How key cancer-related enzyme functions
- Date:
- September 12, 2018
- Source:
- University of Copenhagen The Faculty of Health and Medical Sciences
- Summary:
- In a new study, researchers have discovered how an enzyme that plays a key role in cancer development functions. The researchers hope the new knowledge will lead to the design of more precise drugs.
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Researchers at the University of Copenhagen have come closer to understanding how an enzyme that appears to be important to cancer development behaves inside the cells.
The new study, published in the scientific journal Nature Communications, shows first of all that the enzyme METTL13 helps control the formation of new proteins in the cells.
"Mistakes in the production of proteins are undesirable, as we know from other studies that it can result in the development of cancer tumours and degenerative brain disorders like Alzheimer's and Parkinson's. Therefore, the new knowledge of how this enzyme functions is significant," says Professor Jesper Velgaard Olsen from the Novo Nordisk Foundation Center for Protein Research.
The enzyme helps control protein synthesis by placing so-called methyl marks on a particular protein called eEF1A.
"If methyl is not attached correctly to the protein it will not be able to do its job properly. And that again affects the formation of proteins in the cell, which will take place at a suboptimal pace, and even though that may not sound so bad, it appears to be connected with very serious disorders," says Postdoc Magnus Jakobsson from the Novo Nordisk Foundation Center for Protein Research.
The researchers have shown how the enzyme functions by studying isolated human cancer cells using advanced mass spectrometers which, in short, are able to identify and quantify proteins and their methyl-modifications in a cell.
Now the researchers hope the study will lead to the development of methods and drugs able to target and assure the enzyme to function as intended in our cells.
The study is funded by the Lundbeck Foundation and the Novo Nordisk Foundation, among others.
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Materials provided by University of Copenhagen The Faculty of Health and Medical Sciences. Note: Content may be edited for style and length.
Journal Reference:
- Magnus E. Jakobsson, Jędrzej M. Małecki, Levon Halabelian, Benedikt S. Nilges, Rita Pinto, Srikanth Kudithipudi, Stephanie Munk, Erna Davydova, Fawzi R. Zuhairi, Cheryl H. Arrowsmith, Albert Jeltsch, Sebastian A. Leidel, Jesper V. Olsen, Pål Ø. Falnes. The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates. Nature Communications, 2018; 9 (1) DOI: 10.1038/s41467-018-05646-y
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