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Biology subjects

Darbha, S.

Publications and source records attributed to Darbha, S..

2 recordsLinked to original sources

BCKDK Inhibitors Directly Antagonize Angiotensin II Type 1 Receptor and Induce Vasodilation Independently of BCAA Catabolism or BCKDK

Branched-chain amino acids (BCAA) have been implicated in diabetes and heart failure, leading to ongoing clinical trials with inhibitors of BCKDK, a key regulator of BCAA catabolism. We have previously shown that these inhibitors promote vasodilation and lower blood pressure, well-known cardioprotective effects, but how this occurs remained unclear. We show here, using explanted vessels, in vivo hemodynamics and telemetry, and genetically modified mice, that the vasodilatory effect of BCKDK inhibitors is direct, rapid, independent of nitric oxide, independent of BCAA catabolism, and most strikingly, independent of BCKDK itself. Instead, we demonstrate, using structural and biochemical studies, that BCKDK inhibitors directly antagonize the angiotensin II type I receptor (AT1R) and consequent angiotensin-mediated vasoconstriction. These data demonstrate a strong off-target effect of BCKDK inhibitors, independent of BCAA or BCKDK, which may explain their cardioprotective effects but also questions if this protection would be additive to existing AT1R blockers.

physiology↗

Location-biased β-arrestin conformations direct GPCR signaling

{beta}-arrestins are multifunctional intracellular proteins that regulate the desensitization, internalization and signaling of over 800 different G protein-coupled receptors (GPCRs) and interact with a diverse array of cellular partners1,2. Beyond the plasma membrane, GPCRs can initiate unique signaling cascades from various subcellular locations, a phenomenon known as "location bias"3,4. Here, we investigate how {beta}-arrestins direct location-biased signaling of the angiotensin II type I receptor (AT1R). Using novel bioluminescence resonance energy transfer (BRET) conformational biosensors and extracellular signal-regulated kinase (ERK) activity reporters, we reveal that in response to the endogenous agonist Angiotensin II and the {beta}-arrestin-biased agonist TRV023, {beta}-arrestin 1 and {beta}-arrestin 2 adopt distinct conformations across different subcellular locations, which are intricately linked to differential ERK activation profiles. We also uncover a population of receptor-free catalytically activated {beta}-arrestins in the plasma membrane that exhibits insensitivity to different agonists and promotes ERK activation on the plasma membrane independent of G proteins. These findings deepen our understanding of GPCR signaling complexity and also highlight the nuanced roles of {beta}-arrestins beyond traditional G protein pathways.

biochemistry↗