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Key enzyme discovered to be master regulator in protein-protein reactions
Date:3/24/2010

f (peer-reviewed) papers out there, but nobody understood how PP1 is regulated," said Peti. "It is in fact a master regulator. We have identified now how it works."

To obtain their results, the team showed for the first time how PP1 is bound to a regulator protein, spinophilin. Using nuclear magnetic resonance spectroscopy and X-ray crystallography, the researchers examined the spinophilin-PP1 complex's structure. The scientists saw that spinophilin had attached itself to one of three substrate binding sites on PP1, called the C-terminal substrate binding groove. Examined at the atomic scale, it appears as if spinophilin is a many-tentacled beast that has woven itself into the C-terminal substrate binding groove, effectively blocking any substrate requiring this groove from interacting with PP1.

That leaves only two other binding sites, the acidic and hydrophobic substrate binding grooves. "Any substrate that needs the C-terminal is out of the game," Peti said.

By narrowing the binding sites from three to two, PP1 is in effect becoming more selective, Peti noted. "What that means is PP1 is equally tightly controlled as kinases are," he said.

"Now we know how PP1 is regulated," Peti added. "What simply happens is we don't create more enzymes. We create more protein complexes (holoenzymes) that increase the specificity of PP1."


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Contact: Richard Lewis
Richard_Lewis@brown.edu
401-863-3766
Brown University
Source:Eurekalert  

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