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143 results on '"Sarkar, Parijat"'

15. Contributors

Author

Alenina, Natalia, primary, Bader, Michael, additional, Bartlett, Selena E., additional, Béchade, Catherine, additional, Beecher, Kate, additional, Belmer, Arnauld, additional, Boehm, Stefan, additional, Chattopadhyay, Amitabha, additional, Erland, Lauren A.E., additional, Fex, Malin, additional, Gaspar, Patricia, additional, He, Yanlin, additional, Hosford, Patrick S., additional, Jessup, Claire F., additional, Keating, Damien J., additional, Kumar, G. Aditya, additional, Leong, Lex, additional, Lillesaar, Christina, additional, Maclean, Jessica A., additional, Maroteaux, Luc, additional, Martin, Alyce M., additional, Monassier, Laurent, additional, Mosienko, Valentina, additional, Ohno, Yukihiro, additional, Pal, Sreetama, additional, Pilowsky, Paul M., additional, Ramage, Andrew G., additional, Rogers, Geraint B., additional, Roumier, Anne, additional, Salzer, Isabella, additional, Sarkar, Parijat, additional, Saxena, Praveen K., additional, Schoenwaelder, Simone M., additional, Sévoz-Couche, Caroline, additional, Spencer, Nick J., additional, Stenkula, Karin G., additional, Turi, Christina E., additional, Xu, Pingwen, additional, Xu, Yong, additional, Young, Richard L., additional, and Zoccal, Daniel B., additional

Published
2018
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19. Inositol Phosphoryl Transferase, Ipt1, Is a Critical Determinant of Azole Resistance and Virulence Phenotypes in Candida glabrata

Author

Shahi, Garima, primary, Kumar, Mohit, additional, Khandelwal, Nitesh Kumar, additional, Banerjee, Atanu, additional, Sarkar, Parijat, additional, Kumari, Sonam, additional, Esquivel, Brooke D., additional, Chauhan, Neeraj, additional, Chattopadhyay, Amitabha, additional, White, Theodore C., additional, Gaur, Naseem A., additional, Singh, Ashutosh, additional, and Prasad, Rajendra, additional

Published
2022
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24. Metabolic depletion of sphingolipids inhibits agonist‐induced endocytosis of the serotonin1A receptor.

Author

Kumar, Abhishek, Sarkar, Parijat, and Chattopadhyay, Amitabha

Subjects
*SEROTONIN receptors, *SPHINGOLIPIDS, *ENDOCYTOSIS, *G protein coupled receptors, *FUMONISINS, *CELL receptors, *NEUROTRANSMITTER receptors
Abstract

G protein‐coupled receptors (GPCRs) are vital cellular signaling machinery and currently represent ~40% drug targets. Endocytosis of GPCRs is an important process that allows stringent spatiotemporal control over receptor population on the cell surface. Although the role of proteins in GPCR endocytosis is well addressed, the contribution of membrane lipids in this process is rather unexplored. Sphingolipids are essential functional lipids in higher eukaryotes and are implicated in several neurological functions. To understand the role of sphingolipids in GPCR endocytosis, we subjected cells expressing human serotonin1A receptors (an important neurotransmitter GPCR involved in cognitive and behavioral functions) to metabolic sphingolipid depletion using fumonisin B1, an inhibitor of sphingolipid biosynthetic pathway. Our results, using flow cytometric analysis and confocal microscopic imaging, show that sphingolipid depletion inhibits agonist‐induced endocytosis of the serotonin1A receptor in a concentration‐dependent manner, which was restored when sphingolipid levels were replenished. We further show that there was no change in the internalization of transferrin, a marker for clathrin‐mediated endocytosis, under sphingolipid‐depleted condition, highlighting the specific requirement of sphingolipids for endocytosis of serotonin1A receptors. Our results reveal the regulatory role of sphingolipids in GPCR endocytosis and highlight the importance of neurotransmitter receptor trafficking in health and disease. [ABSTRACT FROM AUTHOR]

Published
2023
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26. Lysine 101 in the CRAC Motif in Transmembrane Helix 2 Confers Cholesterol-Induced Thermal Stability to the Serotonin1A Receptor.

Author

Sarkar, Parijat, Bhat, Akrati, and Chattopadhyay, Amitabha

Subjects
*SEROTONIN receptors, *THERMAL stability, *G protein coupled receptors, *DRUG receptors, *NEUROTRANSMITTER receptors, *LYSINE
Abstract

G protein-coupled receptors (GPCRs) constitute the largest class of membrane proteins that transduce signals across the plasma membrane and orchestrate a multitude of physiological processes within cells. The serotonin1A receptor is a crucial neurotransmitter receptor in the GPCR family involved in a multitude of neurological, behavioral and cognitive functions. We have previously shown, using a combination of experimental and simulation approaches, that membrane cholesterol acts as a key regulator of organization, dynamics, signaling and endocytosis of the serotonin1A receptor. In addition, we showed that membrane cholesterol stabilizes the serotonin1A receptor against thermal deactivation. In the present work, we explored the molecular basis of cholesterol-induced thermal stability of the serotonin1A receptor. For this, we explored the possible role of the K101 residue in a cholesterol recognition/interaction amino acid consensus (CRAC) motif in transmembrane helix 2 in conferring the thermal stability of the serotonin1A receptor. Our results show that a mutation in the K101 residue leads to loss in thermal stability of the serotonin1A receptor imparted by cholesterol, independent of membrane cholesterol content. We envision that our results could have potential implications in structural biological advancements of GPCRs and design of thermally stabilized receptors for drug development. [ABSTRACT FROM AUTHOR]

Published
2022
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