Table 2 Established mechanisms and tested drugs for stimulating SERCA via post-translational modifications or protein to protein interactions. The table lists the proved typical SERCA stimulating interactions, including glutathionylation, SUMOylation, acetylation and the activator through allosteric effect, and their corresponding regulating sites and effective drugs

Glutathionylation

Disulfide bond formed at cysteine residue of SERCA

Nitroxyl (HNO)

Nitric oxide (ONOO)

Adachi et al. [1], Lancel et al. [34]

SUMOylation

SUMO binds to lysine residue of SERCA

Luteolin

Du et al. [13], Hu et al. [22]

Acetylation

Addition of acetyl group at lysine residue on SERCA

Suberanilohydroxamic acid (HDAC inhibitor)

Meraviglia et al. [42]

Allosteric activator

CDN1163

Krajnak and Dahl [31], Qaisar et al. [54]