Search bioRxiv⌕ Search

bioRxiv · 10.64898/2026.05.28.728435

An Integrative Taste Receptor Links pH and Amino Acids to Sugar Sensing in Bemisia tabaci

Abstract

Phloem-feeding insects execute complex behavioral decisions to secure essential nutrients from a diet characterized by nitrogen scarcity and severe osmotic pressure due to high sucrose concentrations. We investigated the sensory mechanisms underlying these decisions in the phloem-feeding whitefly Bemisia tabaci. We demonstrate that the sweet taste receptor BtabGR1, expressed in mouthpart and gut tissues, integrates three environmental chemical cues: sucrose concentration, the presence of the essential amino acid arginine, and pH values. Arginine is a pH-dependent positive modulator of sucrose sensing, increasing receptor responses nearly fourfold under apoplast-like conditions and more than doubling the receptor responses in the gut luminal environment. Insects show a strong feeding preference for arginine-containing diets in dual-choice bioassays, with markedly higher intake when arginine is present. RNAi-mediated silencing of BtabGR1 disrupt intake regulation, leading to increased honeydew excretion. These findings suggest a putative link between arginine and the BtabGR1 receptor in regulating both feeding-site evaluation and diet ingestion. Furthermore, the ability to integrate three distinct environmental cues makes BtabGR1 one of the most complex interdependent sensory systems described for a single insect chemoreceptor.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Aidlin Harari, O., Yakir, E., Wintraube, D., Tadmor, E., Juravel, K., Levi, K., Glik, H., Bohbot, J. D., Morin, S., Malka, O.. 2026-06-01. An Integrative Taste Receptor Links pH and Amino Acids to Sugar Sensing in Bemisia tabaci. https://doi.org/10.64898/2026.05.28.728435

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Rad and Phospholamban are Key Drivers of the Ventricular Adrenergic Response and Stress-Induced Arrhythmia

The adrenergic response is a fundamental mechanism that regulates heart rate (chronotropy), cardiac contractility (inotropy) and relaxation (lusitropy). Adrenergic stress is also a recognized trigger of arrhythmia in disease. Yet, our understanding of the underlying molecular basis remains incomplete. Protein kinase A (PKA) and the calcium/calmodulin-dependent kinase II (CaMKII) phosphorylate multiple targets proposed to participate in the adrenergic response, including the GTP-binding protein Rad, phospholamban (PLB) and ryanodine receptor 2 (RyR2). Here we demonstrate that phosphorylation of both Rad and PLB is necessary for inotropy and lusitropy. We show that changes in cardiac contractility and relaxation are primarily dependent on intracellular calcium handling. Finally, we report that Rad and PLB control stress-induced arrhythmogenesis, despite the phosphorylation of other pro-arrhythmic targets. We have identified the essential molecular components of the adrenergic response, resolving a long-standing debate in cardiac excitation-contraction coupling and refining current models of sympathetic regulation in health and disease.

physiology↗

MCT6 is an intestinal Lac-Phe exporter required for metformin-associated weight loss

Metabolites are increasingly recognized as circulating molecules that regulate physiology, yet the mechanisms that couple intracellular production to organism-wide action remain poorly defined. Using the anorexigenic metabolite Lac-Phe as a tractable system, we identify the orphan transporter MCT6 (SLC16A5) as a physiologic intestinal Lac-Phe exporter. This mechanism controls the extent to which intracellularly synthesized Lac-Phe acquires systemic activity. MCT6 transports Lac-Phe, mediates its cellular efflux, and is required for maintaining its blood levels in mice following strong glycolytic stimuli. Both global and intestinal epithelial-specific deletion of MCT6 confers resistance to metformin-associated weight loss on a high-fat diet. Bypassing the transport defect with exogenous Lac-Phe normalizes the body weight phenotype of MCT6-KO mice. Together, these data connect MCT6 to metformin pharmacology and intestinal lactate metabolism, and more generally underscore the importance of transporter-mediated release in the conversion of an intracellular metabolic state into a circulating metabolite effector.

physiology↗

DEPP1 connects nutrient and oxygen availability to maintenance of muscle mass

Nutrients and oxygen are sensed within the muscle to control growth and disruption of either signal is sufficient to lead to muscle atrophy. While nutrient limitation is sensed via a conserved transcriptional atrophy program (commonly referred to as atrogenes) dictated via the Forkhead box O (FoxO) transcription factors, how low oxygen promotes muscle loss remains unknown. Accordingly, the downstream mechanisms that initiate muscle loss when oxygen and nutrients are limiting are only partly understood. Here, we find Hypoxia Inducible Factor (HIF), the master regulator of our adaptation to low oxygen, is necessary and sufficient to mediate muscle loss under hypoxia in mice. RNA sequencing in skeletal muscle isolated from starved or hypoxic mice identifies Decidual Protein Induced by Progesterone 1 (Depp1), which is induced in skeletal muscle when nutrients or oxygen is limiting via FoxO1 and HIF activation, respectively. Whole body Depp1 loss in mice reduces muscle loss under fasting and hypoxia and skeletal muscle Depp1 overexpression is sufficient to mediate muscle atrophy. Mechanistically, Depp1 localizes to the mitochondria and is necessary to control autophagy activation and mitochondrial degradation in skeletal muscle. Taken together, our studies nominate Depp1 as a new atrogene necessary for muscle loss under multiple atrophy scenarios involving FoxO and HIF.

physiology↗