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481 results on '"Jayaraman, Vasanthi"'

4. Partial agonism in heteromeric GLUK2/GLUK5 kainate receptor.

Author

Paudyal, Nabina, Das, Anindita, Carrillo, Elisa, Berka, Vladimir, and Jayaraman, Vasanthi

Abstract

Kainate receptors are a subtype of ionotropic glutamate receptors that form transmembrane channels upon binding glutamate. Here, we have investigated the mechanism of partial agonism in heteromeric GluK2/K5 receptors, where the GluK2 and GluK5 subunits have distinct agonist binding profiles. Using single‐molecule Förster resonance energy transfer, we found that at the bi‐lobed agonist‐binding domain, the partial agonist AMPA‐bound receptor occupied intermediate cleft closure conformational states at the GluK2 cleft, compared to the more open cleft conformations in apo form and more closed cleft conformations in the full agonist glutamate‐bound form. In contrast, there is no significant difference in cleft closure states at the GluK5 agonist‐binding domain between the partial agonist AMPA‐ and full agonist glutamate‐bound states. Additionally, unlike the glutamate‐bound state, the dimer interface at the agonist‐binding domain is not decoupled in the AMPA‐bound state. Our findings suggest that partial agonism observed with AMPA binding is mediated primarily due to differences in the GluK2 subunit, highlighting the distinct contributions of the subunits towards activation. [ABSTRACT FROM AUTHOR]

Published
2025
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6. Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels

Author

Hansen, Kasper B., Wollmuth, Lonnie P., Bowie, Derek, Furukawa, Hiro, Menniti, Frank S., Sobolevsky, Alexander I., Swanson, Geoffrey T., Swanger, Sharon A., Greger, Ingo H., Nakagawa, Terunaga, McBain, Chris J., Jayaraman, Vasanthi, Low, Chian-Ming, Dell’Acqua, Mark L., Diamond, Jeffrey S., Camp, Chad R., Perszyk, Riley E., Yuan, Hongjie, and Traynelis, Stephen F.

Published
2021
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42. Ca2+ efflux facilitated by co-transport of inorganic phosphate anion in the H+/Ca2+ antiporter YfkE.

Author

Niu, Wei, Zhou, Wenchang, Lu, Shuo, Vu, Trung, Jayaraman, Vasanthi, Faraldo-Gómez, José D., and Zheng, Lei

Subjects
PHOSPHATES, ANIONS, BINDING sites
Abstract

Ca2+ is an important signaling messenger. In microorganisms, fungi, and plants, H+/Ca2+ antiporters (CAX) are known to play key roles in the homeostasis of intracellular Ca2+ by catalyzing its efflux across the cell membrane. Here, we reveal that the bacterial CAX homolog YfkE transports Ca2+ in two distinct modes: a low-flux H+/Ca2+ exchange mode and a high-flux mode in which Ca2+ and phosphate ions are co-transported (1:1) in exchange for H+. Coupling with phosphate greatly accelerates the Ca2+ efflux activity of YfkE. Our studies reveal that Ca2+ and phosphate bind to adjacent sites in a central translocation pathway and lead to mechanistic insights that explain how this CAX alters its conserved alpha-repeat motifs to adopt phosphate as a specific "transport chaperon" for Ca2+ translocation. This finding uncovers a co-transport mechanism within the CAX family that indicates this class of proteins contributes to the cellular homeostasis of both Ca2+ and phosphate. Bacterial CAX antiporter homolog YfkE can transport Ca2+ and inorganic phosphate (Pi) together in a 1:1 ratio, exchanging them for H+ and becoming a high-flux antiporter when coupled with Pi. [ABSTRACT FROM AUTHOR]

Published
2023
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