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Unraveling the complex signaling that helps cells know when to grow, when to sit tight
Date:10/28/2011

DEPTOR to vanish was unknown. Wei, an expert in ubiquitination, decided to take on the problem.

To find out which protein(s) signals DEPTOR to degrade, the investigators employed a technology called ComPASS developed by Harper, the Bert and Natalie Vallee Professor of Molecular Pathology at HMS. Developed in 2009, ComPASS specifically identifies protein interactions and protein complexes.

In the case of DEPTOR, Wei and Harper found that the E3 ligase beta-TrCP marks DEPTOR for disposal by tagging it with ubiquitins. This tagging causes DEPTOR to be rapidly depleted, unleashing mTOR and, in turn, cell growth.

But beta-TrCP only tags DEPTOR if it has been phosphorylated, a process that marks a protein with phosphates to activate or deactivate it. So, asked Wei, how does DEPTOR get phosphorylated?

In a screening process to identify the proteins responsible for phosphorylatingand therefore depletingDEPTOR, he found two culprits: casein kinase 1 (CK1) and mTOR. "We were really surprised to find mTOR itself degrading DEPTOR," says Wei. "In a starvation state, DEPTOR levels are high and mTOR should not be able to do anything."

But when nutrients come in, something changes. With the deftness of Houdini, mTOR escapes from DEPTOR's binds and springs into action. The first thing mTOR does is join with CK1, a helper protein kinase that is always waiting around on standby. Together, mTOR and CK1 phosphorylate DEPTOR, triggering a rapid ubiquitination response from beta-TrCP and the immediate degradation of DEPTOR.

It is this mysterious feat that has now has Wei's attention. "How can mTOR be activated when it is fully suppressed by DEPTOR? We really want to know that," he says. The team is actively examining this question.

While this signaling pathway originally evolved as a nutrient sensor, in more complex organisms it acts as a fitness sensor. "All sorts of stimuli are integrated into one circuit," says Bing Su,
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Contact: Bonnie Prescott
bprescot@bidmc.harvard.edu
617-667-7306
Beth Israel Deaconess Medical Center
Source:Eurekalert

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