SESN1,2,3 bind overoxidized PRDX1

Stable Identifier
Reaction [binding]
Homo sapiens
Sestrins bind overoxidized PRDX1
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Sestrins (SESN1, SESN2 and likely SESN3) bind overoxidized PRDX1, in which the catalytic cysteine C52 has been converted to cysteine-sulfinic acid. Among all peroxiredoxins, PRDX1 is the most abundant member of the PRDX family. The major function is to protect cells against reactive oxygen species (ROS), thus impacting on cell proliferation and survival (Gong et al. 2015). While several reports state that sestrins reduce overoxidized PRDX1 to the catalytically active homodimer (Budanov et al. 2004, Papadia et al. 2008, Essler et al. 2009), there are conflicting reports claiming that sestrins do not possess cysteine sulfinyl reductase activity (Woo et al. 2009).

Literature References
PubMed ID Title Journal Year
25579166 Peroxiredoxin 1 promotes tumorigenesis through regulating the activity of mTOR/p70S6K pathway in esophageal squamous cell carcinoma

Zhang, M, Gong, F, Liu, H, Hou, G

Med. Oncol. 2015
15105503 Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD

Feinstein, E, Budanov, AV, Chumakov, PM, Koonin, EV, Sablina, AA

Science 2004
19113821 Sestrin 2 is not a reductase for cysteine sulfinic acid of peroxiredoxins

Woo, HA, Bae, SH, Park, S, Rhee, SG

Antioxid. Redox Signal. 2009
18344994 Synaptic NMDA receptor activity boosts intrinsic antioxidant defenses

Corriveau, R, Stefovska, V, Hardingham, GE, Hansen, HH, Dakin, KA, McKenzie, G, Fowler, J, Martel, MA, Sifringer, M, Kaindl, A, Ikonomidou, C, Ghazal, P, Wyllie, DJ, Craigon, M, Léveillé, F, Yankner, BA, Horsburgh, K, Soriano, FX, Papadia, S

Nat. Neurosci. 2008
19822145 Role of sestrin2 in peroxide signaling in macrophages

Dehne, N, Brüne, B, Essler, S

FEBS Lett. 2009
Orthologous Events
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