Secret life of cells revealed with new technique
|Dr Yann Gambin (left) with Dr Nick Ariotti and Dr Kerrie-Ann McMahon, who also contributed to the research|
20 March 2014
A new technique that allows researchers to conduct experiments more rapidly and with increased resolution is already giving insights into the workings of proteins important in diseases of the heart and muscles.
The technique, developed by researchers at The University of Queensland’s Institute for Molecular Bioscience (IMB), enables researchers to examine individual proteins and directly observe the way they interact with other proteins in the cell.
Proteins are involved in most critical processes in the body and the ability to study their interactions is a cornerstone of health and medical research.
Dr Yann Gambin, who led the collaborative study between the laboratories of Professor Rob Parton, Professor Kirill Alexandrov and Dr Brett Collins, said the new method was a huge leap forward that would facilitate fundamental and translational research, speeding up the preparation of proteins for experiments to the point where scientists can process 100 proteins a day instead of a few per year.
“Replicating the behaviour of complex proteins in the human body using a different organism can be a very frustrating process,” Dr Gambin said.
“Now, we can analyse proteins directly in cell extracts, without any purification steps that may perturb biological processes. The new method allows us to dramatically accelerate the discovery process, which will translate into rapid advancement of our understanding of the inner workings of cells in health and disease.”
The researchers used the technique to examine cavins, proteins that sit in pockets on the cell surface, an area which has been studied in-depth by IMB’s Professor Rob Parton.
Faulty cavins have been associated with heart disease and muscular dystrophy but until now nothing was really known about how cavins interacted.
“By looking at cavins at single-molecule resolution, we have now discovered how cavins associate into large complexes, with unexpected selectivity as certain types of cavins will bind together, but others won’t,” Dr Gambin said.
“Given the role of these proteins in human diseases, an improved understanding of how the cavin complexes form and break down may assist in developing treatments for diseases caused by faulty cavins such as heart disease and muscular dystrophy.”
Dr Gambin said the technique was already being used in multiple research projects focusing on cancer, inflammation and infectious disease across IMB and would likely be adopted by researchers around the world after being published internationally in the new open-access scientific journal eLife.
eLife is a joint initiative of the Howard Hughes Medical Institute, the Max Planck Society, and the Wellcome Trust; its editor-in-chief is 2013 Nobel Prize winner Randy Schekman.
The publication has already been recommended by F1000Prime as a major advance in our understanding of caveolae biogenesis.
The research was funded by the Australian Research Council and the National Health and Medical Research Council.
A copy of the paper can be accessed at http://elife.elifesciences.org/content/3/e01434
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The Institute for Molecular Bioscience (IMB) is a research institute of The University of Queensland that aims to improve quality of life by advancing medical genomics, drug discovery and biotechnology.
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