Robert Margolskee | |
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![]() Margolskee at Monell Chemical Senses Center | |
Alma mater | Harvard University |
Known for | Mammalian taste transduction |
Awards | IFF Award, Monell Mastertaste-Manheimer Award |
Scientific career | |
Fields | Biology, molecular genetics |
Institutions | Monell Chemical Senses Center |
Doctoral advisor | Daniel Nathans |
Robert F. Margolskee is an American academic. He is the director of the Monell Chemical Senses Center and adjunct professor in the Department of Neuroscience at the Mount Sinai School of Medicine. Margolskee is also the a co-founder of Redpoint Bio. Margolskee has been a pioneer in the application of molecular biology and transgenic animal models to the study of taste transduction and chemosensation. He has made numerous seminal discoveries in the taste field, including the identification and molecular cloning of taste specific receptors, G proteins, channels and other taste signal transduction elements.
Margolskee received his A.B. in biochemistry and molecular biology from Harvard University. He received his an M.D. and a Ph.D in molecular genetics from Johns Hopkins University, where he studied with the late Nobel laureate Daniel Nathans. He carried out postdoctoral studies in biochemistry at Stanford University with Nobel laureate Paul Berg.
Margolskee’s first faculty appointment was in Neuroscience at the Roche Institute of Molecular Biology, where he also held an adjunct appointment in the Department of Biological Sciences of Columbia University. In 1996, Margolskee joined the faculty of the Mount Sinai School of Medicine. [1] [2] In 2009, he joined the faculty at the Monell Center. [3] His work has been published in Nature , Science , Nature Neuroscience , and Scientific American . [3]
Margolskee’s basic science research focus has been on the molecular mechanisms of taste transduction, utilizing molecular biology, biochemistry, structural biology, electrophysiology and transgenesis to study the mechanisms of signal transduction in mammalian taste cells. In 1992, his laboratory discovered gustducin, a taste cell expressed G protein. [4] Subsequently, Margolskee has demonstrated that gustducin is critical to the transduction of compounds that humans consider bitter, sweet or umami. [5] Margolskee’s laboratory discovered the T1r3 sweet taste receptor in 2001 [6] and the Trpm5 cation channel in 2002. [7] Much of his current work is focused on 'taste cells of the gut' and 'endocrine cells of the tongue'. In 2007, he published back-to-back papers in the Proceedings of the National Academy shedding light on how the gut "tastes" nutrients. [8] [9] This new area of research has important implications for diabetes and obesity.
Among his honors and awards are the Monell Mastertaste-Manheimer Award (now the Manheimer-Kerry award) and the IFF Award. [10] [11]
The myenteric plexus provides motor innervation to both layers of the muscular layer of the gut, having both parasympathetic and sympathetic input, whereas the submucous plexus provides secretomotor innervation to the mucosa nearest the lumen of the gut.
Sweetness is a basic taste most commonly perceived when eating foods rich in sugars. Sweet tastes are generally regarded as pleasurable. In addition to sugars like sucrose, many other chemical compounds are sweet, including aldehydes, ketones, and sugar alcohols. Some are sweet at very low concentrations, allowing their use as non-caloric sugar substitutes. Such non-sugar sweeteners include saccharin and aspartame. Other compounds, such as miraculin, may alter perception of sweetness itself.
TAS2R16 is a human gene that encodes for a receptor that may play a role in the perception of bitterness.
A taste receptor or tastant is a type of cellular receptor which facilitates the sensation of taste. When food or other substances enter the mouth, molecules interact with saliva and are bound to taste receptors in the oral cavity and other locations. Molecules which give a sensation of taste are considered "sapid".
Gustducin is a G protein associated with taste and the gustatory system, found in some taste receptor cells. Research on the discovery and isolation of gustducin is recent. It is known to play a large role in the transduction of bitter, sweet and umami stimuli. Its pathways are many and diverse.
Transient receptor potential cation channel subfamily M member 5 (TRPM5), also known as long transient receptor potential channel 5 is a protein that in humans is encoded by the TRPM5 gene.
Taste receptor type 2 member 1 (TAS2R1/T2R1) is a protein that in humans is encoded by the TAS2R1 gene. It belongs to the G protein-coupled receptor (GPCR) family and is related to class A-like GPCRs, they contain 7 transmembrane helix bundles and short N-terminus loop. Furthermore, TAS2R1 is member of the 25 known human bitter taste receptors, which enable the perception of bitter taste in the mouth cavity. Increasing evidence indicates a functional role of TAS2Rs in extra-oral tissues.
Taste receptor type 2 member 3 is a protein that in humans is encoded by the TAS2R3 gene.
Taste receptor type 2 member 4 is a protein that in humans is encoded by the TAS2R4 gene.
Taste receptor type 2 member 8 is a protein that in humans is encoded by the TAS2R8 gene.
Taste receptor type 2 member 9 is a protein that in humans is encoded by the TAS2R9 gene.
Taste receptor type 2 member 10 is a protein that in humans is encoded by the TAS2R10 gene. The protein is responsible for bitter taste recognition in mammals. It serves as a defense mechanism to prevent consumption of toxic substances which often have a characteristic bitter taste.
Taste receptors for bitter substances (T2Rs/TAS2Rs) belong to the family of G-protein coupled receptors and are related to class A-like GPCRs. There are 25 known T2Rs in humans responsible for bitter taste perception.
Taste receptor type 2 member 5 is a protein that in humans is encoded by the TAS2R5 gene.
Taste receptor type 1 member 3 is a protein that in humans is encoded by the TAS1R3 gene. The TAS1R3 gene encodes the human homolog of mouse Sac taste receptor, a major determinant of differences between sweet-sensitive and -insensitive mouse strains in their responsiveness to sucrose, saccharin, and other sweeteners.
Taste receptor type 2 member 43 is a protein that in humans is encoded by the TAS2R43 gene.
Taste receptor type 2 member 19 is a protein that in humans is encoded by the TAS2R19 gene. It seems to be involved in the perception of salt and bitter tastes.
Solitary chemosensory cells (SCCs) are isolated elements located in epithelia of the apparatuses of endodermic origin. In the aquatic vertebrates, SCCs are also present in the skin. In oral cavity, SCCs precedes the development of taste buds. For long time, SCCs were considered to be typical of aquatic vertebrates. Recently, these elements were also demonstrated in mammals.
Chemosensory clusters are aggregates formed by a small number of chemoreceptor cells with characteristics similar to those found in the taste cells of the oropharyngeal cavity. The chemosensory clusters are similar to the taste buds but are smaller, resembling the developing taste buds. Chemosensory clusters are located in the larynx distally to the portion in which are present laryngeal taste buds and proximally to the region in which solitary chemosensory cells are found. Rarely, chemosensory clusters may be found in the distal portion of the airway.
Guanine nucleotide-binding protein G(t) subunit alpha-3, also known as gustducin alpha-3 chain, is a protein subunit that in humans is encoded by the GNAT3 gene.