G protein-coupled receptors

G protein-coupled receptors (GPCRs) are integral membrane proteins with seven membrane-spanning helices. Upon binding to a ligand – which can range from small molecules like cyclic AMP to peptides and large proteins – GPCRs undergo a conformational change that activates heterotrimeric G proteins (guanine nucleotide-binding proteins), which are important for transmitting the extracellular, ligand signal to the cell interior.

Latest Research and Reviews

  • Research | | open

    In the healthy heart, the β2 adrenergic receptor (β2AR) signals through Gs and Gi proteins but the mechanism underlying G protein selectivity is not fully understood. Here, the authors show that membrane charge and intracellular cations modulate the β2AR−Gi3 interaction.

    • M. J. Strohman
    • , S. Maeda
    • , D. Hilger
    • , M. Masureel
    • , Y. Du
    •  & B. K. Kobilka
  • Research | | open

    Takashi Nagata et al. use UV-visible spectroscopic analysis to show that Ser186 increases the retinylidene Schiff base (SB) pKa of a spider rhodopsin in the inactive state but not after light activation. The change in contribution of Ser186 to the SB pKa suggests that the counterion (Glu181)–SB interaction rearranges upon light activation.

    • Takashi Nagata
    • , Mitsumasa Koyanagi
    • , Hisao Tsukamoto
    • , Eshita Mutt
    • , Gebhard F. X. Schertler
    • , Xavier Deupi
    •  & Akihisa Terakita
  • Research |

    The MT1 melatonin receptor differs markedly from 5-HT receptors and shows atypical ligand entry; its structure with various ligands sheds light on receptor specificity.

    • Benjamin Stauch
    • , Linda C. Johansson
    • , John D. McCorvy
    • , Nilkanth Patel
    • , Gye Won Han
    • , Xi-Ping Huang
    • , Cornelius Gati
    • , Alexander Batyuk
    • , Samuel T. Slocum
    • , Andrii Ishchenko
    • , Wolfgang Brehm
    • , Thomas A. White
    • , Nairie Michaelian
    • , Caleb Madsen
    • , Lan Zhu
    • , Thomas D. Grant
    • , Jessica M. Grandner
    • , Anna Shiriaeva
    • , Reid H. J. Olsen
    • , Alexandra R. Tribo
    • , Saïd Yous
    • , Raymond C. Stevens
    • , Uwe Weierstall
    • , Vsevolod Katritch
    • , Bryan L. Roth
    • , Wei Liu
    •  & Vadim Cherezov
    Nature 569, 284-288
  • Research |

    Structural and functional studies show that the MT2 melatonin receptor, unlike the MT1 receptor, contains an extracellular opening for ligand entry, shedding light on receptor subtype specificity.

    • Linda C. Johansson
    • , Benjamin Stauch
    • , John D. McCorvy
    • , Gye Won Han
    • , Nilkanth Patel
    • , Xi-Ping Huang
    • , Alexander Batyuk
    • , Cornelius Gati
    • , Samuel T. Slocum
    • , Chufeng Li
    • , Jessica M. Grandner
    • , Shuming Hao
    • , Reid H. J. Olsen
    • , Alexandra R. Tribo
    • , Sahba Zaare
    • , Lan Zhu
    • , Nadia A. Zatsepin
    • , Uwe Weierstall
    • , Saïd Yous
    • , Raymond C. Stevens
    • , Wei Liu
    • , Bryan L. Roth
    • , Vsevolod Katritch
    •  & Vadim Cherezov
    Nature 569, 289-292
  • Research |

    A chemogenomic approach to explore activity of the free fatty acid receptor FFA2 independently of the related FFA3 shows that FFA2 in differentiated adipocytes and colonic crypt cells in mice is responsible for regulated lipolysis and GLP-1 release.

    • Daniele Bolognini
    • , Natasja Barki
    • , Adrian J. Butcher
    • , Brian D. Hudson
    • , Eugenia Sergeev
    • , Colin Molloy
    • , Catherine E. Moss
    • , Sophie J. Bradley
    • , Christian Le Gouill
    • , Michel Bouvier
    • , Andrew B. Tobin
    •  & Graeme Milligan

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