Jason Young, McGill University
Associate Professor
Biochemistry
Montreal, Quebec
jason.young2@mcgill.ca
Office:
(514) 398-5954
Expert In
Bio/Research
A fundamental biological process is the conversion of genetic information into functional proteins. Linear protein molecules must fold into sophisticated three-dimensional structures, and interact with the appropriate cellular targets. In cells, the folding and maturation of proteins depend on a ...
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Bio/Research
A fundamental biological process is the conversion of genetic information into functional proteins. Linear protein molecules must fold into sophisticated three-dimensional structures, and interact with the appropriate cellular targets. In cells, the folding and maturation of proteins depend on a specialized class of proteins termed 'molecular chaperones'. The chaperones are critical for the prevention of protein misfolding and aggregation, which are thought to underlie several neurodegenerative disorders such as Parkinson's disease.
Two of the most important chaperones in the eukaryotic cytosol are Hsp70 and Hsp90, the 70 kDa and 90 kDa heat shock proteins. The function of both chaperones involves interactions with a variety of regulatory co-chaperone proteins whose activities are still poorly understood.
My research investigates the biochemical mechanisms of chaperone and co-chaperone activity, and the consequences of this essential activity at a cellular level.
Interestingly, Hsp70 and Hsp90 work not only in the folding of soluble proteins, but also help in other cellular processes. These include the targeting of certain precursor proteins to the mitochondria for import into that organelle. Chaperones also work in the regulated assembly or disassembly of protein complexes on other intracellular membranes. It seems that specific co-chaperones are used for the different functions of Hsp70 and Hsp90.
Key questions are how the various co-chaperones direct the activities of the chaperones, for folding and for other purposes, and how chaperone function is integrated into the biogenesis of cellular structures. A combination of biochemistry, molecular and cell biology techniques are being applied to these exciting questions.
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Two of the most important chaperones in the eukaryotic cytosol are Hsp70 and Hsp90, the 70 kDa and 90 kDa heat shock proteins. The function of both chaperones involves interactions with a variety of regulatory co-chaperone proteins whose activities are still poorly understood.
My research investigates the biochemical mechanisms of chaperone and co-chaperone activity, and the consequences of this essential activity at a cellular level.
Interestingly, Hsp70 and Hsp90 work not only in the folding of soluble proteins, but also help in other cellular processes. These include the targeting of certain precursor proteins to the mitochondria for import into that organelle. Chaperones also work in the regulated assembly or disassembly of protein complexes on other intracellular membranes. It seems that specific co-chaperones are used for the different functions of Hsp70 and Hsp90.
Key questions are how the various co-chaperones direct the activities of the chaperones, for folding and for other purposes, and how chaperone function is integrated into the biogenesis of cellular structures. A combination of biochemistry, molecular and cell biology techniques are being applied to these exciting questions.
Click to Shrink <<