Structure of an endosomal signaling GPCR-G protein-β-arrestin megacomplex.

Animals Cattle Cryoelectron Microscopy Endosomes / metabolism GTP-Binding Proteins / chemistry Humans Models, Molecular Protein Conformation Receptors, Adrenergic, beta-2 / chemistry Receptors, G-Protein-Coupled / chemistry Receptors, Vasopressin / chemistry Signal Transduction beta-Arrestins / chemistry

Journal

Nature structural & molecular biology
ISSN: 1545-9985
Titre abrégé: Nat Struct Mol Biol
Pays: United States
ID NLM: 101186374

Informations de publication

Date de publication:
12 2019
Historique:
received: 10 08 2019
accepted: 09 10 2019
pubmed: 20 11 2019
medline: 26 2 2020
entrez: 20 11 2019
Statut: ppublish

Résumé

Classically, 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 β

Identifiants

DOI: 10.1038/s41594-019-0330-y PMID: 31740855 PMC: PMC7108872
pubmed: 31740855
doi: 10.1038/s41594-019-0330-y
pii: 10.1038/s41594-019-0330-y
pmc: PMC7108872
mid: NIHMS1541120
doi:

Substances chimiques

AVPR2 protein, human 0
Receptors, Adrenergic, beta-2 0
Receptors, G-Protein-Coupled 0
Receptors, Vasopressin 0
beta-Arrestins 0
GTP-Binding Proteins EC 3.6.1.-

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1123-1131

Subventions

Organisme : NIGMS NIH HHS
ID : R35 GM133598
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007767
Pays : United States
Organisme : NCRR NIH HHS
ID : P41 RR001209
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL016037
Pays : United States
Organisme : NHLBI NIH HHS
ID : F30 HL149213
Pays : United States
Organisme : NIH HHS
ID : S10 OD019994
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007171
Pays : United States
Organisme : NHLBI NIH HHS
ID : F30 HL129803
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM103310
Pays : United States

Références

Reiter, E., Ahn, S., Shukla, A. K. & Lefkowitz, R. J. Molecular mechanism of beta-arrestin-biased agonism at seven-transmembrane receptors. Annu. Rev. Pharmacol. Toxicol. 52, 179–197 (2012).
pubmed: 21942629 doi: 10.1146/annurev.pharmtox.010909.105800
Lefkowitz, R. J., Stadel, J. M. & Caron, M. G. Adenylate cyclase-coupled beta-adrenergic receptors: structure and mechanisms of activation and desensitization. Annu. Rev. Biochem. 52, 159–186 (1983).
pubmed: 6137187 doi: 10.1146/annurev.bi.52.070183.001111
Rajagopal, S., Rajagopal, K. & Lefkowitz, R. J. Teaching old receptors new tricks: biasing seven-transmembrane receptors. Nat. Rev. Drug Discov. 9, 373–386 (2010).
pubmed: 20431569 pmcid: 2902265 doi: 10.1038/nrd3024
Oakley, R. H., Laporte, S. A., Holt, J. A., Barak, L. S. & Caron, M. G. Association of beta-arrestin with G protein-coupled receptors during clathrin-mediated endocytosis dictates the profile of receptor resensitization. J. Biol. Chem. 274, 32248–32257 (1999).
pubmed: 10542263 doi: 10.1074/jbc.274.45.32248
Oakley, R. H., Laporte, S. A., Holt, J. A., Caron, M. G. & Barak, L. S. Differential affinities of visual arrestin, beta arrestin1, and beta arrestin2 for G protein-coupled receptors delineate two major classes of receptors. J. Biol. Chem. 275, 17201–17210 (2000).
pubmed: 10748214 doi: 10.1074/jbc.M910348199
Calebiro, D. et al. Persistent cAMP-signals triggered by internalized G-protein-coupled receptors. PLoS Biol. 7, e1000172 (2009).
pubmed: 19688034 pmcid: 2718703 doi: 10.1371/journal.pbio.1000172
Ferrandon, S. et al. Sustained cyclic AMP production by parathyroid hormone receptor endocytosis. Nat. Chem. Biol. 5, 734–742 (2009).
pubmed: 19701185 pmcid: 3032084 doi: 10.1038/nchembio.206
Feinstein, T. N. et al. Noncanonical control of vasopressin receptor type 2 signaling by retromer and arrestin. J. Biol. Chem. 288, 27849–27860 (2013).
pubmed: 23935101 pmcid: 3784700 doi: 10.1074/jbc.M112.445098
Thomsen, A. R. B. et al. GPCR-G Protein-beta-Arrestin Super-Complex Mediates Sustained G Protein Signaling. Cell 166, 907–919 (2016).
pubmed: 27499021 pmcid: 5418658 doi: 10.1016/j.cell.2016.07.004
Shukla, A. K. et al. Visualization of arrestin recruitment by a G-protein-coupled receptor. Nature 512, 218–222 (2014).
pubmed: 25043026 pmcid: 4134437 doi: 10.1038/nature13430
Cahill, T. J. 3rd et al. Distinct conformations of GPCR-beta-arrestin complexes mediate desensitization, signaling, and endocytosis. Proc. Natl Acad. Sci. USA 114, 2562–2567 (2017).
pubmed: 28223524 pmcid: 5347553 doi: 10.1073/pnas.1701529114
Wehbi, V. L. et al. Noncanonical GPCR signaling arising from a PTH receptor-arrestin-Gbetagamma complex. Proc. Natl Acad. Sci. USA 110, 1530–1535 (2013).
pubmed: 23297229 pmcid: 3557057 doi: 10.1073/pnas.1205756110
Jimenez-Vargas, N. N. et al. Protease-activated receptor-2 in endosomes signals persistent pain of irritable bowel syndrome. Proc. Natl Acad. Sci. USA 115, E7438–E7447 (2018).
pubmed: 30012612 pmcid: 6077730 doi: 10.1073/pnas.1721891115
Wanka, L., Babilon, S., Kaiser, A., Morl, K. & Beck-Sickinger, A. G. Different mode of arrestin-3 binding at the human Y1 and Y2 receptor. Cell Signal 50, 58–71 (2018).
pubmed: 29944985 doi: 10.1016/j.cellsig.2018.06.010
Rasmussen, S. G. et al. Crystal structure of the beta2 adrenergic receptor-Gs protein complex. Nature 477, 549–555 (2011).
pubmed: 21772288 pmcid: 3184188 doi: 10.1038/nature10361
Cherezov, V. et al. High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science 318, 1258–1265 (2007).
pubmed: 17962520 pmcid: 2583103 doi: 10.1126/science.1150577
Ballesteros, J. A. & Weinstein. H. in Methods in Neurosciences Vol. 25 (ed. Sealfon, S. C.) 366–428 (Elsevier, 1995).
Ring, A. M. et al. Adrenaline-activated structure of beta2-adrenoceptor stabilized by an engineered nanobody. Nature 502, 575–579 (2013).
pubmed: 24056936 pmcid: 3822040 doi: 10.1038/nature12572
Rasmussen, S. G. et al. Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor. Nature 469, 175–180 (2011).
pubmed: 21228869 pmcid: 3058308 doi: 10.1038/nature09648
Shukla, A. K. et al. Structure of active beta-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide. Nature 497, 137–141 (2013).
pubmed: 23604254 pmcid: 3654799 doi: 10.1038/nature12120
Fredericks, Z. L., Pitcher, J. A. & Lefkowitz, R. J. Identification of the G protein-coupled receptor kinase phosphorylation sites in the human beta2-adrenergic receptor. J. Biol. Chem. 271, 13796–13803 (1996).
pubmed: 8662852 doi: 10.1074/jbc.271.23.13796
Lally, C. C., Bauer, B., Selent, J. & Sommer, M. E. C-edge loops of arrestin function as a membrane anchor. Nat. Commun. 8, 14258 (2017).
pubmed: 28220785 pmcid: 5321764 doi: 10.1038/ncomms14258
Zhou, X. E. et al. Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors. Cell 170, 457–469 (2017). e13.
pubmed: 28753425 pmcid: 5567868 doi: 10.1016/j.cell.2017.07.002
Lohse, M. J., Benovic, J. L., Codina, J., Caron, M. G. & Lefkowitz, R. J. beta-Arrestin: a protein that regulates beta-adrenergic receptor function. Science 248, 1547–1550 (1990).
pubmed: 2163110 doi: 10.1126/science.2163110
Lohse, M. J. et al. Receptor-specific desensitization with purified proteins. Kinase dependence and receptor specificity of beta-arrestin and arrestin in the beta 2-adrenergic receptor and rhodopsin systems. J. Biol. Chem. 267, 8558–8564 (1992).
pubmed: 1349018 doi: 10.1016/S0021-9258(18)42479-9
Kang, Y. et al. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature 523, 561–567 (2015).
pubmed: 26200343 pmcid: 4521999 doi: 10.1038/nature14656
Liang, Y. L. et al. Phase-plate cryo-EM structure of a class B GPCR-G-protein complex. Nature 546, 118–123 (2017).
pubmed: 28437792 pmcid: 5832441 doi: 10.1038/nature22327
Zhang, Y. et al. Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein. Nature 546, 248–253 (2017).
pubmed: 28538729 pmcid: 5587415 doi: 10.1038/nature22394
Le Gouill, C., Innamorati, G. & Birnbaumer, M. An expanded V2 receptor retention signal. FEBS Lett. 532, 363–366 (2002).
pubmed: 12482593 doi: 10.1016/S0014-5793(02)03709-2
Innamorati, G., Sadeghi, H. M., Tran, N. T. & Birnbaumer, M. A serine cluster prevents recycling of the V2 vasopressin receptor. Proc. Natl Acad. Sci. USA 95, 2222–2226 (1998).
pubmed: 9482866 pmcid: 19299 doi: 10.1073/pnas.95.5.2222
Mayer, D. et al. Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation. Nat. Commun. 10, 1261 (2019).
pubmed: 30890705 pmcid: 6424980 doi: 10.1038/s41467-019-09204-y
Liang, Y. L. et al. Cryo-EM structure of the active, Gs-protein complexed, human CGRP receptor. Nature 561, 492–497 (2018).
pubmed: 30209400 pmcid: 6166790 doi: 10.1038/s41586-018-0535-y
Liang, Y. L. et al. Phase-plate cryo-EM structure of a biased agonist-bound human GLP-1 receptor-Gs complex. Nature 555, 121–125 (2018).
pubmed: 29466332 doi: 10.1038/nature25773
Irannejad, R. et al. Conformational biosensors reveal GPCR signalling from endosomes. Nature 495, 534–538 (2013).
pubmed: 23515162 doi: 10.1038/nature12000
Yang, M., He, R. L., Benovic, J. L. & Ye, R. D. beta-Arrestin1 interacts with the G-protein subunits beta1gamma2 and promotes beta1gamma2-dependent Akt signalling for NF-kappaB activation. Biochem. J. 417, 287–296 (2009).
pubmed: 18729826 doi: 10.1042/BJ20081561
Gaudet, R., Bohm, A. & Sigler, P. B. Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin. Cell 87, 577–588 (1996).
pubmed: 8898209 doi: 10.1016/S0092-8674(00)81376-8
Lodowski, D. T., Pitcher, J. A., Capel, W. D., Lefkowitz, R. J. & Tesmer, J. J. Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma. Science 300, 1256–1262 (2003).
pubmed: 12764189 doi: 10.1126/science.1082348
Whorton, M. R. & MacKinnon, R. X-ray structure of the mammalian GIRK2-betagamma G-protein complex. Nature 498, 190–197 (2013).
pubmed: 23739333 pmcid: 4654628 doi: 10.1038/nature12241
Noble, A. J. et al. Routine single particle CryoEM sample and grid characterization by tomography. eLife 7, e34257 (2018).
pubmed: 29809143 pmcid: 5999397 doi: 10.7554/eLife.34257
Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36–51 (2005).
pubmed: 16182563 doi: 10.1016/j.jsb.2005.07.007
Tan, Y. Z. et al. Addressing preferred specimen orientation in single-particle cryo-EM through tilting. Nat. Methods 14, 793–796 (2017).
pubmed: 28671674 pmcid: 5533649 doi: 10.1038/nmeth.4347
Suloway, C. et al. Automated molecular microscopy: the new Leginon system. J. Struct. Biol. 151, 41–60 (2005).
pubmed: 15890530 doi: 10.1016/j.jsb.2005.03.010
Tegunov, D. & Cramer, P. Real-time cryo-electron microscopy data preprocessing with Warp. Nat. Methods 16, 1146–1152 (2019).
pubmed: 31591575 pmcid: 6858868 doi: 10.1038/s41592-019-0580-y
Zivanov, J. et al. New tools for automated high-resolution cryo-EM structure determination in RELION-3. eLife 7, e42166 (2018).
pubmed: 30412051 pmcid: 6250425 doi: 10.7554/eLife.42166
Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290–296 (2017).
pubmed: 28165473 doi: 10.1038/nmeth.4169
Vilas, J. L. et al. MonoRes: Automatic and Accurate Estimation of Local Resolution for Electron Microscopy Maps. Structure 26, 337–344 (2018). e4.
pubmed: 29395788 doi: 10.1016/j.str.2017.12.018
Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 6, 213–221 (2010).
doi: 10.1107/S0907444909052925
Roy, A., Kucukural, A. & Zhang, Y. I-TASSER: a unified platform for automated protein structure and function prediction. Nat. Protoc. 5, 725–738 (2010).
pubmed: 20360767 pmcid: 2849174 doi: 10.1038/nprot.2010.5
Pettersen, E. F. et al. UCSF Chimera–a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004).
pubmed: 15264254 doi: 10.1002/jcc.20084
Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D Biol. Crystallogr. 66, 486–501 (2010).
pubmed: 20383002 pmcid: 2852313 doi: 10.1107/S0907444910007493
Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66, 12–21 (2010).
pubmed: 20057044 doi: 10.1107/S0907444909042073
Goddard, T. D. et al. UCSF ChimeraX: Meeting modern challenges in visualization and analysis. Protein Sci. 27, 14–25 (2018).
pubmed: 28710774 doi: 10.1002/pro.3235
Marrink, S. J. & Mark, A. E. Molecular view of hexagonal phase formation in phospholipid membranes. Biophys. J. 87, 3894–3900 (2004).
pubmed: 15377528 pmcid: 1304900 doi: 10.1529/biophysj.104.048710
Jo, S., Kim, T., Iyer, V. G. & Im, W. CHARMM-GUI: a web-based graphical user interface for CHARMM. J. Comput. Chem. 29, 1859–1865 (2008).
pubmed: 18351591 doi: 10.1002/jcc.20945
Pronk, S. et al. GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics 29, 845–854 (2013).
pubmed: 23407358 pmcid: 3605599 doi: 10.1093/bioinformatics/btt055
Humphrey, W., Dalke, A. & Schulten, K. VMD: visual molecular dynamics. J. Mol. Graph. 14, 27–28 (1996).
doi: 10.1016/0263-7855(96)00018-5
Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V. & Mann, M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856–2860 (2006).
pubmed: 17406544 doi: 10.1038/nprot.2006.468
Cox, J. & Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367–1372 (2008).
pubmed: 19029910 doi: 10.1038/nbt.1511
Olsen, J. V. & Mann, M. Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation. Proc. Natl Acad. Sci. USA 101, 13417–13422 (2004).
pubmed: 15347803 pmcid: 518757 doi: 10.1073/pnas.0405549101
MacLean, B. et al. Skyline: an open source document editor for creating and analyzing targeted proteomics experiments. Bioinformatics 26, 966–968 (2010).
pubmed: 20147306 pmcid: 2844992 doi: 10.1093/bioinformatics/btq054

Auteurs

Anthony H Nguyen (AH)

Department of Medicine, Duke University Medical Center, Durham, NC, USA.
Department of Biochemistry, Duke University Medical Center, Durham, NC, USA.

Alex R B Thomsen (ARB)

Department of Medicine, Duke University Medical Center, Durham, NC, USA.
Department of Surgery, Columbia University Irving Medical Center, New York, NY, USA.

Thomas J Cahill (TJ)

Department of Medicine, Duke University Medical Center, Durham, NC, USA.
Department of Biochemistry, Duke University Medical Center, Durham, NC, USA.

Rick Huang (R)

Howard Hughes Medical Institute, Janelia Research Campus, Ashburn, VA, USA.

Li-Yin Huang (LY)

Department of Medicine, Duke University Medical Center, Durham, NC, USA.

Tara Marcink (T)

Department of Pediatrics, Columbia University Irving Medical Center, New York, NY, USA.
Center for Host-Pathogen Interaction, Columbia University Irving Medical Center, New York, NY, USA.

Oliver B Clarke (OB)

Department of Anesthesiology, Columbia University Irving Medical Center, New York, NY, USA.
Department of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY, USA.
The Irving Center for Clinical and Translational Research, Columbia University Irving Medical Center, New York, NY, USA.

Søren Heissel (S)

Proteomics Resource Center, The Rockefeller University, New York, NY, USA.

Ali Masoudi (A)

Department of Medicine, Duke University Medical Center, Durham, NC, USA.

Danya Ben-Hail (D)

Structural Biology Initiative, CUNY Advanced Science Research Center, New York, NY, USA.

Fadi Samaan (F)

Structural Biology Initiative, CUNY Advanced Science Research Center, New York, NY, USA.

Venkata P Dandey (VP)

The National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, USA.

Yong Zi Tan (YZ)

The National Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center, New York, NY, USA.
Department of Biochemistry and Molecular Biophysics, Columbia University Irving Medical Center, New York, NY, USA.

Chuan Hong (C)

Howard Hughes Medical Institute, Janelia Research Campus, Ashburn, VA, USA.

Jacob P Mahoney (JP)

Department of Pharmacology, University of Michigan, Ann Arbor, MI, USA.
Department of Structural Biology, Stanford University, Stanford, CA, USA.

Sarah Triest (S)

Structural Biology Brussels, Vrije Universiteit Brussels, Brussels, Belgium.
Structural Biology Research Center, Vlaams Instituut voor Biotechnologie, Brussels, Belgium.

John Little (J)

Department of Biochemistry, Duke University Medical Center, Durham, NC, USA.
ORCID: 0000-0003-2034-2684

Xin Chen (X)

School of Pharmaceutical Engineering and Life Sciences, Changzhou University, Changzhou, China.

Roger Sunahara (R)

Department of Pharmacology, University of Michigan, Ann Arbor, MI, USA.
Department of Pharmacology, University of California, San Diego, La Jolla, CA, USA.
ORCID: 0000-0003-1702-8619

Jan Steyaert (J)

Structural Biology Brussels, Vrije Universiteit Brussels, Brussels, Belgium.

Henrik Molina (H)

Proteomics Resource Center, The Rockefeller University, New York, NY, USA.

Zhiheng Yu (Z)

Howard Hughes Medical Institute, Janelia Research Campus, Ashburn, VA, USA.

Amedee des Georges (A)

Structural Biology Initiative, CUNY Advanced Science Research Center, New York, NY, USA. adesgeorges@gc.cuny.edu.
Department of Chemistry and Biochemistry, City College of New York, New York, NY, USA. adesgeorges@gc.cuny.edu.
Biochemistry and Chemistry PhD Programs, Graduate Center, City University of New York, New York, NY, USA. adesgeorges@gc.cuny.edu.
ORCID: 0000-0002-9704-3781

Robert J Lefkowitz (RJ)

Department of Medicine, Duke University Medical Center, Durham, NC, USA. lefko001@receptor-biol.duke.edu.
Department of Biochemistry, Duke University Medical Center, Durham, NC, USA. lefko001@receptor-biol.duke.edu.
Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC, USA. lefko001@receptor-biol.duke.edu.
ORCID: 0000-0003-1472-7545

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Structure of an endosomal signaling GPCR-G...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Artiodactyla › Ruminants › Bovins › Structure of an endosomal signaling GPCR-G...
questionsmedicales.fr › Techniques d'investigation › Microscopie électronique › Cryomicroscopie électronique › Structure of an endosomal signaling GPCR-G...
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Vésicules cytoplasmiques › Vésicules de transport › Endosomes › Structure of an endosomal signaling GPCR-G...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines G › Structure of an endosomal signaling GPCR-G...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Structure of an endosomal signaling GPCR-G...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › Structure of an endosomal signaling GPCR-G...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure of an endosomal signaling GPCR-G...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Récepteurs de surface cellulaire › Récepteurs aux neuromédiateurs › Récepteurs catécholaminergiques › Récepteurs adrénergiques › Récepteurs bêta-adrénergiques › Récepteurs bêta-2 adrénergiques › Structure of an endosomal signaling GPCR-G...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Récepteurs de surface cellulaire › Récepteurs couplés aux protéines G › Structure of an endosomal signaling GPCR-G...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Récepteurs de surface cellulaire › Récepteurs peptidiques › Récepteur hormone hypophysaire › Récepteurs à la vasopressine › Structure of an endosomal signaling GPCR-G...
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Transduction du signal › Structure of an endosomal signaling GPCR-G...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Arrestines › bêta-Arrestines › Structure of an endosomal signaling GPCR-G...