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New technique reveals cross-talk between 2 essential cellular processes
Date:7/19/2012

LA JOLLA, CA Scientists at The Scripps Research Institute have simultaneously mapped two of the most important types of protein-modification in cells, revealing their extensive cooperation during an essential cellular process.

Phosphorylation, the attachment of a phosphate group to a protein, and proteolysis, the cleavage of a protein, had almost always been studied independently. The new research combines techniques for mapping these events across all proteins in a cell population to show how they work together to execute the cellular "auto-destruct program" known as apoptosis.

The specific findings on apoptosis may lead to the development of new cancer diagnostics and drugs, since cancer treatments often aim to induce apoptosis in malignant cells. Even more importantly, the study marks the development of a basic new tool of "proteomics"the large-scale study of proteinsthat should provide useful insights into many cellular processes.

"Detecting the cross-talk between protein regulation pathways has long been a challenge, and so with this new technique we can start to do analyses that were difficult or impossible before," said Benjamin F. Cravatt, professor and chair of the Department of Chemical Physiology at Scripps Research, and member of Scripps Research's Skaggs Institute for Chemical Biology. Cravatt was the senior investigator for the study, published in the July 20, 2012 edition of the journal Cell.

Need for a Global Approach

Phosphorylation and proteolysis are among the most important mechanisms of protein modification in cells. They are mediated by enzymes, and occur after a protein has been translated from genetic material and folded. Some proteolysis and phosphorylation events serve to activate a protein so that it can take part in a purposeful cellular process; others have the effect of deactivating a protein.

Previous studies of phosphorylation and proteolysis had suggested
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Contact: Mika Ono
mikaono@scripps.edu
Scripps Research Institute
Source:Eurekalert  

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