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Encyclopedia > Protein phosphatase

Protein phosphatases are enzymes that remove phosphate groups that have been attached to amino acid residues of proteins by protein kinases. The phosphates are important in signal transduction by regulating the proteins they are attached to. To reverse the regulatory effect, the phosphate has to be removed. This occurs on its own by hydrolysis or is mediated by protein phosphatases.

Serine/threonine-specific protein phosphatases

Serine and threonine phosphates are stable under physiological conditions, so a phosphatase has to remove the phosphate to reverse the regulation. There are four known groups:

  1. PP1
  2. PP2A
  3. PP2B (AKA calcineurin)
  4. PP2C

The first three have sequence homology in the catalytic domain, but differ in substrate specifity.


Ser/Thr-specific protein phosphatases are regulated by their location within the cell and by specific inhibitor proteins.

Tyrosine-specific protein phosphatases


  Results from FactBites:
 
Protein Phosphatases (132 words)
Protein phosphatases are a group of enzymes, found ubiquitously, which are responsible for the dephosphorylation of various proteins and enzymes in a cell.
Protein phosphatases were first reported to be inhibited by microcystins by Mackintosh et.
It was found that extremely low concentrations of microcystin-LR could strongly inhibit protein phosphatases 1 and 2A from both plants and mammals, thereby causing hyperphosphorylation of the cell and a massive disruption of a number of important cellular mechanisms.
Ion channel regulation by phosphorylation (804 words)
In addition, it appears that a second protein phosphatase, the Ca2+/calmodulin dependent serine/threonine protein phosphatase (calcineurin/PP2B), may regulate the activity of the protein phosphatase that dephosphorylates the ion channel, although that has not been shown conclusively and may not be true for every system (Victor et al., 1997).
The characterization of ser/thr protein kinase interactions with ion channels has been facilitated by the fact that protein kinases appear to be much more specific in their recognition of targets when compared to protein phosphatases (for a recent review see Shenolikar, 1994).
The serine/threonine protein phosphatases have been grouped into two broad classes (type 1 and type 2) on the basis of whether they are inhibited by endogenous inhibitors known as Inhibitors 1 and 2 (for a review see Cohen and Cohen, 1989).
  More results at FactBites »


 

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