Enhancement by GOSPEL protein of GAPDH aggregation induced by nitric oxide donor and its inhibition by NAD+

GONZALEZ, MARÍA C.; ROMERO, JORGE M.; INGARAMO, MARÍA C.; MUÑOZ SOSA, CHRISTIAN J.; CURTINO, JUAN A.; CARRIZO, MARÍA E.

FEBS LETTERS

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2016 vol. 590 p. 2210 - 2220

0014-5793

GOSPEL is the protein that competes with Siah1 for binding to GAPDH under NO-induced stress conditions preventing Siah1-bound GAPDH nuclear translocation and subsequent apoptosis. Under these conditions, GAPDH may also form amyloid-like aggregates proposed to be involved in cell death. Here we report the in vitro enhancement by GOSPEL of NO-induced GAPDH aggregation resulting in the formation GOSPEL-GAPDH co-aggregates with some amyloid-like properties. Our findings suggest a new function for GOSPEL, contrasting with its helpful role against the apoptotic nuclear translocation of GAPDH. NAD+ inhibited both GAPDH aggregation and co-aggregation with GOSPEL, a hitherto undescribed effect of the coenzyme against the consequences of oxidative stress.