The small ubiquitin-related modifier (SUMO) can be conjugated to lysine residues of target proteins, and is involved in many cellular processes. The calcium-transporting ATPase ATP2A2, also known as SERCA2a, is SUMOylated at lysines 480 and 585 and that this SUMOylation is essential for preserving SERCA2a ATPase activity and stability in mouse and human cells. The levels of SUMO1 and the SUMOylation of SERCA2a itself are greatly reduced in failing hearts.
SUMO1 restitution by adeno-associated-virus-mediated gene delivery maintains the protein abundance of SERCA2a and markedly improves cardiac function in mice with heart failure. SUMO1 overexpression in isolated cardiomyocytes augments contractility and accelerated Ca2+ decay.
It is clear that SUMOylation is a critical post-translational modification that regulates SERCA2a function, and provides a platform for the design of novel therapeutic strategies for heart failure.
"SUMO1-dependent modulation of SERCA2a in heart failure": read the full Nature paper here.
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