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Frontiers in Cytoskeleton Research—from Development to Disease 2022

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

Deadline for manuscript submissions: closed (20 August 2022) | Viewed by 12487

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Special Issue Editor

Dr. Bor Luen Tang

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Guest Editor

Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore
Interests: membrane trafficking; neuronal death and regeneration; Sirt1 and aging
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The dynamic cellular cytoskeleton provides shape, rigidity, and motility to all eukaryotic cells. Regulation of the structure, organization, and dynamics of the cytoskeleton underlies a variety of processes, including cellular compartmentation, membrane traffic, signaling, and cell division, all of which impact tissue and organogenesis during development, and underpin pathophysiological processes, such as wound healing, tissue regeneration, cellular transformation, and the formation of intracellular sanctuaries of invasive pathogens.

In this Special Issue of Cells, we invite contributions, in the form of either original research articles or reviews, on aspects related to the theme “Frontiers in Cytoskeleton Research−From Development to Disease”. Articles with mechanistic and functional insights from cellular or molecular biological perspectives are particularly welcome. The content of the manuscripts should be broadly relevant to the topics outlined below. Suggestions for other topics are also welcome, and should be addressed to the editor. The topics of interest include, but are not limited to, the following:

Structural and functional aspects of cytoskeletal components—actin, tubulin, microtubules, microfilaments, and intermediate filaments;
Cytoskeleton and cellular compartmentation—formation of specialized cellular domains, such as cilia and axonal segment fence;
The role of the cytoskeleton in cell division and cell migration;
The role of the cytoskeleton in embryonic and postnatal development;
Cytoskeletal changes in cellular transformation and cancer;
Cytoskeletal changes in cell and tissue regeneration;
Cytoskeletal changes in intracellular viral and bacterial invasions.

Following the successful publication of the first Special Issue “Frontiers in Cytoskeleton Research—From Development to Disease”, we are pleased to announce the launch of a new edition, which is dedicated to highlighting the recent developments in this field of research. Please click on the following link to view the previous publications:

https://0-www-mdpi-com.brum.beds.ac.uk/journal/cells/special_issues/cytoskeleton_research

Dr. Bor Luen Tang
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.

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

cytoskeleton
actin
tubulin
intermediate filaments
cell migration, regeneration
development

Published Papers (5 papers)

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Research

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24 pages, 87194 KiB

Open AccessArticle

Coordination of LMO7 with FAK Signaling Sustains Epithelial Integrity in Renal Epithelia Exposed to Osmotic Pressure

by Yen-Yi Zhen, Chien-Hsing Wu, Hung-Chun Chen, Eddy Essen Chang, Jia-Jung Lee, Wei-Yu Chen, Jer-Ming Chang, Pei-Yun Tseng, Yue-Fang Wang and Chi-Chih Hung

Cells 2022, 11(23), 3805; https://0-doi-org.brum.beds.ac.uk/10.3390/cells11233805 - 28 Nov 2022

Viewed by 1650

Abstract

The kidney epithelial barrier has multifaceted functions in body fluids, electrolyte homeostasis, and urine production. The renal epithelial barrier (REB) frequently faces and challenges osmotic dynamics, which gives rise to osmotic pressure (a physical force). Osmotic pressure overloading can crack epithelial integrity and damage the REB. The endurance of REB to osmotic pressure forces remains obscure. LMO7 (LIM domain only 7) is a protein associated with the cell–cell junctional complex and cortical F-actin. Its upregulation was observed in cells cultured under hypertonic conditions. LMO7 is predominantly distributed in renal tubule epithelial cells. Hypertonic stimulation leads to LMO7 and F-actin assembly in the cortical stress fibers of renal epithelial cells. Hypertonic-isotonic alternation, as a pressure force pushing the plasma membrane inward/outward, was set as osmotic disturbance and was applied to test FAK signaling and LMO7 functioning in maintaining junctional integrity. LMO7 depletion in cells resulted in junctional integrity loss in the epithelial sheet-cultured hypertonic medium or hypertonic-isotonic alternation. Conversely, FAK inhibition by PF-573228 led to failure in robust cortical F-actin assembly and LMO7 association with cortical F-actin in epithelial cells responding to hypertonic stress. Epithelial integrity against osmotic stress and LMO7 and FAK signaling are involved in assembling robust cortical F-actin and maintaining junctional integrity. LMO7 elaborately manages FAK activation in renal epithelial cells, which was demonstrated excessive FAK activation present in LMO7 depleted NRK-52E cells and epithelial integrity loss when cells with LMO7 depletion were exposed to a hypertonic environment. Our data suggests that LMO7 regulates FAK activation and is responsible for maintaining REB under osmotic disturbance. Full article

(This article belongs to the Special Issue Frontiers in Cytoskeleton Research—from Development to Disease 2022)

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21 pages, 6412 KiB

Open AccessArticle

Inhibition of Arp2/3 Complex after ADP-Ribosylation of Arp2 by Binary Clostridioides Toxins

by Carsten Schwan, Alexander E. Lang, Andreas Schlosser, Setsuko Fujita-Becker, Abdulatif AlHaj, Rasmus R. Schröder, Jan Faix, Klaus Aktories and Hans Georg Mannherz

Cells 2022, 11(22), 3661; https://0-doi-org.brum.beds.ac.uk/10.3390/cells11223661 - 18 Nov 2022

Cited by 2 | Viewed by 1920

Abstract

Clostridioides bacteria are responsible for life threatening infections. Here, we show that in addition to actin, the binary toxins CDT, C2I, and Iota from Clostridioides difficile, botulinum, and perfrigens, respectively, ADP-ribosylate the actin-related protein Arp2 of Arp2/3 complex and its additional components ArpC1, ArpC2, and ArpC4/5. The Arp2/3 complex is composed of seven subunits and stimulates the formation of branched actin filament networks. This activity is inhibited after ADP-ribosylation of Arp2. Translocation of the ADP-ribosyltransferase component of CDT toxin into human colon carcinoma Caco2 cells led to ADP-ribosylation of cellular Arp2 and actin followed by a collapse of the lamellipodial extensions and F-actin network. Exposure of isolated mouse colon pieces to CDT toxin induced the dissolution of the enterocytes leading to luminal aggregation of cellular debris and the collapse of the mucosal organization. Thus, we identify the Arp2/3 complex as hitherto unknown target of clostridial ADP-ribosyltransferases. Full article

(This article belongs to the Special Issue Frontiers in Cytoskeleton Research—from Development to Disease 2022)

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18 pages, 19082 KiB

Open AccessCommunication

A Ca²⁺-Mediated Switch of Epiplakin from a Diffuse to Keratin-Bound State Affects Keratin Dynamics

by Sonia Ratajczyk, Corinne Drexler, Reinhard Windoffer, Rudolf E. Leube and Peter Fuchs

Cells 2022, 11(19), 3077; https://0-doi-org.brum.beds.ac.uk/10.3390/cells11193077 - 30 Sep 2022

Cited by 1 | Viewed by 1664

Abstract

Keratins exert important structural but also cytoprotective functions. They have to be adaptable to support cellular homeostasis. Epiplakin (EPPK1) has been shown to decorate keratin filaments in epithelial cells and to play a protective role under stress, but the mechanism is still unclear. Using live-cell imaging of epithelial cells expressing fluorescently tagged EPPK1 and keratin, we report here an unexpected dynamic behavior of EPPK1 upon stress. EPPK1 was diffusely distributed throughout the cytoplasm and not associated with keratin filaments in living cells under standard culture conditions. However, ER-, oxidative and UV-stress, as well as cell fixation, induced a rapid association of EPPK1 with keratin filaments. This re-localization of EPPK1 was reversible and dependent on the elevation of cytoplasmic Ca²⁺ levels. Moreover, keratin filament association of EPPK1 led to significantly reduced keratin dynamics. Thus, we propose that EPPK1 stabilizes the keratin network in stress conditions, which involve increased cytoplasmic Ca²⁺. Full article

(This article belongs to the Special Issue Frontiers in Cytoskeleton Research—from Development to Disease 2022)

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Review

Jump to: Research

15 pages, 1446 KiB

Open AccessReview

Links of Cytoskeletal Integrity with Disease and Aging

by Yu Jin Kim, Min Jeong Cho, Won Dong Yu, Myung Joo Kim, Sally Yunsun Kim and Jae Ho Lee

Cells 2022, 11(18), 2896; https://0-doi-org.brum.beds.ac.uk/10.3390/cells11182896 - 16 Sep 2022

Cited by 14 | Viewed by 4447

Abstract

Aging is a complex feature and involves loss of multiple functions and nonreversible phenotypes. However, several studies suggest it is possible to protect against aging and promote rejuvenation. Aging is associated with many factors, such as telomere shortening, DNA damage, mitochondrial dysfunction, and loss of homeostasis. The integrity of the cytoskeleton is associated with several cellular functions, such as migration, proliferation, degeneration, and mitochondrial bioenergy production, and chronic disorders, including neuronal degeneration and premature aging. Cytoskeletal integrity is closely related with several functional activities of cells, such as aging, proliferation, degeneration, and mitochondrial bioenergy production. Therefore, regulation of cytoskeletal integrity may be useful to elicit antiaging effects and to treat degenerative diseases, such as dementia. The actin cytoskeleton is dynamic because its assembly and disassembly change depending on the cellular status. Aged cells exhibit loss of cytoskeletal stability and decline in functional activities linked to longevity. Several studies reported that improvement of cytoskeletal stability can recover functional activities. In particular, microtubule stabilizers can be used to treat dementia. Furthermore, studies of the quality of aged oocytes and embryos revealed a relationship between cytoskeletal integrity and mitochondrial activity. This review summarizes the links of cytoskeletal properties with aging and degenerative diseases and how cytoskeletal integrity can be modulated to elicit antiaging and therapeutic effects. Full article

(This article belongs to the Special Issue Frontiers in Cytoskeleton Research—from Development to Disease 2022)

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15 pages, 2506 KiB

Open AccessReview

Reforming the Barrier: The Role of Formins in Wound Repair

by Parinaz Ahangar and Allison J. Cowin

Cells 2022, 11(18), 2779; https://0-doi-org.brum.beds.ac.uk/10.3390/cells11182779 - 06 Sep 2022

Cited by 3 | Viewed by 2117

Abstract

The restoration of an intact epidermal barrier after wound injury is the culmination of a highly complex and exquisitely regulated physiological process involving multiple cells and tissues, overlapping dynamic events and protein synthesis and regulation. Central to this process is the cytoskeleton, a system of intracellular proteins that are instrumental in regulating important processes involved in wound repair including chemotaxis, cytokinesis, proliferation, migration, and phagocytosis. One highly conserved family of cytoskeletal proteins that are emerging as major regulators of actin and microtubule nucleation, polymerization, and stabilization are the formins. The formin family includes 15 different proteins categorized into seven subfamilies based on three formin homology domains (FH1, FH2, and FH3). The formins themselves are regulated in different ways including autoinhibition, activation, and localization by a range of proteins, including Rho GTPases. Herein, we describe the roles and effects of the formin family of cytoskeletal proteins on the fundamental process of wound healing and highlight recent advances relating to their important functions, mechanisms, and regulation at the molecular and cellular levels. Full article

(This article belongs to the Special Issue Frontiers in Cytoskeleton Research—from Development to Disease 2022)

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