Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41594-019-0330-y
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dc.titleStructure of an endosomal signaling GPCR-G protein-beta-arrestin megacomplex
dc.contributor.authorNguyen, Anthony H
dc.contributor.authorThomsen, Alex RB
dc.contributor.authorCahill, Thomas J
dc.contributor.authorHuang, Rick
dc.contributor.authorHuang, Li-Yin
dc.contributor.authorMarcink, Tara
dc.contributor.authorClarke, Oliver B
dc.contributor.authorHeissel, Soren
dc.contributor.authorMasoudi, Ali
dc.contributor.authorBen-Hail, Danya
dc.contributor.authorSamaan, Fadi
dc.contributor.authorDandey, Venkata P
dc.contributor.authorTan, Yong Zi
dc.contributor.authorHong, Chuan
dc.contributor.authorMahoney, Jacob P
dc.contributor.authorTriest, Sarah
dc.contributor.authorLittle, John
dc.contributor.authorChen, Xin
dc.contributor.authorSunahara, Roger
dc.contributor.authorSteyaert, Jan
dc.contributor.authorMolina, Henrik
dc.contributor.authorYu, Zhiheng
dc.contributor.authordes Georges, Amedee
dc.contributor.authorLefkowitz, Robert J
dc.date.accessioned2022-06-20T07:32:09Z
dc.date.available2022-06-20T07:32:09Z
dc.date.issued2019-12-01
dc.identifier.citationNguyen, Anthony H, Thomsen, Alex RB, Cahill, Thomas J, Huang, Rick, Huang, Li-Yin, Marcink, Tara, Clarke, Oliver B, Heissel, Soren, Masoudi, Ali, Ben-Hail, Danya, Samaan, Fadi, Dandey, Venkata P, Tan, Yong Zi, Hong, Chuan, Mahoney, Jacob P, Triest, Sarah, Little, John, Chen, Xin, Sunahara, Roger, Steyaert, Jan, Molina, Henrik, Yu, Zhiheng, des Georges, Amedee, Lefkowitz, Robert J (2019-12-01). Structure of an endosomal signaling GPCR-G protein-beta-arrestin megacomplex. NATURE STRUCTURAL & MOLECULAR BIOLOGY 26 (12) : 1123-+. ScholarBank@NUS Repository. https://doi.org/10.1038/s41594-019-0330-y
dc.identifier.issn15459993
dc.identifier.issn15459985
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/227206
dc.description.abstractClassically, G-protein-coupled receptors (GPCRs) are thought to activate G protein from the plasma membrane and are subsequently desensitized by β-arrestin (β-arr). However, some GPCRs continue to signal through G protein from internalized compartments, mediated by a GPCR–G protein–β-arr ‘megaplex’. Nevertheless, the molecular architecture of the megaplex remains unknown. Here, we present its cryo-electron microscopy structure, which shows simultaneous engagement of human G protein and bovine β-arr to the core and phosphorylated tail, respectively, of a single active human chimeric β2-adrenergic receptor with the C-terminal tail of the arginine vasopressin type 2 receptor (β2V2R). All three components adopt their canonical active conformations, suggesting that a single megaplex GPCR is capable of simultaneously activating G protein and β-arr. Our findings provide a structural basis for GPCR-mediated sustained internalized G protein signaling.
dc.language.isoen
dc.publisherNATURE PUBLISHING GROUP
dc.sourceElements
dc.subjectScience & Technology
dc.subjectLife Sciences & Biomedicine
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.subjectCell Biology
dc.subjectCRYO-EM STRUCTURE
dc.subjectCRYSTAL-STRUCTURE
dc.subjectCOUPLED RECEPTOR
dc.subjectPEPTIDE IDENTIFICATION
dc.subjectGLP-1 RECEPTOR
dc.subjectCOMPLEX
dc.subjectVISUALIZATION
dc.subjectRESOLUTION
dc.subjectDESENSITIZATION
dc.subjectBETA-ARRESTIN1
dc.typeArticle
dc.date.updated2022-06-18T14:55:05Z
dc.contributor.departmentDEPT OF BIOLOGICAL SCIENCES
dc.description.doi10.1038/s41594-019-0330-y
dc.description.sourcetitleNATURE STRUCTURAL & MOLECULAR BIOLOGY
dc.description.volume26
dc.description.issue12
dc.description.page1123-+
dc.published.statePublished
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