Muscarinic receptor family interacting proteins: Role in receptor function

Borroto-Escuela, Dasiel O.; Correia, Patrícia A.; Romero-Fernández, Wilber; Narváez, Manuel; Fuxé, Kjell; Ciruela, Francisco; Garriga, Pere

doi:10.1016/j.jneumeth.2010.11.025

Cited by 24 publications

(33 citation statements)

References 30 publications

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“…dephosphorylates the M3-MR, per se, a recent study indicates the binding of both SET and PP2A to the third intracellular loop of selected muscarinic receptor subtypes (Borroto-Escuela et al, 2011). Although not reported for all subtypes, the interaction of SET with the M1 muscarinic receptor was dependent on agonist activation, whereas the interaction with PP2A was independent of agonist binding.…”

Section: Discussionmentioning

confidence: 96%

Influence of the Accessory Protein SET on M3 Muscarinic Receptor Phosphorylation and G Protein Coupling

Simon¹,

Öner²,

Cohen‐Tannoudji³

et al. 2012

Mol Pharmacol

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Section: Discussionmentioning

confidence: 96%

Influence of the Accessory Protein SET on M3 Muscarinic Receptor Phosphorylation and G Protein Coupling

Simon¹,

Öner²,

Cohen‐Tannoudji³

et al. 2012

Mol Pharmacol

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“…So far the work on receptor-receptor interactions and receptor-protein interactions has mainly been performed in parallel in view of the complexities of the interactions. Overall, GIPs by impinging on the GPCR trafficking, localization and/or pharmacological properties, play a prominent role in GPCR biology including learning and memory (see below) since they fine-tune the receptor functioning [60][61][62].…”

Section: Gpcr Interacting Proteins and Their Receptor-protein Interacmentioning

confidence: 99%

Receptor-receptor interactions in heteroreceptor complexes: a new principle in biology. Focus on their role in learning and memory

Fuxé

Borroto‐Escuela²,

Ciruela³

et al. 2014

Neurosci Discov

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The allosteric receptor-receptor interactions over the interfaces in heteroreceptor complexes have been explored and their biochemical, pharmacological and functional integrative implications in the Central Nervous System (CNS) described. GPCR interacting proteins participate in these complexes mainly through modulation of receptor-receptor interactions. Methodologies to study heteroreceptor complexes in living cells (FRET and BRET-based techniques) and in brain tissue (in situ proximity ligation assay) are briefly summarized. The physiological and pathological relevance of the allosteric receptor-receptor interactions in heteroreceptor complexes is emphasized and novel strategies for treatment of mental and neurological disease are developed based on this new biological principle of integration. The molecular basis of learning and memory is proposed to be based on the reorganization of the homo-and heteroreceptor complexes in the postjunctional membrane of synapses leading also to changes in the prejunctional receptor complexes to facilitate the pattern of transmitter release to be learned. Long-term memory may be created by the transformation of parts of the heteroreceptor complexes into unique transcription factors which can lead to the formation of specific adapter proteins which can consolidate the heteroreceptor complexes into long-lived complexes with conserved allosteric receptor-receptor interactions.

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“…In the case of M2-M3 heteromers also covalent interactions exist namely a disulfide crosslink between extracellular loops besides the non-covalent interaction name represented by electrostatic and hydrophobic bonds [27].…”

Section: On the Receptor Interface In Gpcr Hetero-mersmentioning

confidence: 99%

GPCR Heteromers and their Allosteric Receptor-Receptor Interactions

Fuxé

Marcellino

Romero-Fernández

et al. 2012

CMC

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The concept of intramembrane receptor-receptor interactions and evidence for their existences were introduced in the beginning of the 1980's, suggesting the existence of receptor heterodimerization. The discovery of GPCR heteromers and the receptor mosaic (higher order oligomers, more than two) has been related to the parallel development and application of a variety of resonance energy transfer techniques such as bioluminescence (BRET), fluorescence (FRET) and sequential energy transfer (SRET). The assembly of interacting GPCRs, heterodimers and receptor mosaic leads to changes in the agonist recognition, signaling, and trafficking of participating receptors via allosteric mechanisms, sometimes involving the appearance of cooperativity. The receptor interface in the GPCR heteromers is beginning to be characterized and the key role of electrostatic epitope-epitope interactions for the formation of the receptor heteromers will be discussed. Furthermore, a "guide-and-clasp" manner of receptor-receptor interactions has been proposed where the "adhesive guides" may be the triplet homologies. These interactions probably represent a general molecular mechanism for receptor-receptor interactions. It is proposed that changes in GPCR function (moonlighting) may develop through the intracellular loops and C-terminii of the GPCR heteromers as a result of dynamic allosteric interactions between different types of G proteins and other receptor interacting proteins in these domains of the receptors. The evidence for the existence of receptor heteromers opens up a new field for a better understanding of neurophysiology and neuropathology. Furthermore, novel therapeutic approaches could be possible based on the use of heteromers as targets for drug development based on their unique pharmacology.

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Muscarinic receptor family interacting proteins: Role in receptor function

Cited by 24 publications

References 30 publications

Influence of the Accessory Protein SET on M3 Muscarinic Receptor Phosphorylation and G Protein Coupling

Influence of the Accessory Protein SET on M3 Muscarinic Receptor Phosphorylation and G Protein Coupling

Receptor-receptor interactions in heteroreceptor complexes: a new principle in biology. Focus on their role in learning and memory

GPCR Heteromers and their Allosteric Receptor-Receptor Interactions

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