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Single Molecule Tracking and Dynamics

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: closed (30 April 2024) | Viewed by 1912

Special Issue Editor


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Guest Editor
Department of Physics, New York Institute of Technology, Old Westbury, NY, USA
Interests: biophysics; microscopy; single molecule imaging

Special Issue Information

Dear Colleagues,

Please join me as we explore the latest developments in "Single Molecule Tracking and Dynamics". With this Special Issue, I encourage you to present the findings from your experimental, theoretical or computational research. Review articles that highlight recent developments and applications are also welcome. Although the foundations for many of the methods that enable single particle tracking and single molecule imaging are now well established, this area of research is remarkably vibrant. Advances in research on photoactivated proteins and permeable dyes have enabled applications to progress from imaging cell membranes to imaging intracellularly with single molecule sensitivity and specificity. Concomitant with these developments, optical instrumentation and methods that were once restricted to an individual's laboratory are now widely commercially available. This terrific progress has been highlighted by a series of recent Nobel Prizes, including the 2022 prize for developments and applications in click chemistry and bio-orthogonal chemistry. Furthermore, the advent of ubiquitous pattern recognition approaches has simplified the analysis of tracking results. These methods have reduced the number of experimental errors and significantly increased the confidence in analytical interpretation of acquired data. Since their inception, single molecule tracking approaches have enabled the verification of proposed models. Nevertheless, contemporary applications continue to push the boundaries and establish new frontiers.

Dr. Ben Ovryn
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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Published Papers (1 paper)

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Research

16 pages, 2376 KiB  
Article
Single-Molecule Imaging Reveals Differential AT1R Stoichiometry Change in Biased Signaling
by Gege Qin, Jiachao Xu, Yuxin Liang and Xiaohong Fang
Int. J. Mol. Sci. 2024, 25(1), 374; https://doi.org/10.3390/ijms25010374 - 27 Dec 2023
Cited by 2 | Viewed by 1606
Abstract
G protein-coupled receptors (GPCRs) represent promising therapeutic targets due to their involvement in numerous physiological processes mediated by downstream G protein- and β-arrestin-mediated signal transduction cascades. Although the precise control of GPCR signaling pathways is therapeutically valuable, the molecular details for governing biased [...] Read more.
G protein-coupled receptors (GPCRs) represent promising therapeutic targets due to their involvement in numerous physiological processes mediated by downstream G protein- and β-arrestin-mediated signal transduction cascades. Although the precise control of GPCR signaling pathways is therapeutically valuable, the molecular details for governing biased GPCR signaling remain elusive. The Angiotensin II type 1 receptor (AT1R), a prototypical class A GPCR with profound implications for cardiovascular functions, has become a focal point for biased ligand-based clinical interventions. Herein, we used single-molecule live-cell imaging techniques to evaluate the changes in stoichiometry and dynamics of AT1R with distinct biased ligand stimulations in real time. It was revealed that AT1R existed predominantly in monomers and dimers and underwent oligomerization upon ligand stimulation. Notably, β-arrestin-biased ligands induced the formation of higher-order aggregates, resulting in a slower diffusion profile for AT1R compared to G protein-biased ligands. Furthermore, we demonstrated that the augmented aggregation of AT1R, triggered by activation from each biased ligand, was completely abrogated in β-arrestin knockout cells. These findings furnish novel insights into the intricate relationship between GPCR aggregation states and biased signaling, underscoring the pivotal role of molecular behaviors in guiding the development of selective therapeutic agents. Full article
(This article belongs to the Special Issue Single Molecule Tracking and Dynamics)
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