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ProtMetD: Protein Modifications, Metabolism and Disease
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Tension release by N-terminal acetylation

Hypertension or high blood pressure is a major health problem that can result in cardiovascular diseases including hypertensive crisis and stroke. A recent paper in Science by Hwang and Varshavsky shows that the molecular signaling underlying regulation of blood pressure involves N-terminal acetylation of specific proteins and their consecutive degradation by the N-end rule pathway.

Illustrasjon
Taking the N-end rule to the next level. A recent study links N-terminal acetylation and N-end rule degradation to blood pressure regulation. N-terminal mutants of Rgs2 (a key G-protein regulator) are found in patients with hypertension. These are differentially processed by N-terminal acetyltransferases (NATs) and the two branches of the N-end rule pathway. This leads to an imbalance in the signaling governing blood pressure. Refer to original Spotlight in TiBS for details.

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Hypertension or high blood pressure is a major health problem that can result in cardiovascular diseases including hypertensive crisis and stroke. A recent paper in Science by Hwang and Varshavsky shows that the molecular signaling underlying regulation of blood pressure involves N-terminal acetylation of specific proteins and their consecutive degradation by the N-end rule pathway.

 

N-terminal acetylation is a modification that happens to about 80% of the cell’s proteins. For some N-terminally acetylated proteins, the modification is associated with a shorter molecular lifespan (half-life). However, we still know little about how such molecular effects of N-terminal acetylation are connected to physiological functioning. In a Spotlight article in Trends in Biochemical Sciences (TiBS), Aksnes and colleagues in the NAT group describe this recently revealed connection to blood pressure pathology to provide a new physiological understanding of the N-end rule pathway and N-terminal acetylation.