A role for annexin A2 in scaffolding the peroxiredoxin 2-STAT3 redox relay complex.

ABSTRACT: Hydrogen peroxide (H₂O₂) is recognized to act as a signaling molecule. Peroxiredoxins (Prxs) have the ability to transfer H₂O₂-derived oxidizing equivalents to redox-regulated target proteins, thus facilitating the transmission of H₂O₂ signals. It has remained unclear how Prxs and their target proteins are brought together to allow for target-specific protein thiol oxidation. Addressing the specific case of Prx2-dependent STAT3 oxidation, we here show that the association of the two proteins occurs prior to Prx oxidation and depends on a scaffolding protein, the membrane chaperone annexin A2. Deletion or depletion of annexin A2 interrupts the transfer of oxidizing equivalents from Prx2 to STAT3, which is observed to take pla

SUBMITTER: Talwar D 

PROVIDER: S-EPMC7481202 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature