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New details on the molecular machinery of cancer
Date:2/11/2013

problems with the EGFR. However, despite its well-established links to cancer, EGFR activation has only been partially understood.

"As a member of the large class of cell surface receptors known as receptor tyrosine kinases, EGFR features a ligand-binding domain on its extracellular side and a kinase domain on its intracellular side," Groves says. "The text-book explanation for EGFR activation is that the binding of EGFR's ligand, EGF, to its extracellular side induces dimerization of the receptor, which in turn brings together the kinase domains on the intracellular sides of the dimer, allowing them to phosphorylate one another."

Groves says while the picture is accurate, it is an oversimplification of the mechanics behind the process because isolated intracellular kinase domains in solution can be active on their own at relatively low concentration without EGF ligand-induced dimerization. Dimerization is the combining of two identical molecules into a single compound molecule.

Measuring autophosphorylation as a function of EGFR surface density in cells, Groves, Kuriyan and their colleagues found that structural coupling between the EGFR transmembrane helix and extracellular juxtamembrane modules in addition to EGF ligand-engagement is required for EGFR activation. This structural coupling permits dimerization to take place in the presence of the EGF ligand.

"The un-ligated EGFR sits in a structural configuration that prevents the intracellular kinase domains from being able to reach each other," Groves says. "When the EGF ligand binds, this restraint is removed, dimerization occurs, and one kinase phosphorylates the other."

The inclusion by Groves and his colleagues of time-resolved fluorescence spectroscopy on living cells is another new advance in bringing a quantitative approach to the biological sciences. By combining picosecond light pulses from two different colors of lasers into a single beam, then genetically
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Contact: Lynn Yarris
lcyarris@lbl.gov
510-486-5375
DOE/Lawrence Berkeley National Laboratory
Source:Eurekalert  

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