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Structural basis of sensory receptor evolution in octopus
by
Valencia-Montoya, Wendy A.
, Hibbs, Ryan E.
, Kang, Guipeun
, Bellono, Nicholas W.
, Allard, Corey A. H.
, Kim, Jeong Joo
in
101/28
/ 631/181/735
/ 631/378/2586
/ 631/535/1258/1259
/ 631/57/2283
/ 64
/ 9/74
/ Acetylcholine receptors (nicotinic)
/ Adaptation
/ Animals
/ Binding Sites
/ Chemoreception
/ Cryoelectron Microscopy
/ Ecological adaptation
/ Electron microscopy
/ Evolution
/ Evolution, Molecular
/ Humanities and Social Sciences
/ Hydrophobic and Hydrophilic Interactions
/ Hydrophobicity
/ Ligands
/ Marine environment
/ Microscopy
/ multidisciplinary
/ Mutation
/ Neurotransmission
/ Neurotransmitter receptors
/ Neurotransmitters
/ Ocean floor
/ Octopodiformes - chemistry
/ Octopodiformes - physiology
/ Octopodiformes - ultrastructure
/ Octopuses
/ Permeability
/ Receptors
/ Receptors, Nicotinic - chemistry
/ Receptors, Nicotinic - physiology
/ Receptors, Nicotinic - ultrastructure
/ Science
/ Science & Technology - Other Topics
/ Science (multidisciplinary)
/ Sensation
/ Sensory Receptor Cells - chemistry
/ Sensory Receptor Cells - physiology
/ Sensory Receptor Cells - ultrastructure
/ Signal transduction
/ Synaptic Transmission
/ Touch - physiology
/ Transmission electron microscopy
2023
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Structural basis of sensory receptor evolution in octopus
by
Valencia-Montoya, Wendy A.
, Hibbs, Ryan E.
, Kang, Guipeun
, Bellono, Nicholas W.
, Allard, Corey A. H.
, Kim, Jeong Joo
in
101/28
/ 631/181/735
/ 631/378/2586
/ 631/535/1258/1259
/ 631/57/2283
/ 64
/ 9/74
/ Acetylcholine receptors (nicotinic)
/ Adaptation
/ Animals
/ Binding Sites
/ Chemoreception
/ Cryoelectron Microscopy
/ Ecological adaptation
/ Electron microscopy
/ Evolution
/ Evolution, Molecular
/ Humanities and Social Sciences
/ Hydrophobic and Hydrophilic Interactions
/ Hydrophobicity
/ Ligands
/ Marine environment
/ Microscopy
/ multidisciplinary
/ Mutation
/ Neurotransmission
/ Neurotransmitter receptors
/ Neurotransmitters
/ Ocean floor
/ Octopodiformes - chemistry
/ Octopodiformes - physiology
/ Octopodiformes - ultrastructure
/ Octopuses
/ Permeability
/ Receptors
/ Receptors, Nicotinic - chemistry
/ Receptors, Nicotinic - physiology
/ Receptors, Nicotinic - ultrastructure
/ Science
/ Science & Technology - Other Topics
/ Science (multidisciplinary)
/ Sensation
/ Sensory Receptor Cells - chemistry
/ Sensory Receptor Cells - physiology
/ Sensory Receptor Cells - ultrastructure
/ Signal transduction
/ Synaptic Transmission
/ Touch - physiology
/ Transmission electron microscopy
2023
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Structural basis of sensory receptor evolution in octopus
by
Valencia-Montoya, Wendy A.
, Hibbs, Ryan E.
, Kang, Guipeun
, Bellono, Nicholas W.
, Allard, Corey A. H.
, Kim, Jeong Joo
in
101/28
/ 631/181/735
/ 631/378/2586
/ 631/535/1258/1259
/ 631/57/2283
/ 64
/ 9/74
/ Acetylcholine receptors (nicotinic)
/ Adaptation
/ Animals
/ Binding Sites
/ Chemoreception
/ Cryoelectron Microscopy
/ Ecological adaptation
/ Electron microscopy
/ Evolution
/ Evolution, Molecular
/ Humanities and Social Sciences
/ Hydrophobic and Hydrophilic Interactions
/ Hydrophobicity
/ Ligands
/ Marine environment
/ Microscopy
/ multidisciplinary
/ Mutation
/ Neurotransmission
/ Neurotransmitter receptors
/ Neurotransmitters
/ Ocean floor
/ Octopodiformes - chemistry
/ Octopodiformes - physiology
/ Octopodiformes - ultrastructure
/ Octopuses
/ Permeability
/ Receptors
/ Receptors, Nicotinic - chemistry
/ Receptors, Nicotinic - physiology
/ Receptors, Nicotinic - ultrastructure
/ Science
/ Science & Technology - Other Topics
/ Science (multidisciplinary)
/ Sensation
/ Sensory Receptor Cells - chemistry
/ Sensory Receptor Cells - physiology
/ Sensory Receptor Cells - ultrastructure
/ Signal transduction
/ Synaptic Transmission
/ Touch - physiology
/ Transmission electron microscopy
2023
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Journal Article
Structural basis of sensory receptor evolution in octopus
2023
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Overview
Chemotactile receptors (CRs) are a cephalopod-specific innovation that allow octopuses to explore the seafloor via ‘taste by touch’
1
. CRs diverged from nicotinic acetylcholine receptors to mediate contact-dependent chemosensation of insoluble molecules that do not readily diffuse in marine environments. Here we exploit octopus CRs to probe the structural basis of sensory receptor evolution. We present the cryo-electron microscopy structure of an octopus CR and compare it with nicotinic receptors to determine features that enable environmental sensation versus neurotransmission. Evolutionary, structural and biophysical analyses show that the channel architecture involved in cation permeation and signal transduction is conserved. By contrast, the orthosteric ligand-binding site is subject to diversifying selection, thereby mediating the detection of new molecules. Serendipitous findings in the cryo-electron microscopy structure reveal that the octopus CR ligand-binding pocket is exceptionally hydrophobic, enabling sensation of greasy compounds versus the small polar molecules detected by canonical neurotransmitter receptors. These discoveries provide a structural framework for understanding connections between evolutionary adaptations at the atomic level and the emergence of new organismal behaviour.
Cryo-electron microscopy analyses reveal adaptations that facilitate the octopus chemotactile receptor’s evolutionary transition from an ancestral role in neurotransmission to detecting greasy environmental agonists for ‘taste by touch’ sensory behaviour.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 64
/ 9/74
/ Acetylcholine receptors (nicotinic)
/ Animals
/ Humanities and Social Sciences
/ Hydrophobic and Hydrophilic Interactions
/ Ligands
/ Mutation
/ Octopodiformes - ultrastructure
/ Receptors, Nicotinic - chemistry
/ Receptors, Nicotinic - physiology
/ Receptors, Nicotinic - ultrastructure
/ Science
/ Science & Technology - Other Topics
/ Sensory Receptor Cells - chemistry
/ Sensory Receptor Cells - physiology
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