Agonist binding affinity determines palmitoylation of the glucagon-like peptide-1 receptor and its f...
Agonist binding affinity determines palmitoylation of the glucagon-like peptide-1 receptor and its functional interaction with plasma membrane nanodomains in pancreatic beta cells
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Author / Creator
Buenaventura, Teresa , Laughlin, William E , Bitsi, Stavroula , Burgoyne, Thomas , Lyu, Zekun , Oqua, Affiong I , Hannah, Norman , Mcglone, Emma R , Klymchenko, Andrey S , Corrêa, Ivan R , Walker, Abigail , Inoue, Asuka , Hanyaloglou, Aylin , Rutter, Guy A , Bloom, Stephen R , Jones, Ben and Tomas, Alejandra
Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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English
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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Contents
The glucagon-like peptide-1 receptor (GLP-1R), a key pharmacological target in type 2 diabetes and obesity, is known to undergo palmitoylation by covalent ligation of an acyl chain to cysteine 438 in its carboxyl-terminal tail. Work with other GPCRs indicates that palmitoylation can be dynamically regulated to allow receptors to partition into plas...
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Full title
Agonist binding affinity determines palmitoylation of the glucagon-like peptide-1 receptor and its functional interaction with plasma membrane nanodomains in pancreatic beta cells
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TN_cdi_proquest_journals_2153840188
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2153840188
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E-ISSN
2692-8205
DOI
10.1101/492496
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https://www.proquest.com/docview/2153840188?pq-origsite=primo&accountid=13902
