CytoskeletonPub Date : 2024-01-15DOI: 10.1002/cm.21818
Juyeon Hwang, Haruaki Yanagisawa, Keira C. Davis, Emily L. Hunter, Laura A. Fox, Ariana R. Jimenez, Reagan E. Goodwin, Sarah A. Gordon, Courtney D. E. Stuart, Raqual Bower, Mary E. Porter, Susan K. Dutcher, Winfield S. Sale, Karl F. Lechtreck, Lea M. Alford
{"title":"Assembly of FAP93 at the proximal axoneme in Chlamydomonas cilia","authors":"Juyeon Hwang, Haruaki Yanagisawa, Keira C. Davis, Emily L. Hunter, Laura A. Fox, Ariana R. Jimenez, Reagan E. Goodwin, Sarah A. Gordon, Courtney D. E. Stuart, Raqual Bower, Mary E. Porter, Susan K. Dutcher, Winfield S. Sale, Karl F. Lechtreck, Lea M. Alford","doi":"10.1002/cm.21818","DOIUrl":"10.1002/cm.21818","url":null,"abstract":"<p>To identify proteins specific to the proximal ciliary axoneme, we used iTRAQ to compare short (~2 μm) and full-length (~11 μm) axonemes of <i>Chlamydomonas</i>. Known components of the proximal axoneme such as minor dynein heavy chains and LF5 kinase as well as the ciliary tip proteins FAP256 (CEP104) and EB1 were enriched in short axonemes whereas proteins present along the length of the axoneme were of similar abundance in both samples. The iTRAQ analysis revealed that FAP93, a protein of unknown function, and protein phosphatase 2A (PP2A) are enriched in the short axonemes. Consistently, immunoblots show enrichment of FAP93 and PP2A in short axonemes and immunofluorescence confirms the localization of FAP93 and enrichment of PP2A at the proximal axoneme. Ciliary regeneration reveals that FAP93 assembles continuously but more slowly than other axonemal structures and terminates at 1.03 μm in steady-state axonemes. The length of FAP93 assembly correlates with ciliary length, demonstrating ciliary length-dependent assembly of FAP93. Dikaryon rescue experiments show that FAP93 can assemble independently of IFT transport. In addition, FRAP analysis of GFP-tagged FAP93 demonstrates that FAP93 is stably anchored in the axoneme. FAP93 may function as a scaffold for assembly of other specific proteins at the proximal axoneme.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 11","pages":"539-555"},"PeriodicalIF":2.4,"publicationDate":"2024-01-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139466767","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}
CytoskeletonPub Date : 2024-01-12DOI: 10.1002/cm.21828
Ryosuke Yamamoto, Takahide Kon
{"title":"Functional and structural significance of the inner-arm-dynein subspecies d in ciliary motility","authors":"Ryosuke Yamamoto, Takahide Kon","doi":"10.1002/cm.21828","DOIUrl":"10.1002/cm.21828","url":null,"abstract":"<p>Motile cilia play various important physiological roles in eukaryotic organisms including cell motility and fertility. Inside motile cilia, large motor-protein complexes called “ciliary dyneins” coordinate their activities and drive ciliary motility. The ciliary dyneins include the outer-arm dyneins, the double-headed inner-arm dynein (IDA f/I1), and several single-headed inner-arm dyneins (IDAs a, b, c, d, e, and g). Among these single-headed IDAs, one of the ciliary dyneins, IDA d, is of particular interest because of its unique properties and subunit composition. In addition, defects in this subspecies have recently been associated with several types of ciliopathies in humans, such as primary ciliary dyskinesia and multiple morphologic abnormalities of the flagellum. In this mini-review, we discuss the composition, structure, and motor properties of IDA d, which have been studied in the model organism <i>Chlamydomonas reinhardtii</i>, and further discuss the relationship between IDA d and human ciliopathies. In addition, we provide future perspectives and discuss remaining questions regarding this intriguing dynein subspecies.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 11","pages":"569-577"},"PeriodicalIF":2.4,"publicationDate":"2024-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21828","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139426114","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}
CytoskeletonPub Date : 2023-12-29DOI: 10.1002/cm.21827
Christine M. Loescher, Wolfgang A. Linke
{"title":"Titin takes centerstage among cytoskeletal contributions to myocardial passive stiffness","authors":"Christine M. Loescher, Wolfgang A. Linke","doi":"10.1002/cm.21827","DOIUrl":"10.1002/cm.21827","url":null,"abstract":"<p>Both diastolic filling and systolic pumping of the heart are dependent on the passive stiffness characteristics of various mechanical elements of myocardium. However, the specific contribution from each element, including the extracellular matrix, actin filaments, microtubules, desmin intermediate filaments, and sarcomeric titin springs, remains challenging to assess. Recently, a mouse model allowing for precise and acute cleavage of the titin springs was used to remove one mechanical element after the other from cardiac fibers and record the effect on passive stiffness. It became clear that the stiffness contribution from each element is context-dependent and varies depending on strain level and the force component considered (elastic or viscous); elements do not act in isolation but in a tensegral relationship. Titin is a substantial contributor under all conditions and dominates the elastic forces at both low and high strains. The contribution to viscous forces is more equally shared between microtubules, titin, and actin. However, the extracellular matrix substantially contributes to both force components at higher strain levels. Desmin filaments may bear low stiffness. These insights enhance our understanding of how different filament networks contribute to passive stiffness in the heart and offer new perspectives for targeting this stiffness in heart failure treatment.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 2-3","pages":"184-187"},"PeriodicalIF":2.9,"publicationDate":"2023-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21827","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139068453","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}
CytoskeletonPub Date : 2023-12-23DOI: 10.1002/cm.21823
Mohona Gupta, Gregory J. Pazour
{"title":"Intraflagellar transport: A critical player in photoreceptor development and the pathogenesis of retinal degenerative diseases","authors":"Mohona Gupta, Gregory J. Pazour","doi":"10.1002/cm.21823","DOIUrl":"10.1002/cm.21823","url":null,"abstract":"<p>In vertebrate vision, photons are detected by highly specialized sensory cilia called outer segments. Photoreceptor outer segments form by remodeling the membrane of a primary cilium into a stack of flattened disks. Intraflagellar transport (IFT) is critical to the formation of most types of eukaryotic cilia including the outer segments. This review covers the state of knowledge of the role of IFT in the formation and maintenance of outer segments and the human diseases that result from mutations in genes encoding the IFT complex and associated motors.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 11","pages":"556-568"},"PeriodicalIF":2.4,"publicationDate":"2023-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11193844/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138886785","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}
CytoskeletonPub Date : 2023-12-21DOI: 10.1002/cm.21822
Khalid Iqbal
{"title":"Tau and Alzheimer's disease: Past, present and future","authors":"Khalid Iqbal","doi":"10.1002/cm.21822","DOIUrl":"10.1002/cm.21822","url":null,"abstract":"<p>My journey with tau started when in 1974 for the first time I isolated neurofibrillary tangles of paired helical filaments (PHFs) from autopsied Alzheimer's disease (AD) brains and discovered that they were made up of a ~50–70 KDa protein on SDS-polyacrylamide gels. Subsequently my team discovered that this PHF protein and the microtubule-associated factor called tau were one and the same protein. However, we found that tau in neurofibrillary tangles/PHFs in AD brain was abnormally hyperphosphorylated, and unlike normal tau, which promoted the assembly of tubulin into microtubules, the AD-hyperphosphorylated tau inhibited microtubule assembly. These discoveries of tau pathology in AD opened a new and a major area of research on tau and on the molecular pathology of this major cause of dementia in middle- and old-age individuals. Tau pathology, which without fail is made up of the aggregated hyperphosphorylated state of the protein, is also the hallmark lesion of a family of around 20 related neurodegenerative diseases, called tauopathies. Currently, tau pathology is a major drug target for the treatment of AD and related tauopathies. Both active and passive tau immunization human clinical trials at various stages are underway. Initial results range from negative to partially promising. Future studies will reveal whether tau therapy alone or in combination with drugs targeting Aβ and/or neurodegeneration will be required to achieve the most effective treatment for AD and related disorders.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 1","pages":"116-121"},"PeriodicalIF":2.9,"publicationDate":"2023-12-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21822","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138833310","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}
CytoskeletonPub Date : 2023-12-16DOI: 10.1002/cm.21815
Thomas Fath, Vladimir Sytnyk, Ramón Martínez-Mármol
{"title":"‘10th cell architecture in development and disease (CADD)’: Meeting report","authors":"Thomas Fath, Vladimir Sytnyk, Ramón Martínez-Mármol","doi":"10.1002/cm.21815","DOIUrl":"10.1002/cm.21815","url":null,"abstract":"","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 6-7","pages":"264-265"},"PeriodicalIF":2.9,"publicationDate":"2023-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138685721","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}
CytoskeletonPub Date : 2023-12-16DOI: 10.1002/cm.21820
Nicholas M. Kanaan
{"title":"Tau here, tau there, tau almost everywhere: Clarifying the distribution of tau in the adult CNS","authors":"Nicholas M. Kanaan","doi":"10.1002/cm.21820","DOIUrl":"10.1002/cm.21820","url":null,"abstract":"<p>The microtubule-associated protein tau has gained significant attention over the last several decades primarily due to its apparent role in the pathogenesis of several diseases, most notably Alzheimer's disease. While the field has focused largely on tau's potential contributions to disease mechanisms, comparably less work has focused on normal tau physiology. Moreover, as the field has grown, some misconceptions and dogmas regarding normal tau physiology have become engrained in the traditional narrative. Here, one of the most common misconceptions regarding tau, namely its normal cellular/subcellular distribution in the CNS, is discussed. The literature describing the presence of tau in neuronal somata, dendrites, axons and synapses, as well as in glial cells is described. The origins for the erroneous description of tau as an “axon-specific,” “axon-enriched” and/or “neuron-specific” protein are discussed as well. The goal of this work is to help address these specific dogmatic misconceptions and provide a concise description of tau's normal cellular/subcellular localization in the adult CNS. This information can help refine our collective understanding of- and hypotheses about tau biology and pathobiology.</p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 1","pages":"107-115"},"PeriodicalIF":2.9,"publicationDate":"2023-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21820","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138685549","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}
CytoskeletonPub Date : 2023-12-16DOI: 10.1002/cm.21825
{"title":"Back Cover Image","authors":"","doi":"10.1002/cm.21825","DOIUrl":"https://doi.org/10.1002/cm.21825","url":null,"abstract":"<p>ON THE BACK COVER: The cell expresses both GFP-α-tubulin (green) and mRFP-myosin II (red). It divides into nucleate and anucleate fragments with myosin II (red) accumulating at centrosome furrows. Centrosomes are crucial for furrow positioning, while the spindle or nucleus is not essential.</p><p>Credit: Shigehiko Yumura, Emeritus Professor, Graduate School of Sciences and Technology for Innovation, Yamaguchi University\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure></p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"80 11-12","pages":"C4"},"PeriodicalIF":2.9,"publicationDate":"2023-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21825","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138679032","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}
CytoskeletonPub Date : 2023-12-16DOI: 10.1002/cm.21817
Paul Trevorrow, Douglas N. Robinson
{"title":"An interview with Douglas N. Robinson—Johns Hopkins School of Medicine, Baltimore, Maryland, USA","authors":"Paul Trevorrow, Douglas N. Robinson","doi":"10.1002/cm.21817","DOIUrl":"10.1002/cm.21817","url":null,"abstract":"","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"81 6-7","pages":"266-268"},"PeriodicalIF":2.9,"publicationDate":"2023-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138813570","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}
CytoskeletonPub Date : 2023-12-16DOI: 10.1002/cm.21824
{"title":"Front Cover Image","authors":"","doi":"10.1002/cm.21824","DOIUrl":"https://doi.org/10.1002/cm.21824","url":null,"abstract":"<p>ON THE FRONT COVER: Confocal image of the central quail myotube expressing mNeonGreen fluorescent protein linked to muscle myosin light chain 2 (green) and stained with phalloidin (red) reveals the premyofibrils, nascent and mature myofibrils extending in order from the extending edge during myofibrillogenesis.</p><p>Credit: Jushuo Wang, Department of Cell and Developmental Biology, SUNY Upstate Medical University.\u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure></p>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"80 11-12","pages":"C1"},"PeriodicalIF":2.9,"publicationDate":"2023-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/cm.21824","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138679030","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}