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@ARTICLE{Navarro:130228,
      author       = {G. Navarro and A. Cordomí and M. Zelman-Femiak$^*$ and M.
                      Brugarolas and E. Moreno and D. Aguinaga and L. Perez-Benito
                      and A. Cortés and V. Casadó and J. Mallol and E. I. Canela
                      and C. Lluís and L. Pardo and A. J. García-Sáez$^*$ and
                      P. J. McCormick and R. Franco},
      title        = {{Q}uaternary structure of a {G}-protein-coupled receptor
                      heterotetramer in complex with {G}i and {G}s.},
      journal      = {BMC biology},
      volume       = {14},
      number       = {1},
      issn         = {1741-7007},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {DKFZ-2017-05308},
      pages        = {26},
      year         = {2016},
      abstract     = {G-protein-coupled receptors (GPCRs), in the form of
                      monomers or homodimers that bind heterotrimeric G proteins,
                      are fundamental in the transfer of extracellular stimuli to
                      intracellular signaling pathways. Different GPCRs may also
                      interact to form heteromers that are novel signaling units.
                      Despite the exponential growth in the number of solved GPCR
                      crystal structures, the structural properties of heteromers
                      remain unknown.We used single-particle tracking experiments
                      in cells expressing functional adenosine A1-A2A receptors
                      fused to fluorescent proteins to show the loss of Brownian
                      movement of the A1 receptor in the presence of the A2A
                      receptor, and a preponderance of cell surface 2:2 receptor
                      heteromers (dimer of dimers). Using computer modeling, aided
                      by bioluminescence resonance energy transfer assays to
                      monitor receptor homomerization and heteromerization and
                      G-protein coupling, we predict the interacting interfaces
                      and propose a quaternary structure of the GPCR tetramer in
                      complex with two G proteins.The combination of results
                      points to a molecular architecture formed by a
                      rhombus-shaped heterotetramer, which is bound to two
                      different interacting heterotrimeric G proteins (Gi and Gs).
                      These novel results constitute an important advance in
                      understanding the molecular intricacies involved in GPCR
                      function.},
      keywords     = {Receptors, Purinergic P1 (NLM Chemicals) / Heterotrimeric
                      GTP-Binding Proteins (NLM Chemicals)},
      cin          = {B160},
      ddc          = {570},
      cid          = {I:(DE-He78)B160-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27048449},
      pmc          = {pmc:PMC4822319},
      doi          = {10.1186/s12915-016-0247-4},
      url          = {https://inrepo02.dkfz.de/record/130228},
}