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Biomolecules
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Actin and Its Associates: Biophysical Aspects in Functional Roles
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Actin and Its Associates: Biophysical Aspects in Functional Roles

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: closed (30 November 2023) | Viewed by 21489

Special Issue Editors

Prof. Dr. Hans Georg Mannherz

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Guest Editor
Department of Anatomy and Molecular Embryology, Medical Faculty, Ruhr-University Bochum, D-44780 Bochum, Germany
Interests: actin related protein 2-3 complex; actin depolymerizing factors; microfilaments
Prof. Dr. Brigitte M. Jockusch

E-Mail Website
Guest Editor
Biosciences, Technical University of Braunschweig, BRICS, 38092 Braunschweig, Germany
Interests: actin and associated proteins cooperating in cell anchorage, cell motility, cell-cell-interactions, tissue generation, in health and disease
Dr. Beáta Bugyi

E-Mail Website
Guest Editor
Department of Biophysics, Medical School, University of Pécs, Szigeti str. 12, H-7624 Pécs, Hungary
Interests: actin cytoskeleton; actin-binding proteins; actin structure and dynamics; functional polymorphism of actin; actin-microtubule crosstalk

Special Issue Information

Dear Colleagues,

Actin, a ubiquitous cellular protein, is vital to a multitude of cell functions relying on force generation and transduction such as cellular motility, transport and division, cell shaping and polarity. Within the cohesive structure of the actin cytoskeleton, helical polymers assembled from actin monomers self-organize into higher-order networks with diverse structural, dynamic, and mechanical properties fine-tuned by an inventory of actin-binding proteins. These distinct assemblies serve specialized roles in cell response and behavior. Significant advances have been made to unravel how the functional polymorphism of the actin cytoskeleton emerges from actin’s intrinsic physicochemical features. However, challenges remain in the understanding of the mechanisms coupling the molecular pattern of actin networks with their biomechanical and functional behavior. In this Special Issue of Biomolecules, original research publications are invited that cover the recent advances related to the biophysical principles governing the architecture, dynamics, and function of actin polymers and networks either isolated in solution or in the cellular environment. The Special Issue is also a place for review articles summarizing the existing knowledge on the mechanical aspects and regulation of actin homeostasis in health and disease.

Prof. Dr. Hans Georg Mannherz
Prof. Dr. Brigitte M. Jockusch
Dr. Beáta Bugyi
Guest Editors

Manuscript Submission Information

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • actin isoforms and mutations
  • actin cytoskeleton
  • actin-binding proteins
  • actin dynamics
  • self-organization
  • polymer mechanics
  • biophysical and cell biological approaches and biomedical con sequences

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Published Papers (6 papers)

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Research

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14 pages, 2733 KiB  
Article
Molecular Basis for Actin Polymerization Kinetics Modulated by Solution Crowding
by Bryan Demosthene, Myeongsang Lee, Ryan R. Marracino, James B. Heidings and Ellen Hyeran Kang
Biomolecules 2023, 13(5), 786; https://doi.org/10.3390/biom13050786 - 2 May 2023
Cited by 3 | Viewed by 2566
Abstract
Actin polymerization drives cell movement and provides cells with structural integrity. Intracellular environments contain high concentrations of solutes, including organic compounds, macromolecules, and proteins. Macromolecular crowding has been shown to affect actin filament stability and bulk polymerization kinetics. However, the molecular mechanisms behind [...] Read more.
Actin polymerization drives cell movement and provides cells with structural integrity. Intracellular environments contain high concentrations of solutes, including organic compounds, macromolecules, and proteins. Macromolecular crowding has been shown to affect actin filament stability and bulk polymerization kinetics. However, the molecular mechanisms behind how crowding influences individual actin filament assembly are not well understood. In this study, we investigated how crowding modulates filament assembly kinetics using total internal reflection fluorescence (TIRF) microscopy imaging and pyrene fluorescence assays. The elongation rates of individual actin filaments analyzed from TIRF imaging depended on the type of crowding agent (polyethylene glycol, bovine serum albumin, and sucrose) as well as their concentrations. Further, we utilized all-atom molecular dynamics (MD) simulations to evaluate the effects of crowding molecules on the diffusion of actin monomers during filament assembly. Taken together, our data suggest that solution crowding can regulate actin assembly kinetics at the molecular level. Full article
(This article belongs to the Special Issue Actin and Its Associates: Biophysical Aspects in Functional Roles)
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14 pages, 2997 KiB  
Article
Spatiotemporal Regulation of FMNL2 by N-Terminal Myristoylation and C-Terminal Phosphorylation Drives Rapid Filopodia Formation
by Lina Lorenzen, Dennis Frank, Carsten Schwan and Robert Grosse
Biomolecules 2023, 13(3), 548; https://doi.org/10.3390/biom13030548 - 17 Mar 2023
Cited by 4 | Viewed by 2142
Abstract
The actin nucleating and polymerizing formin-like 2 (FMNL2) is upregulated in several cancers and has been shown to play important roles in cell migration, invasion, cell–cell adhesion and filopodia formation. Here, using structured illumination microscopy we show that FMNL2 promotes rapid and highly [...] Read more.
The actin nucleating and polymerizing formin-like 2 (FMNL2) is upregulated in several cancers and has been shown to play important roles in cell migration, invasion, cell–cell adhesion and filopodia formation. Here, using structured illumination microscopy we show that FMNL2 promotes rapid and highly dynamic filopodia formation in epithelial cells while remaining on the tip of the growing filopodia. This filopodia tip localization depends fully on its N-terminal myristoylation. We further show that FMNL2-dependent filopodia formation requires its serine 1072 phosphorylation within the diaphanous-autoregulatory domain (DAD) by protein kinase C (PKC) α. Consistent with this, filopodia formation depends on PKC activity and PKCα localizes to the base of growing filopodia. Thus, a PKCα–FMNL2 signaling module spatiotemporally controls dynamic filopodia formation. Full article
(This article belongs to the Special Issue Actin and Its Associates: Biophysical Aspects in Functional Roles)
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Review

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43 pages, 4219 KiB  
Review
Cytochalasans and Their Impact on Actin Filament Remodeling
by Christopher Lambert, Katharina Schmidt, Marius Karger, Marc Stadler, Theresia E. B. Stradal and Klemens Rottner
Biomolecules 2023, 13(8), 1247; https://doi.org/10.3390/biom13081247 - 15 Aug 2023
Cited by 10 | Viewed by 3646
Abstract
The eukaryotic actin cytoskeleton comprises the protein itself in its monomeric and filamentous forms, G- and F-actin, as well as multiple interaction partners (actin-binding proteins, ABPs). This gives rise to a temporally and spatially controlled, dynamic network, eliciting a plethora of motility-associated processes. [...] Read more.
The eukaryotic actin cytoskeleton comprises the protein itself in its monomeric and filamentous forms, G- and F-actin, as well as multiple interaction partners (actin-binding proteins, ABPs). This gives rise to a temporally and spatially controlled, dynamic network, eliciting a plethora of motility-associated processes. To interfere with the complex inter- and intracellular interactions the actin cytoskeleton confers, small molecular inhibitors have been used, foremost of all to study the relevance of actin filaments and their turnover for various cellular processes. The most prominent inhibitors act by, e.g., sequestering monomers or by interfering with the polymerization of new filaments and the elongation of existing filaments. Among these inhibitors used as tool compounds are the cytochalasans, fungal secondary metabolites known for decades and exploited for their F-actin polymerization inhibitory capabilities. In spite of their application as tool compounds for decades, comprehensive data are lacking that explain (i) how the structural deviances of the more than 400 cytochalasans described to date influence their bioactivity mechanistically and (ii) how the intricate network of ABPs reacts (or adapts) to cytochalasan binding. This review thus aims to summarize the information available concerning the structural features of cytochalasans and their influence on the described activities on cell morphology and actin cytoskeleton organization in eukaryotic cells. Full article
(This article belongs to the Special Issue Actin and Its Associates: Biophysical Aspects in Functional Roles)
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39 pages, 3251 KiB  
Review
Actin Bundles Dynamics and Architecture
by Sudeepa Rajan, Dmitri S. Kudryashov and Emil Reisler
Biomolecules 2023, 13(3), 450; https://doi.org/10.3390/biom13030450 - 28 Feb 2023
Cited by 24 | Viewed by 6094
Abstract
Cells use the actin cytoskeleton for many of their functions, including their division, adhesion, mechanosensing, endo- and phagocytosis, migration, and invasion. Actin bundles are the main constituent of actin-rich structures involved in these processes. An ever-increasing number of proteins that crosslink actin into [...] Read more.
Cells use the actin cytoskeleton for many of their functions, including their division, adhesion, mechanosensing, endo- and phagocytosis, migration, and invasion. Actin bundles are the main constituent of actin-rich structures involved in these processes. An ever-increasing number of proteins that crosslink actin into bundles or regulate their morphology is being identified in cells. With recent advances in high-resolution microscopy and imaging techniques, the complex process of bundles formation and the multiple forms of physiological bundles are beginning to be better understood. Here, we review the physiochemical and biological properties of four families of highly conserved and abundant actin-bundling proteins, namely, α-actinin, fimbrin/plastin, fascin, and espin. We describe the similarities and differences between these proteins, their role in the formation of physiological actin bundles, and their properties—both related and unrelated to their bundling abilities. We also review some aspects of the general mechanism of actin bundles formation, which are known from the available information on the activity of the key actin partners involved in this process. Full article
(This article belongs to the Special Issue Actin and Its Associates: Biophysical Aspects in Functional Roles)
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17 pages, 3315 KiB  
Review
The Actin Network Interfacing Diverse Integrin-Mediated Adhesions
by Benjamin Geiger, Rajaa Boujemaa-Paterski, Sabina E. Winograd-Katz, Jubina Balan Venghateri, Wen-Lu Chung and Ohad Medalia
Biomolecules 2023, 13(2), 294; https://doi.org/10.3390/biom13020294 - 4 Feb 2023
Cited by 6 | Viewed by 3619
Abstract
The interface between the cellular actin network and diverse forms of integrin-mediated cell adhesions displays a unique capacity to serve as accurate chemical and mechanical sensors of the cell’s microenvironment. Focal adhesion-like structures of diverse cell types, podosomes in osteoclasts, and invadopodia of [...] Read more.
The interface between the cellular actin network and diverse forms of integrin-mediated cell adhesions displays a unique capacity to serve as accurate chemical and mechanical sensors of the cell’s microenvironment. Focal adhesion-like structures of diverse cell types, podosomes in osteoclasts, and invadopodia of invading cancer cells display distinct morphologies and apparent functions. Yet, all three share a similar composition and mode of coupling between a protrusive structure (the lamellipodium, the core actin bundle of the podosome, and the invadopodia protrusion, respectively), and a nearby adhesion site. Cytoskeletal or external forces, applied to the adhesion sites, trigger a cascade of unfolding and activation of key adhesome components (e.g., talin, vinculin, integrin), which in turn, trigger the assembly of adhesion sites and generation of adhesion-mediated signals that affect cell behavior and fate. The structural and molecular mechanisms underlying the dynamic crosstalk between the actin cytoskeleton and the adhesome network are discussed. Full article
(This article belongs to the Special Issue Actin and Its Associates: Biophysical Aspects in Functional Roles)
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14 pages, 1020 KiB  
Review
Unconventional Myosins from Caenorhabditis elegans as a Probe to Study Human Orthologues
by Chloe A Johnson, Ranya Behbehani and Folma Buss
Biomolecules 2022, 12(12), 1889; https://doi.org/10.3390/biom12121889 - 16 Dec 2022
Cited by 2 | Viewed by 2267
Abstract
Unconventional myosins are a superfamily of actin-based motor proteins that perform a number of roles in fundamental cellular processes, including (but not limited to) intracellular trafficking, cell motility, endocytosis, exocytosis and cytokinesis. 40 myosins genes have been identified in humans, which belong to [...] Read more.
Unconventional myosins are a superfamily of actin-based motor proteins that perform a number of roles in fundamental cellular processes, including (but not limited to) intracellular trafficking, cell motility, endocytosis, exocytosis and cytokinesis. 40 myosins genes have been identified in humans, which belong to different 12 classes based on their domain structure and organisation. These genes are widely expressed in different tissues, and mutations leading to loss of function are associated with a wide variety of pathologies while over-expression often results in cancer. Caenorhabditis elegans (C. elegans) is a small, free-living, non-parasitic nematode. ~38% of the genome of C. elegans has predicted orthologues in the human genome, making it a valuable tool to study the function of human counterparts and human diseases. To date, 8 unconventional myosin genes have been identified in the nematode, from 6 different classes with high homology to human paralogues. The hum-1 and hum-5 (heavy chain of an unconventional myosin) genes encode myosin of class I, hum-2 of class V, hum-3 and hum-8 of class VI, hum-6 of class VII and hum-7 of class IX. The hum-4 gene encodes a high molecular mass myosin (307 kDa) that is one of the most highly divergent myosins and is a member of class XII. Mutations in many of the human orthologues are lethal, indicating their essential properties. However, a functional characterisation for many of these genes in C. elegans has not yet been performed. This article reviews the current knowledge of unconventional myosin genes in C. elegans and explores the potential use of the nematode to study the function and regulation of myosin motors to provide valuable insights into their role in diseases. Full article
(This article belongs to the Special Issue Actin and Its Associates: Biophysical Aspects in Functional Roles)
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