Haseena P A, Nimisha Basavaraju, Anant Gupta, Reddy Peera Kommaddi
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.
{"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":"10.1002/cm.21993","url":null,"abstract":"<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":55186,"journal":{"name":"Cytoskeleton","volume":"83 1","pages":"15-28"},"PeriodicalIF":1.6,"publicationDate":"2025-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21993","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143017353","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ON THE INNER BACK COVER: The focal adhesion protein Hic-5 localizes to the distal ends of stress fiber-associated septin filaments. U2OS osteosarcoma cells were stained for Hic-5 (blue), Septin 7 (green), and F-actin (red).
Credit: Katia Brock (Department of Cell and Developmental Biology, State University of New York Upstate Medical University)
{"title":"Inner Back Cover Image","authors":"","doi":"10.1002/cm.21991","DOIUrl":"https://doi.org/10.1002/cm.21991","url":null,"abstract":"<p>ON THE INNER BACK COVER: The focal adhesion protein Hic-5 localizes to the distal ends of stress fiber-associated septin filaments. U2OS osteosarcoma cells were stained for Hic-5 (blue), Septin 7 (green), and F-actin (red).</p><p>Credit: Katia Brock (Department of Cell and Developmental Biology, State University of New York Upstate Medical University)\u0000\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure>\u0000 </p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 1-2","pages":"C3"},"PeriodicalIF":2.4,"publicationDate":"2025-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21991","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143117683","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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.
{"title":"In Situ Mechanics of the Cytoskeleton","authors":"Ryota Orii, Hirokazu Tanimoto","doi":"10.1002/cm.21995","DOIUrl":"10.1002/cm.21995","url":null,"abstract":"<div>\u0000 \u0000 <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>\u0000 </div>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 10","pages":"621-623"},"PeriodicalIF":1.6,"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":4,"RegionCategory":"生物学","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
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)P2 (PIP2). 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 PIP2, 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.
{"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":"10.1002/cm.21997","url":null,"abstract":"<div>\u0000 \u0000 <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 <i>Schizosaccharomyces pombe</i> 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>\u0000 </div>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 10","pages":"624-642"},"PeriodicalIF":1.6,"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":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ON THE FRONT COVER: The focal adhesion protein Paxillin localizes to the distal ends of stress fiber-associated septin filaments. U2OS osteosarcoma cells were stained for Paxillin (blue), Septin 7 (green), and F-actin (red).
Credit: Katia Brock (Department of Cell and Developmental Biology, State University of New York Upstate Medical University)
{"title":"Front Cover Image","authors":"","doi":"10.1002/cm.21989","DOIUrl":"https://doi.org/10.1002/cm.21989","url":null,"abstract":"<p>ON THE FRONT COVER: The focal adhesion protein Paxillin localizes to the distal ends of stress fiber-associated septin filaments. U2OS osteosarcoma cells were stained for Paxillin (blue), Septin 7 (green), and F-actin (red).</p><p>Credit: Katia Brock (Department of Cell and Developmental Biology, State University of New York Upstate Medical University)\u0000\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure>\u0000 </p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 1-2","pages":"C1"},"PeriodicalIF":2.4,"publicationDate":"2025-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21989","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143117684","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ON THE INNER FRONT COVER: Endogenous tropomyosin Tpm4.2 tagged with APEX at its C-terminus is incorporated into actin filament bundles in homozygous mouse embryo fibroblasts. The endogenous Tpm4.2-APEX shown in red were visualised by an anti-Tpm4.2 antibody and actin filaments shown in green were visualised by phalloidin.
Credit: Jeff Hook (Cytoskeleton Therapeutics Research Unit, School of Biomedical Sciences, UNSW Sydney, Australia)
{"title":"Inner Front Cover Image","authors":"","doi":"10.1002/cm.21990","DOIUrl":"https://doi.org/10.1002/cm.21990","url":null,"abstract":"<p>ON THE INNER FRONT COVER: Endogenous tropomyosin Tpm4.2 tagged with APEX at its C-terminus is incorporated into actin filament bundles in homozygous mouse embryo fibroblasts. The endogenous Tpm4.2-APEX shown in red were visualised by an anti-Tpm4.2 antibody and actin filaments shown in green were visualised by phalloidin.</p><p>Credit: Jeff Hook (Cytoskeleton Therapeutics Research Unit, School of Biomedical Sciences, UNSW Sydney, Australia)\u0000\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure>\u0000 </p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 1-2","pages":"C2"},"PeriodicalIF":2.4,"publicationDate":"2025-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21990","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143117685","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
ON THE BACK COVER: DA-Raf inhibits ERK activation, resulting in the suppression of collective cell migration and invasion of KRASmutant cancer cells. In human pancreatic carcinoma MIA PaCa-2 cells, phospho-ERK1/2 (magenta) is suppressed by the expression of EGFP–DA-Raf (green). EGFP–DA-Raf is concentrated on the plasma membrane.
Credit: Aoi Matsuda and Takeshi Endo (Chiba University, Japan)
{"title":"Back Cover Image","authors":"","doi":"10.1002/cm.21992","DOIUrl":"https://doi.org/10.1002/cm.21992","url":null,"abstract":"<p>ON THE BACK COVER: DA-Raf inhibits ERK activation, resulting in the suppression of collective cell migration and invasion of KRASmutant cancer cells. In human pancreatic carcinoma MIA PaCa-2 cells, phospho-ERK1/2 (magenta) is suppressed by the expression of EGFP–DA-Raf (green). EGFP–DA-Raf is concentrated on the plasma membrane.</p><p>Credit: Aoi Matsuda and Takeshi Endo (Chiba University, Japan)\u0000\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure>\u0000 </p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 1-2","pages":"C4"},"PeriodicalIF":2.4,"publicationDate":"2025-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21992","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143117686","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Picture of the Month by Katia Brock","authors":"","doi":"10.1002/cm.21982","DOIUrl":"10.1002/cm.21982","url":null,"abstract":"","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 1-2","pages":"71"},"PeriodicalIF":2.4,"publicationDate":"2025-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143017362","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","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":"10.1002/cm.21994","url":null,"abstract":"","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 12","pages":"850-851"},"PeriodicalIF":1.6,"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":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Picture of the Month by Jeff Hook","authors":"","doi":"10.1002/cm.21983","DOIUrl":"10.1002/cm.21983","url":null,"abstract":"","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 1-2","pages":"72"},"PeriodicalIF":2.4,"publicationDate":"2025-01-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142967592","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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