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Unexpected signaling role for foul-smelling hydrogen sulfide in cell response to protein misfolding
Date:12/13/2011

e called apoptosis.

The surprise in the research performed by Tonks' team which is published online today in Science Signaling is that H2S plays a critical role in the exquisitely tuned signaling pathway through which cells make this fateful determination.

Navasona Krishnan, a postdoctoral fellow, performed an experiment to determine whether H2S could covalently modify an enzyme called PTP1B. Discovered by Tonks in 1988, PTP1B is a protein tyrosine phosphatase, or PTP an enzyme that specifically removes phosphate groups from amino acid residues called tyrosines. This function is critical in regulating cellular signaling in normal and disease conditions.

H2S did indeed modify PTP1B, specifically on a cysteine amino acid residue in the enzyme's active site, which inactivated the enzyme. A number of subsequent experiments performed in collaboration with CSHL Professor Darryl Pappin, who directs the proteomics Shared Resource at the Laboratory, identified this modification and revealed that it occurred in vitro and in vivo.

Because PTP1B is itself a signaling pathway regulator, this inactivation was immediately understood to be important and potentially useful. Further experimentation revealed that the H2S-induced modification to PTP1B prevented this phosphatase from inactivating an enzyme called PERK, which is a sensor of the presence of unfolded proteins and a critical regulator of the cell's response to ER stress.

The completed puzzle is as follows: small amounts of hydrogen sulfide are produced when the cell senses ER stress; PTP1B undergoes a unique covalent modification at its active site in response to the H2S that is produced, which in turn prevents the phosphatase from dephosphorylating PERK thereby allowing the latter protein to play its specific regulatory role in response to the stress. Importantly, the process is fully reversible, such that this previously undiscovered pathway can act lik
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Contact: Peter Tarr
tarr@cshl.edu
516-367-8455
Cold Spring Harbor Laboratory
Source:Eurekalert

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