{"title":"Betrayal From the Core: Centriolar and Cytoskeletal Subversion by Infectious Pathogens.","authors":"Himanshi Amita, Zidhan Subair, Tulasiram Mora, Pranay Eknath Dudhe, Karthigeyan Dhanasekaran","doi":"10.1002/cm.22004","DOIUrl":"https://doi.org/10.1002/cm.22004","url":null,"abstract":"<p><p>Microbes and parasites have evolved several means to evade and usurp the host cellular machinery to mediate pathogenesis. Being the major microtubule-organizing center (MTOC) of the cell, the centrosome is targeted by multiple viral and nonviral pathogens to mediate their assembly and trafficking within the host cell. This review examines the consequence of such targeting to the centrosome and associated cytoskeletal machinery. We have also amassed a substantial body of evidence of viruses utilizing the cilia within airway epithelium to mediate infection and the hijacking of host cytoskeletal machinery for efficient entry, replication, and egress. While infections have been demonstrated to induce structural, functional, and numerical aberrations in centrosomes, and induce ciliary dysfunction, current literature increasingly supports the notion of a pro-viral role for these organelles. Although less explored, the impact of bacterial and parasitic pathogens on these structures has also been addressed very briefly. Mechanistically, the molecular pathways responsible for these effects remain largely uncharacterized in many instances. Future research focusing on the centriolar triad comprising the centrosome, cilia, and centriolar satellites will undoubtedly provide vital insights into the tactics employed by infectious agents to subvert the host centriole and cytoskeleton-based machinery.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-02-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143124003","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Picture of the Month by E. S. Klimenko.","authors":"","doi":"10.1002/cm.22001","DOIUrl":"https://doi.org/10.1002/cm.22001","url":null,"abstract":"","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-02-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143124007","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Picture of the Month by E. S. Klimenko.","authors":"","doi":"10.1002/cm.22000","DOIUrl":"https://doi.org/10.1002/cm.22000","url":null,"abstract":"","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-02-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143082424","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Overexpression of Drosophila NUAK or Constitutively-Active Formin-Like Promotes the Formation of Aberrant Myofibrils.","authors":"Prabhat Tiwari, David Brooks, Erika R Geisbrecht","doi":"10.1002/cm.21999","DOIUrl":"https://doi.org/10.1002/cm.21999","url":null,"abstract":"<p><p>Muscle development and maintenance is central to the normal functioning of animals. Muscle tissues exhibit high levels of activity and require the dynamic turnover of proteins. An actomyosin scaffold functions with additional proteins comprising the basic contractile subunit of striated muscle, known as the sarcomere. Drosophila muscles are similar to vertebrate muscles in composition and they share a similar mechanism of development. Drosophila NUAK (NUAK) is the homolog of NUAK1 and NUAK2 in vertebrates. NUAK belongs to the family of AMP-activated protein kinases (AMPKs), a group of proteins with broad and overlapping cellular targets. Here we confirm that NUAK dynamically modulates larval muscle sarcomere size as upregulation of NUAK produces longer sarcomeres, including increased thin filament lengths. Furthermore, NUAK overexpression results in aberrant myofibers above the nuclei plane, upregulation of Formin-like (Frl), and an increase in newly synthesized proteins at sites consistent with actin filament assembly. Expression of constitutively-active Frl also produces aberrant myofibers similar to NUAK overexpression. These results taken together strongly suggest a functional link between NUAK and Frl in myofibril formation in an in vivo setting.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143061378","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Introduction to the Special Issue \"Actin-Binding Proteins in Diseases\".","authors":"Partha Roy, Yongho Bae","doi":"10.1002/cm.21996","DOIUrl":"https://doi.org/10.1002/cm.21996","url":null,"abstract":"","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143061373","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Haseena P A, Nimisha Basavaraju, Anant Gupta, Reddy Peera Kommaddi
{"title":"Actin Cytoskeleton at the Synapse: An Alzheimer's Disease Perspective.","authors":"Haseena P A, Nimisha Basavaraju, Anant Gupta, Reddy Peera Kommaddi","doi":"10.1002/cm.21993","DOIUrl":"https://doi.org/10.1002/cm.21993","url":null,"abstract":"<p><p>Actin, a ubiquitous and highly conserved cytoskeletal protein, plays a pivotal role in various cellular functions such as structural support, facilitating cell motility, and contributing to the dynamic processes of synaptic function. Apart from its established role in inducing morphological changes, recent developments in the field indicate an active involvement of actin in modulating both the structure and function of pre- and postsynaptic terminals. Within the presynapse, it is involved in the organization and trafficking of synaptic vesicles, contributing to neurotransmitter release. In the postsynapse, actin dynamically modulates dendritic spines, influencing the postsynaptic density organization and anchoring of neurotransmitter receptors. In addition, the dynamic interplay of actin at the synapse underscores its essential role in regulating neural communication. This review strives to offer a comprehensive overview of the recent advancements in understanding the multifaceted role of the actin cytoskeleton in synaptic functions. By emphasizing its aberrant regulation, we aim to provide valuable insights into the underlying mechanisms of Alzheimer's disease pathophysiology.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143017353","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"In Situ Mechanics of the Cytoskeleton.","authors":"Ryota Orii, Hirokazu Tanimoto","doi":"10.1002/cm.21995","DOIUrl":"https://doi.org/10.1002/cm.21995","url":null,"abstract":"<p><p>Not only for man-made architecture but also for living cells, the relationship between force and structure is a fundamental properties that governs their mechanical behaviors. However, our knowledge of the mechanical properties of intracellular structures is very limited because of the lack of direct measurement methods. We established high-force intracellular magnetic tweezers that can generate calibrated forces up to 10 nN, enabling direct force measurements of the cytoskeleton. Using this method, we show that the strain field of the microtubule and actin meshwork follow the same scaling, suggesting that the two cytoskeletal systems behave as an integrated elastic body. Furthermore, quantification of structural response of single microtubules demonstrates that microtubules are enclosed by the elastic medium of filamentous actin. Our results defining the force-structure relationship of the cytoskeleton serve as a framework to understand cellular behaviors by direct intracellular mechanical measurement.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143017358","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Shogo Yoshihara, Takao Nakata, Jun Kashiwazaki, Kazuhiro Aoyama, Issei Mabuchi
{"title":"In Vitro Formation of Actin Ring in the Fission Yeast Cell Extracts.","authors":"Shogo Yoshihara, Takao Nakata, Jun Kashiwazaki, Kazuhiro Aoyama, Issei Mabuchi","doi":"10.1002/cm.21997","DOIUrl":"https://doi.org/10.1002/cm.21997","url":null,"abstract":"<p><p>Cytokinesis in animal and fungal cells requires the contraction of actomyosin-based contractile rings formed in the division cortex of the cell during late mitosis. However, the detailed mechanism remains incompletely understood. Here, we aim to develop a novel cell-free system by encapsulating cell extracts obtained from fission yeast cells within lipid vesicles, which subsequently leads to the formation of a contractile ring-like structure inside the vesicles. Using this system, we found that an actin ring structure formed in vesicles of a size similar to that of fission yeast cells, with the frequency of ring appearance increasing in the presence of PI(4,5)P<sub>2</sub> (PIP<sub>2</sub>). In contrast, larger vesicles tended to form actin bundles, which were sometimes associated with ring structures or network-like structures. The effects of various inhibitors affecting cytoskeleton formation were investigated, revealing that actin polymerization was essential for the formation of these actin structures. Additionally, the involvement of ATP, the Schizosaccharomyces pombe PLK \"Plo1,\" and the small GTPase Rho was suggested to play a crucial role in this process. Examination of mitotic extracts revealed the formation of actin dot structures in phosphatidylethanolamine vesicles. However, most of these structures disappeared in the presence of PIP<sub>2</sub>, leading to the formation of actin Rings instead. Using extracts from cells expressing α-actinin Ain1 or myosin-II light chain Rlc1, both fused with fluorescent proteins, we found that these proteins colocalized with actin bundles. In summary, we have developed a new semi-in vitro system to investigate mechanisms such as cell division and cytoskeleton formation.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143017360","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"An Interview With Dan Mulvihill, School of Biosciences, University of Kent, UK.","authors":"Dan Mulvihill, Paul Trevorrow","doi":"10.1002/cm.21994","DOIUrl":"https://doi.org/10.1002/cm.21994","url":null,"abstract":"","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143017355","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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