in cancer, for example, is
the basis for some anti-cancer therapies: some of the newest and most
selective, or ‘intelligent,’ therapies are based on the specific
inhibition of kinases that are mutated in cancer. So Dr. Gingras’
research in this area is helping lead to new and better ways to treat
cancer and other illnesses.
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