GPCR Signalling Complexes – Synthesis, Assembly, Trafficking and Specificity

1. Front Matter

   Pages i-viii

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2. ER-Bound Steps in the Biosynthesis of G Protein-Coupled Receptors

   • Christian Nanoff, Michael Freissmuth

   Pages 1-21

3. Role of Chaperones in G Protein Coupled Receptor Signaling Complex Assembly

   • Denis J. Dupré, Maha M. Hammad, Patrick Holland, Jaime Wertman

   Pages 23-42

4. GPCR Oligomerization: Contribution to Receptor Biogenesis

   • Kathleen Van Craenenbroeck

   Pages 43-65

5. The Functional Size of GPCRs – Monomers, Dimers or Tetramers?

   • Darlaine Pétrin, Terence E. Hébert

   Pages 67-81

6. Regulation of Post-Golgi Traffic of G Protein-Coupled Receptors

   • Guangyu Wu

   Pages 83-95

7. Regulated GPCR Trafficking to the Plasma Membrane: General Issues and the CCR5 Chemokine Receptor Example

   • Hamasseh Shirvani, Gabriel Gätà, Stefano Marullo

   Pages 97-111

8. Regulatory Processes Governing the Cell Surface Expression of LH and FSH Receptors

   • Deborah L. Segaloff

   Pages 113-129

9. Chaperone-Mediated Assembly of G Protein Complexes

   • Barry M. Willardson, Christopher M. Tracy

   Pages 131-153

10. Synthesis and Assembly of G Protein βγ Dimers: Comparison of In Vitro and In Vivo Studies

    • Jane Dingus, John D. Hildebrandt

    Pages 155-180

11. Preferential Assembly of G-αβγ Complexes Directed by the γ Subunits

    • Janet D. Robishaw

    Pages 181-191

12. G Protein Trafficking

    • Philip B. Wedegaertner

    Pages 193-223

13. Differential Assembly of GPCR Signaling Complexes Determines Signaling Specificity

    • Pascal Maurice, Abla Benleulmi-Chaachoua, Ralf Jockers

    Pages 225-240

14. GPCR and Voltage-Gated Calcium Channels (VGCC) Signaling Complexes

    • Christophe Altier

    Pages 241-262

15. Pharmacological Chaperones Correct Misfolded GPCRs and Rescue Function: Protein Trafficking as a Therapeutic Target

    • Guadalupe Maya-Núñez, Alfredo Ulloa-Aguirre, Jo Ann Janovick, P. Michael Conn

    Pages 263-289

16. Back Matter

    Pages 291-299

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Main Question: G protein coupled receptors are involved in highly efficient and specific activation of signalling pathways. How do GPCR signalling complexes get assembled to generate such specificity? In order to answer this question, we need to understand how receptors and their signalling partners are synthesized, folded and quality-controlled in order to generate functional proteins. Then, we need to understand how each partner of the signalling complex is selected to join a complex, and what makes this assembly possible. GPCRs are known to be able to function as oligomers, what drives the assembly into oligomers and what will be the effects of such organization on specificity and efficacy of signal transduction. Once the receptor complexes are assembled, they need to reach different locations in the cell; what drives and controls the trafficking of GPCR signalling complexes. Finally, defects in synthesis, maturation or trafficking can alter functionality of GPCRs signalling complexes; how can we manipulate the system to make it function normally again? Pharmacological chaperones may just be part of the answer to this question.

• Assembly
• Chaperone
• G protein coupled receptor
• Signaling
• Trafficking
• Receptors

• Faculty of Medicine, Pharmacology, Dalhousie University, Halifax, Canada

  Denis J. Dupré

• , Pharmacology and Therapeutics, McGill University, Montreal, Canada

  Terence E. Hébert

• Institut Cochin, Paris, France

  Ralf Jockers

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