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Sci. Signal., 13 December 2011
Vol. 4, Issue 203, p. ra86
Inactivating a Phosphatase with H2S
Protein tyrosine phosphatases (PTPs) have a cysteine in their active sites that is susceptible to oxidation. Krishnan et al. show that the reactive gas hydrogen sulfide (H2S) is produced by cystathionine -lyase during the unfolded protein response (UPR) that occurs when cells experience endoplasmic reticulum (ER) stress. In vitro experiments and experiments with cultured cells showed that H2S reacted with the active-site cysteine of PTP1B and inhibited the activity of this ER-associated enzyme. Inhibition of PTP1B by H2S during the ER stress response promoted the activity of the kinase PERK, a mediator of the UPR that inhibits protein translation. Thus, reversible posttranslational sulfhydration of PTP1B contributes to the ER stress response to promote a return to cellular homeostasis.
Citation: N. Krishnan, C. Fu, D. J. Pappin, N. K. Tonks, H2S-Induced Sulfhydration of the Phosphatase PTP1B and Its Role in the Endoplasmic Reticulum Stress Response. Sci. Signal.4, ra86 (2011).