Chemoproteomics identifies protein ligands for monoacylglycerol lipids

Abstract Signaling lipids are important hormone-like biomolecules that regulate many physiological processes in humans. However, a significant number of them still remain poorly characterized, despite their direct association to human diseases. While the signaling pathways regulated by the endocanna...

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Main Authors: Karthik Shanbhag, Amol B. Mhetre, Ojal Saharan, Archit Devarajan, Anisha Rai, M. S. Madhusudhan, Harinath Chakrapani, Siddhesh S. Kamat
Format: Article
Language:English
Published: Nature Portfolio 2025-07-01
Series:Communications Chemistry
Online Access:https://doi.org/10.1038/s42004-025-01589-w
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author Karthik Shanbhag
Amol B. Mhetre
Ojal Saharan
Archit Devarajan
Anisha Rai
M. S. Madhusudhan
Harinath Chakrapani
Siddhesh S. Kamat
author_facet Karthik Shanbhag
Amol B. Mhetre
Ojal Saharan
Archit Devarajan
Anisha Rai
M. S. Madhusudhan
Harinath Chakrapani
Siddhesh S. Kamat
author_sort Karthik Shanbhag
collection DOAJ
description Abstract Signaling lipids are important hormone-like biomolecules that regulate many physiological processes in humans. However, a significant number of them still remain poorly characterized, despite their direct association to human diseases. While the signaling pathways regulated by the endocannabinoid 2-arachidonoyl-glycerol in mammals are extensively characterized, the same cannot be said about other members of the monoacylglycerol (MAG) family of signaling lipids. Here, we report the synthesis of a bifunctional MAG probe, containing a photoreactive group and an alkyne handle. Using established chemoproteomics approaches coupled to bioorthogonal chemistry, we profile this bifunctional MAG probe in mouse brain and mammalian cell proteomes, and identify hitherto unknown protein ligands for MAG lipids. Finally, we find that the neuronal calcium sensor Hippocalcin is indeed a putative MAG protein ligand, and show that MAG lipids may have a role to play in calcium sensing and downstream signaling in the mammalian brain.
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institution Kabale University
issn 2399-3669
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publishDate 2025-07-01
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spelling doaj-art-5886b80d4f2f4cb7b3c39287c934e0fa2025-08-20T03:37:20ZengNature PortfolioCommunications Chemistry2399-36692025-07-018111310.1038/s42004-025-01589-wChemoproteomics identifies protein ligands for monoacylglycerol lipidsKarthik Shanbhag0Amol B. Mhetre1Ojal Saharan2Archit Devarajan3Anisha Rai4M. S. Madhusudhan5Harinath Chakrapani6Siddhesh S. Kamat7Department of Biology, Indian Institute of Science Education and ResearchDepartment of Biology, Indian Institute of Science Education and ResearchDepartment of Biology, Indian Institute of Science Education and ResearchDepartment of Biology, Indian Institute of Science Education and ResearchDepartment of Biology, Indian Institute of Science Education and ResearchDepartment of Biology, Indian Institute of Science Education and ResearchDepartment of Chemistry, Indian Institute of Science Education and ResearchDepartment of Biology, Indian Institute of Science Education and ResearchAbstract Signaling lipids are important hormone-like biomolecules that regulate many physiological processes in humans. However, a significant number of them still remain poorly characterized, despite their direct association to human diseases. While the signaling pathways regulated by the endocannabinoid 2-arachidonoyl-glycerol in mammals are extensively characterized, the same cannot be said about other members of the monoacylglycerol (MAG) family of signaling lipids. Here, we report the synthesis of a bifunctional MAG probe, containing a photoreactive group and an alkyne handle. Using established chemoproteomics approaches coupled to bioorthogonal chemistry, we profile this bifunctional MAG probe in mouse brain and mammalian cell proteomes, and identify hitherto unknown protein ligands for MAG lipids. Finally, we find that the neuronal calcium sensor Hippocalcin is indeed a putative MAG protein ligand, and show that MAG lipids may have a role to play in calcium sensing and downstream signaling in the mammalian brain.https://doi.org/10.1038/s42004-025-01589-w
spellingShingle Karthik Shanbhag
Amol B. Mhetre
Ojal Saharan
Archit Devarajan
Anisha Rai
M. S. Madhusudhan
Harinath Chakrapani
Siddhesh S. Kamat
Chemoproteomics identifies protein ligands for monoacylglycerol lipids
Communications Chemistry
title Chemoproteomics identifies protein ligands for monoacylglycerol lipids
title_full Chemoproteomics identifies protein ligands for monoacylglycerol lipids
title_fullStr Chemoproteomics identifies protein ligands for monoacylglycerol lipids
title_full_unstemmed Chemoproteomics identifies protein ligands for monoacylglycerol lipids
title_short Chemoproteomics identifies protein ligands for monoacylglycerol lipids
title_sort chemoproteomics identifies protein ligands for monoacylglycerol lipids
url https://doi.org/10.1038/s42004-025-01589-w
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