Studying the rhodopsin‐like G protein‐coupled receptors by atomic force microscopy

Rhodopsin‐like G protein‐coupled receptors (GPCRs), widely distributed in microorganisms, invertebrates, and vertebrates, are the largest class in GPCRs, and are involved in many important physiological and pathological processes, including the photosensitivity, regulation of behavior and emotion, a...

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Bibliographic Details
Published in:Cytoskeleton (Hoboken, N.J.) N.J.), 2021-08, Vol.78 (8), p.400-416
Main Authors: Fang, Bin, Zhao, Li, Du, Xiaowei, Liu, Qiyuan, Yang, Hui, Li, Fangzuo, Sheng, Yaohuan, Zhao, Weidong, Zhong, Haijian
Format: Article
Language:English
Subjects:
AFM
Animals
Atomic force microscopy
GPCRs
Mechanical properties
Membrane proteins
Membrane Proteins - metabolism
Microscopy
Microscopy, Atomic Force
Photosensitivity
Physiology
Receptors, G-Protein-Coupled - chemistry
Rhodopsin
Rhodopsin - chemistry
Rhodopsin - metabolism
SMFS
Spatial discrimination
Spectroscopy
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Summary:Rhodopsin‐like G protein‐coupled receptors (GPCRs), widely distributed in microorganisms, invertebrates, and vertebrates, are the largest class in GPCRs, and are involved in many important physiological and pathological processes, including the photosensitivity, regulation of behavior and emotion, and so on. Atomic force microscopy (AFM) is a powerful and multifunctional toolkit in bionanotechnology, as it can image the morphology of membrane proteins at subnanometer spatial resolution and detect forces related with membrane proteins down to piconewton level by single‐molecule force spectroscopy (SMFS) mode under physiological conditions. Herein, the achievements of AFM in the study of rhodopsin‐like GPCRs, including observing the high‐resolution topography and structural changes, revealing the interaction forces, binding kinetics, and mechanical properties (such as modulus), are reviewed and summarized. Finally, the challenges, outlook, and prospects of AFM in the study of rhodopsin‐like GPCRs are discussed.
ISSN:1949-3584
1949-3592
DOI:10.1002/cm.21692