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Cells
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Cytoskeletal Remodeling in Health and Disease
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Cytoskeletal Remodeling in Health and Disease

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cell Motility and Adhesion".

Deadline for manuscript submissions: 30 April 2024 | Viewed by 4249

Special Issue Editors

Prof. Dr. Annette Müller-Taubenberger

E-Mail Website
Guest Editor
Biomedical Center Munich, Cell Biology (Anatomy III), Ludwig Maximilian University, 82152 Planegg-Martinsried, Germany
Interests: actin cytoskeleton dynamics; cell migration; cytoskeletal proteins; live-cell imaging; reproductive medicine
Special Issues, Collections and Topics in MDPI journals
Dr. Francisco Rivero

E-Mail Website
Guest Editor
Reader in Biomedical Science, Hull York Medical School, University of Hull, Hull HU6 7RX, UK
Interests: actin cytoskeleton; actin-binding proteins; Rho GTPases; cyclase-associated protein; coronin; plastin; cell motility; platelet biology; endothelial cell biology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Cytoskeleton remodeling, the dynamic process of modulating the cytoskeleton structure and organization, is essential for a variety of cellular functions, including modulation of the mechanical properties of cells, morphogenesis, cell migration, intracellular transport, cell division, gene expression, and metabolism. The regulation of the cytoskeleton is a complex process that involves a vast array of proteins, signaling pathways, and molecular motors. Despite its critical role in normal cellular function, cytoskeleton remodeling contributes to a range of diseases.

Understanding the mechanisms that trigger cytoskeletal remodeling is instrumental to understand the pathophysiology of numerous musculoskeletal, cardiovascular, immunological, and neurological disorders. Dysregulation of the cytoskeleton facilitates migration, invasion, and angiogenesis characteristic of cancer metastasis. The cytoskeleton remodeling machinery is also a target that pathogens manipulate to facilitate their own spread. Exciting recent advances have identified several new proteins and pathways involved in cytoskeletal regulation, and this knowledge will be key to developing new treatments for many diseases.

This Special Issue of Cells aims to collect the newest advances in the field of cytoskeletal remodeling, with an emphasis on studies that provide insight into molecular pathogenesis and potential therapeutic interventions of disorders with a strong cytoskeletal component. Studies on microfilament-, microtubule- and intermediate filament-associated proteins and on components involved in the organization of their remodeling are welcome.

Prof. Dr. Annette Müller-Taubenberger
Dr. Francisco Rivero
Guest Editors

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.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cells is an international peer-reviewed open access semimonthly journal published by MDPI.

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 cytoskeleton
  • cellular mechanics
  • cancer
  • cytoskeletal proteins
  • immunity

Published Papers (5 papers)

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Research

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15 pages, 2664 KiB  
Article
A Novel Interaction of Slug (SNAI2) and Nuclear Actin
by Ling Zhuo, Jan B. Stöckl, Thomas Fröhlich, Simone Moser, Angelika M. Vollmar and Stefan Zahler
Cells 2024, 13(8), 696; https://doi.org/10.3390/cells13080696 - 17 Apr 2024
Viewed by 227
Abstract
Actin is a protein of central importance to many cellular functions. Its localization and activity are regulated by interactions with a high number of actin-binding proteins. In a yeast two-hybrid (Y2H) screening system, snail family transcriptional repressor 2 (SNAI2 or slug) was identified [...] Read more.
Actin is a protein of central importance to many cellular functions. Its localization and activity are regulated by interactions with a high number of actin-binding proteins. In a yeast two-hybrid (Y2H) screening system, snail family transcriptional repressor 2 (SNAI2 or slug) was identified as a yet unknown potential actin-binding protein. We validated this interaction using immunoprecipitation and analyzed the functional relation between slug and actin. Since both proteins have been reported to be involved in DNA double-strand break (DSB) repair, we focused on their interaction during this process after treatment with doxorubicin or UV irradiation. Confocal microscopy elicits that the overexpression of actin fused to an NLS stabilizes complexes of slug and γH2AX, an early marker of DNA damage repair. Full article
(This article belongs to the Special Issue Cytoskeletal Remodeling in Health and Disease)
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21 pages, 3255 KiB  
Article
The Role of β-Dystroglycan in Nuclear Dynamics
by Matthew Cook, Ben Stevenson, Laura A. Jacobs, Daniel Leocadio Victoria, Bulmaro Cisneros, Jamie K. Hobbs, Colin L. Stewart and Steve J. Winder
Cells 2024, 13(5), 431; https://doi.org/10.3390/cells13050431 - 29 Feb 2024
Viewed by 691
Abstract
Dystroglycan is a ubiquitously expressed heterodimeric cell-surface laminin receptor with roles in cell adhesion, signalling, and membrane stabilisation. More recently, the transmembrane β-subunit of dystroglycan has been shown to localise to both the nuclear envelope and the nucleoplasm. This has led to the [...] Read more.
Dystroglycan is a ubiquitously expressed heterodimeric cell-surface laminin receptor with roles in cell adhesion, signalling, and membrane stabilisation. More recently, the transmembrane β-subunit of dystroglycan has been shown to localise to both the nuclear envelope and the nucleoplasm. This has led to the hypothesis that dystroglycan may have a structural role at the nuclear envelope analogous to its role at the plasma membrane. The biochemical fraction of myoblast cells clearly supports the presence of dystroglycan in the nucleus. Deletion of the dystroglycan protein by disruption of the DAG1 locus using CRISPR/Cas9 leads to changes in nuclear size but not overall morphology; moreover, the Young’s modulus of dystroglycan-deleted nuclei, as determined by atomic force microscopy, is unaltered. Dystroglycan-disrupted myoblasts are also no more susceptible to nuclear stresses including chemical and mechanical, than normal myoblasts. Re-expression of dystroglycan in DAG1-disrupted myoblasts restores nuclear size without affecting other nuclear parameters. Full article
(This article belongs to the Special Issue Cytoskeletal Remodeling in Health and Disease)
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17 pages, 5840 KiB  
Article
Differential Role of the RAC1-Binding Proteins FAM49b (CYRI-B) and CYFIP1 in Platelets
by Dmitri Sisario, Markus Spindler, Katharina J. Ermer, Noah Grütz, Leo Nicolai, Florian Gaertner, Laura M. Machesky and Markus Bender
Cells 2024, 13(4), 299; https://doi.org/10.3390/cells13040299 - 06 Feb 2024
Viewed by 776
Abstract
Platelet function at vascular injury sites is tightly regulated through the actin cytoskeleton. The Wiskott–Aldrich syndrome protein-family verprolin-homologous protein (WAVE)-regulatory complex (WRC) activates lamellipodia formation via ARP2/3, initiated by GTP-bound RAC1 interacting with the WRC subunit CYFIP1. The protein FAM49b (Family of Unknown [...] Read more.
Platelet function at vascular injury sites is tightly regulated through the actin cytoskeleton. The Wiskott–Aldrich syndrome protein-family verprolin-homologous protein (WAVE)-regulatory complex (WRC) activates lamellipodia formation via ARP2/3, initiated by GTP-bound RAC1 interacting with the WRC subunit CYFIP1. The protein FAM49b (Family of Unknown Function 49b), also known as CYRI-B (CYFIP-Related RAC Interactor B), has been found to interact with activated RAC1, leading to the negative regulation of the WRC in mammalian cells. To investigate the role of FAM49b in platelet function, we studied platelet-specific Fam49b−/−-, Cyfip1−/−-, and Cyfip1/Fam49b−/−-mice. Platelet counts and activation of Fam49b−/− mice were comparable to those of control mice. On fully fibrinogen-coated surfaces, Fam49b−/−-platelets spread faster with an increased mean projected cell area than control platelets, whereas Cyfip1/Fam49b−/−-platelets did not form lamellipodia, phenocopying the Cyfip1−/−-platelets. However, Fam49b−/−-platelets often assumed a polarized shape and were more prone to migrate on fibrinogen-coated surfaces. On 2D structured micropatterns, however, Fam49b−/−-platelets displayed reduced spreading, whereas spreading of Cyfip1−/−- and Cyfip1/Fam49b−/−-platelets was enhanced. In summary, FAM49b contributes to the regulation of morphology and migration of spread platelets, but to exert its inhibitory effect on actin polymerization, the functional WAVE complex must be present. Full article
(This article belongs to the Special Issue Cytoskeletal Remodeling in Health and Disease)
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19 pages, 3426 KiB  
Article
Plasma Membrane Blebbing Is Controlled by Subcellular Distribution of Vimentin Intermediate Filaments
by Aleksandra S. Chikina, Anna O. Zholudeva, Maria E. Lomakina, Igor I. Kireev, Alexander A. Dayal, Alexander A. Minin, Mathieu Maurin, Tatyana M. Svitkina and Antonina Y. Alexandrova
Cells 2024, 13(1), 105; https://doi.org/10.3390/cells13010105 - 04 Jan 2024
Viewed by 1433
Abstract
The formation of specific cellular protrusions, plasma membrane blebs, underlies the amoeboid mode of cell motility, which is characteristic for free-living amoebae and leukocytes, and can also be adopted by stem and tumor cells to bypass unfavorable migration conditions and thus facilitate their [...] Read more.
The formation of specific cellular protrusions, plasma membrane blebs, underlies the amoeboid mode of cell motility, which is characteristic for free-living amoebae and leukocytes, and can also be adopted by stem and tumor cells to bypass unfavorable migration conditions and thus facilitate their long-distance migration. Not all cells are equally prone to bleb formation. We have previously shown that membrane blebbing can be experimentally induced in a subset of HT1080 fibrosarcoma cells, whereas other cells in the same culture under the same conditions retain non-blebbing mesenchymal morphology. Here we show that this heterogeneity is associated with the distribution of vimentin intermediate filaments (VIFs). Using different approaches to alter the VIF organization, we show that blebbing activity is biased toward cell edges lacking abundant VIFs, whereas the VIF-rich regions of the cell periphery exhibit low blebbing activity. This pattern is observed both in interphase fibroblasts, with and without experimentally induced blebbing, and during mitosis-associated blebbing. Moreover, the downregulation of vimentin expression or displacement of VIFs away from the cell periphery promotes blebbing even in cells resistant to bleb-inducing treatments. Thus, we reveal a new important function of VIFs in cell physiology that involves the regulation of non-apoptotic blebbing essential for amoeboid cell migration and mitosis. Full article
(This article belongs to the Special Issue Cytoskeletal Remodeling in Health and Disease)
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Review

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13 pages, 3536 KiB  
Review
Miro GTPases at the Crossroads of Cytoskeletal Dynamics and Mitochondrial Trafficking
by Pontus Aspenström
Cells 2024, 13(7), 647; https://doi.org/10.3390/cells13070647 - 07 Apr 2024
Viewed by 572
Abstract
Miro GTPases are key components in the machinery responsible for transporting mitochondria and peroxisomes along microtubules, and also play important roles in regulating calcium homeostasis and organizing contact sites between mitochondria and the endoplasmic reticulum. Moreover, Miro GTPases have been shown to interact [...] Read more.
Miro GTPases are key components in the machinery responsible for transporting mitochondria and peroxisomes along microtubules, and also play important roles in regulating calcium homeostasis and organizing contact sites between mitochondria and the endoplasmic reticulum. Moreover, Miro GTPases have been shown to interact with proteins that actively regulate cytoskeletal organization and dynamics, suggesting that these GTPases participate in organizing cytoskeletal functions and organelle transport. Derailed mitochondrial transport is associated with neuropathological conditions such as Parkinson’s and Alzheimer’s diseases. This review explores our recent understanding of the diverse roles of Miro GTPases under cytoskeletal control, both under normal conditions and during the course of human diseases such as neuropathological disorders. Full article
(This article belongs to the Special Issue Cytoskeletal Remodeling in Health and Disease)
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