SESSION 1B: Inaugural Lectures by Fellows/Associates

E D Jemmis

Molecular chaperones as gateways to mitochondrial health

Mitochondrial dysfunction has lately been appreciated as a major causal factor in a myriad of diseases. For its function, a typical mitochondrion requires around 1500–2000 proteins. However, the mitochondrial genome is highly gene-deficient and most of the mitochondrial proteome is nuclear encoded. Therefore, the system has developed a robust transport mechanism, which involves coordinated recycling of Hsp70 (heat shock protein 70) machinery at the transport channel. In lower organisms, these transporters are limited to their primary import role. But in higher organisms, the speaker found that the transport machinery is highly specialized with dedicated machines present for constitutive and regulated functions. Particularly the J-proteins, which are major drivers of Hsp70 functions have evolved multifunctionality and influence, other than protein transport, other cellular processes such as cell proliferation, redox maintenance, responses to xenobiotic drugs etc. Indeed, these J-proteins have been found to be overexpressed or mutated in different pathophysiological conditions such as cancer and cardiomyopathies. Their initial findings provide some hints on how these J-proteins might be hard-wired into the cellular systems, thereby furthering our understanding of these multifunctional entities.