Illuminating GPCR Signaling by Cryo-EM

Trends in Cell Biology

Volumn 28, Issue 8, 2018, Pages 591-594

  Safdari, Haaris Ahsan ^a   Pandey, Shubhi ^b   Shukla, Arun K ^b   Dutta, Somnath ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b INDIAN INSTITUTE OF TECHNOLOGY KANPUR   (India)

Author keywords

arrestins; biased signaling; cryo EM; GPCR; negative staining

Indexed keywords

ADENOSINE A2A RECEPTOR; CALCITONIN RECEPTOR; G PROTEIN COUPLED RECEPTOR;

AMINO TERMINAL SEQUENCE; CRYOELECTRON MICROSCOPY; CRYSTALLIZATION; CRYSTALLOGRAPHY; GPCR SIGNALING; HUMAN; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SHORT SURVEY; SIGNAL TRANSDUCTION; CHEMISTRY; METABOLISM;

CRYOELECTRON MICROSCOPY; HUMANS; RECEPTORS, G-PROTEIN-COUPLED; SIGNAL TRANSDUCTION;

EID: 85048873187     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2018.06.002     Document Type: Short Survey

References (15)

1. Kumari, P., et al. Emerging approaches to GPCR ligand screening for drug discovery. Trends Mol. Med. 21 (2015), 687–701.
2. Ghosh, E., et al. Methodological advances: the unsung heroes of the GPCR structural revolution. Nat. Rev. Mol. Cell Biol. 16 (2015), 69–81.
3. Rasmussen, S.G., et al. Crystal structure of the beta2 adrenergic receptor-Gs protein complex. Nature 477 (2011), 549–555.
4. Liang, Y.L., et al. Phase-plate cryo-EM structure of a class B GPCR-G-protein complex. Nature 546 (2017), 118–123.
5. Zhang, Y., et al. Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein. Nature 546 (2017), 248–253.
6. Liang, Y.L., et al. Phase-plate cryo-EM structure of a biased agonist-bound human GLP-1 receptor-Gs complex. Nature 555 (2018), 121–125.
7. Garcia-Nafria, J., et al. Cryo-EM structure of the adenosine A2A receptor coupled to an engineered heterotrimeric G protein. eLife, 7, 2018, e35946.
8. Farrens, D.L., et al. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274 (1996), 768–770.
9. Baidya, M., et al. Frozen in action: cryo-EM structure of a GPCR-G-protein complex. Nat. Struct. Mol. Biol. 24 (2017), 500–502.
10. Westfield, G.H., et al. Structural flexibility of the G alpha s alpha-helical domain in the beta2-adrenoceptor Gs complex. Proc. Natl. Acad. Sci. U. S. A. 108 (2011), 16086–16091.
11. Shukla, A.K., et al. Visualization of arrestin recruitment by a G-protein-coupled receptor. Nature 512 (2014), 218–222.
12. Thomsen, A.R.B., et al. GPCR-G protein-beta-arrestin super-complex mediates sustained G protein signaling. Cell 166 (2016), 907–919.
13. Kumari, P., et al. Functional competence of a partially engaged GPCR-beta-arrestin complex. Nat. Commun., 7, 2016, 13416.
14. Kumari, P., et al. Core engagement with beta-arrestin is dispensable for agonist-induced vasopressin receptor endocytosis and ERK activation. Mol. Biol. Cell 28 (2017), 1003–1010.
15. Cahill, T.J. 3rd, et al. Distinct conformations of GPCR-beta-arrestin complexes mediate desensitization, signaling, and endocytosis. Proc. Natl. Acad. Sci. U. S. A. 114 (2017), 2562–2567.