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Molecular Mechanisms Subserving Taste and Olfaction Systems

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Neurobiology".

Deadline for manuscript submissions: 30 September 2024 | Viewed by 3099

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Dr. Lindsey Schier

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Guest Editor

Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA
Interests: ingestive behavior; taste; chemosensory systems; food learning & memory; gut-brain axis

Special Issue Information

Dear Colleagues,

Olfaction and gustation are the two main sensory systems that subserve nutrition. Our ability to rapidly and accurately sense the odorants and tastants released from foods enables us to locate, select, and ingest the essential compounds required for good health and survival, and avoid those that may be detrimental. Although both chemosensory systems come hardwired to detect these biologically significant substances in the environment, they are also highly plastic, shaped by experience and physiological conditions. Empirical evidence has showcased the sheer complexity of canonical and non-canonical molecular machinery present in chemosensory end organs and pathways, through which their signals are broadcast to higher-order brain areas for integrative processing. However, precise knowledge on how these peripheral and central systems facilitate dynamic sensing and orchestrate adaptive behaviors, as well as how they are in turn regulated by diverse factors (such as genes, diets and disease states across the lifespan), is lacking. For this Special Issue, we invite original research articles and critical reviews that advance our understanding of the molecular mechanisms that subserve chemosensory function.

Dr. Lindsey Schier
Guest Editor

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Keywords

taste
olfaction
gustation
odor
chemoreception
taste bud cells
nutrient sensing
ingestive behavior
olfactory cilia
olfactory receptor neurons
olfactory bulb
gustatory cortex
piriform cortex
sensory development
food learning
neural plasticity
obesity
eating disorders
appetite

Published Papers (4 papers)

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Research

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21 pages, 3138 KiB

Open AccessArticle

Response Plasticity of Drosophila Olfactory Sensory Neurons

by Lorena Halty-deLeon, Venkatesh Pal Mahadevan, Eric Wiesel, Bill S. Hansson and Dieter Wicher

Int. J. Mol. Sci. 2024, 25(13), 7125; https://doi.org/10.3390/ijms25137125 - 28 Jun 2024

Viewed by 389

Abstract

In insect olfaction, sensitization refers to the amplification of a weak olfactory signal when the stimulus is repeated within a specific time window. In the vinegar fly, Drosophila melanogaster, this occurs already at the periphery, at the level of olfactory sensory neurons (OSNs) located in the antenna. In our study, we investigate whether sensitization is a widespread property in a set of seven types of OSNs, as well as the mechanisms involved. First, we characterize and compare the differences in spontaneous activity, response velocity and response dynamics, among the selected OSN types. These express different receptors with distinct tuning properties and behavioral relevance. Second, we show that sensitization is not a general property. Among our selected OSN types, it occurs in those responding to more general food odors, while OSNs involved in very specific detection of highly specific ecological cues like pheromones and warning signals show no sensitization. Moreover, we show that mitochondria play an active role in sensitization by contributing to the increase in intracellular Ca²⁺ upon weak receptor activation. Thus, by using a combination of single sensillum recordings (SSRs), calcium imaging and pharmacology, we widen the understanding of how the olfactory signal is processed at the periphery. Full article

(This article belongs to the Special Issue Molecular Mechanisms Subserving Taste and Olfaction Systems)

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21 pages, 3873 KiB

Open AccessArticle

Role of iRhom2 in Olfaction: Implications for Odorant Receptor Regulation and Activity-Dependent Adaptation

by Stephanie A. Azzopardi, Hsiu-Yi Lu, Sebastien Monette, Ariana I. Rabinowitsch, Jane E. Salmon, Hiroaki Matsunami and Carl P. Blobel

Int. J. Mol. Sci. 2024, 25(11), 6079; https://doi.org/10.3390/ijms25116079 - 31 May 2024

Viewed by 768

Abstract

The cell surface metalloprotease ADAM17 (a disintegrin and metalloprotease 17) and its binding partners iRhom2 and iRhom1 (inactive Rhomboid-like proteins 1 and 2) modulate cell–cell interactions by mediating the release of membrane proteins such as TNFα (Tumor necrosis factor α) and EGFR (Epidermal growth factor receptor) ligands from the cell surface. Most cell types express both iRhoms, though myeloid cells exclusively express iRhom2, and iRhom1 is the main iRhom in the mouse brain. Here, we report that iRhom2 is uniquely expressed in olfactory sensory neurons (OSNs), highly specialized cells expressing one olfactory receptor (OR) from a repertoire of more than a thousand OR genes in mice. iRhom2-/- mice had no evident morphological defects in the olfactory epithelium (OE), yet RNAseq analysis revealed differential expression of a small subset of ORs. Notably, while the majority of ORs remain unaffected in iRhom2-/- OE, OSNs expressing ORs that are enriched in iRhom2-/- OE showed fewer gene expression changes upon odor environmental changes than the majority of OSNs. Moreover, we discovered an inverse correlation between the expression of iRhom2 compared to OSN activity genes and that odor exposure negatively regulates iRhom2 expression. Given that ORs are specialized G-protein coupled receptors (GPCRs) and many GPCRs activate iRhom2/ADAM17, we investigated if ORs could activate iRhom2/ADAM17. Activation of an olfactory receptor that is ectopically expressed in keratinocytes (OR2AT4) by its agonist Sandalore leads to ERK1/2 phosphorylation, likely via an iRhom2/ADAM17-dependent pathway. Taken together, these findings point to a mechanism by which odor stimulation of OSNs activates iRhom2/ADAM17 catalytic activity, resulting in downstream transcriptional changes to the OR repertoire and activity genes, and driving a negative feedback loop to downregulate iRhom2 expression. Full article

(This article belongs to the Special Issue Molecular Mechanisms Subserving Taste and Olfaction Systems)

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17 pages, 7716 KiB

Open AccessArticle

EsigPBP3 Was the Important Pheromone-Binding Protein to Recognize Male Pheromones and Key Eucalyptus Volatiles

by Hengfei Fu, Guipeng Xiao, Zhende Yang and Ping Hu

Int. J. Mol. Sci. 2024, 25(5), 2940; https://doi.org/10.3390/ijms25052940 - 3 Mar 2024

Viewed by 1028

Abstract

Pheromone-binding proteins (PBPs) are specific odorant-binding proteins that can specifically recognize insect pheromones. Through transcriptional analysis of the antennae of adult Endoclita signifer, EsigPBP3 was discovered and identified, and EsigPBP3 was found to be highly expressed in the antennae of male moths. Based on the binding characteristics and ability of EsigPBP3, we can find the key ligands and binding site to consider as a target to control the key wood bore E. signifier. In this study, the fluorescence competitive binding assays (FCBA) showed that EsigPBP3 had a high binding affinity for seven key eucalyptus volatiles. Molecular docking analysis revealed that EsigPBP3 had the strongest binding affinity for the sexual pheromone component, (3E,7E)-4,7,11-trimethyl-1,3,7,10-dodecatetraene. Furthermore, same as the result of FCBA, the EsigPBP3 exhibited high binding affinities to key eucalyptus volatiles, eucalyptol, α-terpinene, (E)-beta-ocimene, (−)-β-pinene, and (−)-α-pinene, and PHE35, MET7, VAL10, PHE38, ILE52, and PHE118 are key sites. In summary, EsigPBP3 exhibits high binding affinity to male pheromones and key volatile compounds and the crucial binding sites PHE35, MET7, VAL10, PHE38, ILE52, and PHE118 can act as targets in the recognition of E. signifier pheromones. Full article

(This article belongs to the Special Issue Molecular Mechanisms Subserving Taste and Olfaction Systems)

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Review

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20 pages, 1712 KiB

Open AccessReview

Mechanisms and Functions of Sweet Reception in Oral and Extraoral Organs

by Ryusuke Yoshida and Yuzo Ninomiya

Int. J. Mol. Sci. 2024, 25(13), 7398; https://doi.org/10.3390/ijms25137398 - 5 Jul 2024

Viewed by 281

Abstract

The oral detection of sugars relies on two types of receptor systems. The first is the G-protein-coupled receptor TAS1R2/TAS1R3. When activated, this receptor triggers a downstream signaling cascade involving gustducin, phospholipase Cβ2 (PLCβ2), and transient receptor potential channel M5 (TRPM5). The second type of receptor is the glucose transporter. When glucose enters the cell via this transporter, it is metabolized to produce ATP. This ATP inhibits the opening of K_ATP channels, leading to cell depolarization. Beside these receptor systems, sweet-sensitive taste cells have mechanisms to regulate their sensitivity to sweet substances based on internal and external states of the body. Sweet taste receptors are not limited to the oral cavity; they are also present in extraoral organs such as the gastrointestinal tract, pancreas, and brain. These extraoral sweet receptors are involved in various functions, including glucose absorption, insulin release, sugar preference, and food intake, contributing to the maintenance of energy homeostasis. Additionally, sweet receptors may have unique roles in certain organs like the trachea and bone. This review summarizes past and recent studies on sweet receptor systems, exploring the molecular mechanisms and physiological functions of sweet (sugar) detection in both oral and extraoral organs. Full article

(This article belongs to the Special Issue Molecular Mechanisms Subserving Taste and Olfaction Systems)

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