Now an Australian Research Council laureate fellow and professor in structural biology at the University of Queensland’s Institute for Molecular Bioscience, where she has been since 1993 (previous stops included an appointment at Australia’s Bond University and a postdoc with John Kuriyan at Rockefeller University), Martin continues to focus on the relationship between protein structure and drug action. As someone who always has been interested in puzzles and how things piece together, teasing out this structure-function relationship is a perfect fit.
|The Queensland Bioscience Precinct— the building that houses UQ’s Institute for Molecular Bioscience.
Much of Martin’s work centers on proteins involved in insulin signaling and diabetes, and her recent efforts have focused on understanding the regulation of SNARE proteins, which are involved in the insulin-stimulated trafficking of the GLUT4 glucose transporter. For instance, she discovered that the regulatory protein Munc18c can accelerate SNARE complex formation and vesicle fusion by binding to a short N-terminal peptide on the SNARE protein syntaxin4 and that this interaction is conserved in almost all SNARE systems.
Martin also recently was awarded a program grant from Australia’s National Health and Medical Research Council to work alongside cell biologists, metabolic scientists and clinicians to identify novel proteins associated with diabetes and to characterize these proteins at a structural and functional level.
In addition to her own group’s work, Martin has been instrumental in nurturing Australia’s structural biology presence through work on various scientific committees.
“Protein crystallography has grown tremendously in Australia since I first started my lab in 1993,” she says. “There were maybe six or seven groups back then, but today, that number has grown to over 40.”
The growth in protein crystallography is a welcome trend, especially considering Australia’s history in this field, adds Martin, who is a bit of a history buff. Australia’s first ever Nobel laureate was Lawrence Bragg in 1915. He won the award at age 25 alongside his father, William Bragg, for solving the first ever x-ray crystal structure (of sodium chloride).
And, because of the efforts of Martin and her colleagues, today’s Australian and New Zealander crystallographers can achieve their own breakthroughs much more easily, thanks to the 2007 opening of the Australian Synchrotron in Victoria. Previously, synchrotron data measurement required time-consuming and expensive trips to the U.S., Japan or Europe, but now, researchers have a much more convenient destination, as well as a centralized area where the burgeoning crystallography community can converge.
Of course, some part of Martin may miss the frequent airline travel; after all, you never know what kind of life-changing experience you might have while waiting to board a plane.