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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
GPCR Desensitization01:12

GPCR Desensitization

G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical, 7TM, or...

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Related Experiment Video

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Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
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DVL as a scaffold protein capturing classical GPCRs.

Hagit Turm1, Sorina Grisaru-Granvosky, Myriam Maoz

  • 1Department of Oncology; Hadassah-Hebrew University Medical Center; Jerusalem, Israel.

Communicative & Integrative Biology
|February 19, 2011
PubMed
Summary
This summary is machine-generated.

Classical GPCRs can activate Wnt signaling protein dishevelled (DvL) to stabilize beta-catenin, independent of Wnt pathways. This DvL-Gα13 axis links GPCRs to beta-catenin stabilization in physiological and pathological invasion processes.

Keywords:
DVLGPCRGα13PAR1β-catenin

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Published on: January 20, 2015

Area of Science:

  • Cellular Biology
  • Molecular Signaling
  • Receptor Biology

Background:

  • G-protein-coupled receptors (GPCRs) are classical seven-transmembrane receptors (7TMRs) that signal via heterotrimeric G proteins.
  • Frizzleds (Fzs) are atypical 7TMRs activated by Wnts, crucial for development and cancer, but their GPCR classification is debated.
  • Canonical Wnt/β-catenin signaling involves β-catenin stabilization and nuclear translocation for gene transcription.

Purpose of the Study:

  • To investigate whether classical GPCRs can activate Wnt signaling components.
  • To determine the role of dishevelled (DvL) in mediating β-catenin stabilization downstream of GPCR activation.
  • To explore the involvement of the Gα13 subunit in this novel signaling axis.

Main Methods:

  • Activation of proteinase-activated receptor 1 (PAR(1)), a classical GPCR, in cellular models.
  • Assessment of β-catenin stabilization and its dependence on Wnt pathway components (Wnt, Fz, LRP5/6, SFRPs).
  • Co-immunoprecipitation to detect interactions between DvL and Gα13 subunits.
  • siRNA-mediated knockdown of LRP5/6 and DvL to assess their necessity.

Main Results:

  • PAR(1) activation recruits dishevelled (DvL), an upstream Wnt signaling protein, leading to β-catenin stabilization.
  • DvL selectively binds to the activated Gα13 subunit, forming a PAR(1)-induced DvL-Gα13 signaling axis.
  • This axis operates independently of Wnt ligands, Frizzled receptors, and LRP5/6 co-receptors.
  • PAR(1)-induced placental cytotrophoblast invasion was abrogated by siRNA-DvL but unaffected by Wnt inhibition.

Conclusions:

  • Dishevelled (DvL) acts as a central mediator, linking classical GPCRs to β-catenin stabilization.
  • The Gα13 subunit is crucial for mediating this GPCR-induced Wnt-independent signaling.
  • This pathway is relevant for both physiological processes (placental invasion) and pathological conditions (cancer).