"The topic was fresh and exciting, and I was able to work on a project that became a nexus for all of the lab's interests," she says. "I could contribute to projects ranging from structural biology to virology to mouse development."
The work cemented an interest in how protein phosphorylation regulates protein activity and also set off a graduate training career of which even the most demanding taskmaster would be proud. The various projects she collaborated on at McGill resulted in nearly 50 scientific publications, a number that continues to grow to this day.
The Highly Interactive STRIPAK Complex. Model of the numerous protein-protein interactions (including self-interactions) within the STRIPAK complex, as unraveled by Gingras and her colleagues. Green nodes represent the previously characterized association between PP2Ac, PP2A A, striatins, and Mob3; pink nodes indicate previously characterized interactions between CCM3 and the CGK-III subgroup. From Mol. Cell. Proteomics 8, 157-171.
Gingras is quick to point out she owes a good deal of that remarkable number to arriving at Sonenberg's lab at an extremely opportune time and that most of the work was collaborative.
In addition, she spent a little longer than average in her graduate lab as she waited for her partner, Brian Raught (now a researcher at the Ontario Cancer Institute), so they could move on together. "That worked out really well," she notes. "I had enough data to graduate, but I knew once I started my postdoc the pressure to get positive findings would start again. But in this intermediate period, I had this window where I could try these fun, fishing-type projects, and I took full advantage of that opportunity."
One of Gingras' favorite studies during her McGill time was a project that combined old-school gel electrophoresis with mass spectrometry to identify 4E-BP1 phosphorylation sites regulated by the mTOR signaling pathway, which then led to identifying the in vivo hierarchy of 4E-BP1 phosphorylation. That publication played a big part in stimulating a desire to do postdoctoral training in proteomics.
Fortuitously, one of the best proteome researchers, Ruedi Aebersold at the Institute for Systems Biology in Seattle, was a long-time collaborator of Sonenberg.
"Ruedi had just published his first ICAT paper, which documented the use of stable isotopes to quantify proteins," she says. "I had already collaborated extensively with Ruedi's group, particularly Steve Gygi, who is now at Harvard, to identify phosphorylation sites on various translation factors, and I thought that was the place to go to learn how to perform quantitative proteomics and phosphoproteomics."