AI Article Synopsis
- - ACE2 plays a crucial role in regulating blood pressure and acts as the main receptor for the SARS-CoV-2 virus, linking it to both cardiovascular health and COVID-19.
- - Researchers discovered that a process involving γ-secretase (γS) can lead to the breakdown of ACE2, where its soluble fragment is released after an initial shedding from the cell surface.
- - Inhibiting γS doesn't affect how SARS-CoV-2 enters cells, but it does highlight a new mechanism for how ACE2 is processed and managed within cells.
Article Abstract
Angiotensin converting enzyme 2 (ACE2) is a key regulator of the renin-angiotensin system, but also the functional receptor of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Based on structural similarity with other γ-secretase (γS) targets, we hypothesized that ACE2 may be affected by γS proteolytic activity. We found that after ectodomain shedding, ACE2 is targeted for intramembrane proteolysis by γS, releasing a soluble ACE2 C-terminal fragment. Consistently, chemical or genetic inhibition of γS results in the accumulation of a membrane-bound fragment of ectodomain-deficient ACE2. Although chemical inhibition of γS does not alter SARS-CoV-2 cell entry, these data point to a novel pathway for cellular ACE2 trafficking.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8105332 | PMC |
| http://dx.doi.org/10.1038/s41598-021-89379-x | DOI Listing |
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