scholarly journals α-Conotoxins active at α3-containing nicotinic acetylcholine receptors and their molecular determinants for selective inhibition

2017 ◽  
Vol 175 (11) ◽  
pp. 1855-1868 ◽  
Author(s):  
Hartmut Cuny ◽  
Rilei Yu ◽  
Han-Shen Tae ◽  
Shiva N Kompella ◽  
David J Adams
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Selective Inhibition ◽  
Nicotinic Acetylcholine ◽  
Molecular Determinants

scholarly journals Molecular Determinants for Competitive Inhibition of α4β2 Nicotinic Acetylcholine Receptors

2010 ◽  
Vol 78 (3) ◽  
pp. 366-375 ◽  
Author(s):  
Patricio Iturriaga-Vásquez ◽  
Annalisa Carbone ◽  
Olimpo García-Beltrán ◽  
Phil D. Livingstone ◽  
Philip C. Biggin ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Competitive Inhibition ◽  
Nicotinic Acetylcholine ◽  
Molecular Determinants

scholarly journals An Inside Job: Molecular Determinants for Postsynaptic Localization of Nicotinic Acetylcholine Receptors

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3065
Author(s):  
Michael Ferns
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Adaptor Proteins ◽  
Scaffolding Proteins ◽  
Nicotinic Acetylcholine ◽  
Functional Studies ◽  
Molecular Determinants ◽  
Α3 Subunit ◽  
Cytoplasmic Loops ◽  
Intracellular Domains

Nicotinic acetylcholine receptors (nAChRs) mediate fast synaptic transmission at neuromuscular and autonomic ganglionic synapses in the peripheral nervous system. The postsynaptic localization of muscle ((α1)2β1γδ) and neuronal ((α3β4)2β4) nicotinic receptors at these synapses is mediated by interactions between the nAChR intracellular domains and cytoplasmic scaffolding proteins. Recent high resolution structures and functional studies provide new insights into the molecular determinants that mediate these interactions. Surprisingly, they reveal that the muscle nAChR binds 1–3 rapsyn scaffolding molecules, which dimerize and thereby form an interconnected lattice between receptors. Moreover, rapsyn binds two distinct sites on the nAChR subunit cytoplasmic loops; the MA-helix on one or more subunits and a motif specific to the β subunit. Binding at the latter site is regulated by agrin-induced phosphorylation of βY390, and increases the stoichiometry of rapsyn/AChR complexes. Similarly, the neuronal nAChR may be localized at ganglionic synapses by phosphorylation-dependent interactions with 14-3-3 adaptor proteins which bind specific motifs in each of the α3 subunit cytoplasmic loops. Thus, postsynaptic localization of nAChRs is mediated by regulated interactions with multiple scaffolding molecules, and the stoichiometry of these complexes likely helps regulate the number, density, and stability of receptors at the synapse.

scholarly journals Molecular Determinants of α3β4 Nicotinic Acetylcholine Receptors Inhibition by Triterpenoids

2018 ◽  
Vol 41 (1) ◽  
pp. 65-72 ◽  
Author(s):  
Sanung Eom ◽  
Yoon Suh Kim ◽  
Sung Bae Lee ◽  
Shinhwa Noh ◽  
Hye Duck Yeom ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Nicotinic Acetylcholine ◽  
Molecular Determinants

Nicotinic acetylcholine receptors in the patients with Parkinson's disease: 5IA-SPECT

2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S586-S586 ◽  
Author(s):  
Kazuo Hashikawa ◽  
Hidefumi Yoshida ◽  
Nobukatsu Sawamoto ◽  
Shigetoshi Takaya ◽  
Chihiro Namiki ◽  
...  
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Nicotinic Acetylcholine
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