Ramanujan Hegde elected Fellow of the Royal Society

Manu HegdeManu Hegde, group leader in the LMB’s Cell Biology Division, has been elected as a Fellow of the Royal Society, in recognition of his “seminal contributions to understanding how nascent secretory and membrane proteins mature to their functional state, and how quality control pathways detect and resolve mistakes during maturation.” The Royal Society is a Fellowship of the world’s most eminent scientists and is the oldest scientific academy in continuous existence.

Manu joined the LMB as a group leader in 2011 following a successful career at the National Institutes of Health in the USA. He and his group are researching membrane protein biosynthesis and quality control. Membrane proteins need to be carefully guided through biogenesis as their hydrophobic transmembrane domains are not water-soluble and are thus prone to aggregation during synthesis, insertion and folding. To further ensure fidelity, quality control systems degrade defective proteins if biogenesis fails. Manu’s lab dissects the mechanisms underlying these biosynthetic and quality control processes by using a combination of in vitro reconstitution and structure determination of key complexes. This research seeks to understand how secreted and membrane proteins are assembled, how cells handle mistakes in these pathways, and the diseases that arise from their failure. The failure of protein maturation and quality control underlies a wide range of human diseases ranging from neurodegeneration to cystic fibrosis, so a molecular understanding of these processes may help to identify points of therapeutic intervention in the future.

The Royal Society seeks to promote excellence in science through its Fellowship and Foreign membership. Each year, the Royal Society elects up to 52 new Fellows and up to ten new Foreign Members, recognising those scientists who have made substantial contributions to the improvement of knowledge in the sciences.

Further references:

Manu’s group page
The Royal Society

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Unfinished proteins: how to find a needle in the haystack
Stop codons: a decoding puzzle decoded
An open translocation channel revealed
Cryo-EM reveals protein export machinery