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Sarcomeric tropomyosin expression during human iPSC differentiation into cardiomyocytes Cytoskeleton (IF 2.9) Pub Date : 2024-03-12 Dipak K. Dube, Syamalima Dube, Huaiyu Shi, Patricia Benz, Samender Randhawa, Yingli Fan, Jusuo Wang, Zhen Ma, Joseph W. Sanger, Jean M. Sanger, Bernard J. Poiesz
Tropomyosin (TPM) is an essential sarcomeric component, stabilizing the thin filament and facilitating actin's interaction with myosin. In mammals, including humans, there are four TPM genes (TPM1, TPM2, TPM3, and TPM4) each of which generates a multitude of TPM isoforms via alternative splicing and using different promoters. In this study, we have examined the expression of transcripts as well as
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Biochemical characterization of cardiac α‐actin mutations A21V and D26N implicated in hypertrophic cardiomyopathy Cytoskeleton (IF 2.9) Pub Date : 2024-03-09 Johannes N. Greve, Frederic V. Schwäbe, Manuel H. Taft, Dietmar J. Manstein
Familial hypertrophic cardiomyopathy (HCM) affects .2% of the world's population and is inherited in an autosomal dominant manner. Mutations in cardiac α‐actin are the cause in 1%–5% of all observed cases. Here, we describe the recombinant production, purification, and characterization of the HCM‐linked cardiac α‐actin variants p.A21V and p.D26N. Mass spectrometric analysis of the initially purified
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Distribution and bulk flow analyses of the intraflagellar transport (IFT) motor kinesin‐2 support an “on‐demand” model for Chlamydomonas ciliary length control Cytoskeleton (IF 2.9) Pub Date : 2024-03-08 Mansi B. Patel, Paul J. Griffin, Spencer F. Olson, Jin Dai, Yuqing Hou, Tara Malik, Poulomi Das, Gui Zhang, Winston Zhao, George B. Witman, Karl F. Lechtreck
Most cells tightly control the length of their cilia. The regulation likely involves intraflagellar transport (IFT), a bidirectional motility of multi‐subunit particles organized into trains that deliver building blocks into the organelle. In Chlamydomonas, the anterograde IFT motor kinesin‐2 consists of the motor subunits FLA8 and FLA10 and the nonmotor subunit KAP. KAP dissociates from IFT at the
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Myosin‐induced F‐actin fragmentation facilitates contraction of actin networks Cytoskeleton (IF 2.9) Pub Date : 2024-03-08 Kyohei Matsuda, Wonyeong Jung, Yusei Sato, Takuya Kobayashi, Masahiko Yamagishi, Taeyoon Kim, Junichiro Yajima
Mechanical forces play a crucial role in diverse physiological processes, such as cell migration, cytokinesis, and morphogenesis. The actin cytoskeleton generates a large fraction of the mechanical forces via molecular interactions between actin filaments (F‐actins) and myosin motors. Recent studies have shown that the common tendency of actomyosin networks to contract into a smaller structure deeply
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Microtubule length correlates with spindle length in C. elegans meiosis Cytoskeleton (IF 2.9) Pub Date : 2024-03-07 Vitaly Zimyanin, Stefanie Redemann
The accurate segregation of chromosomes during female meiosis relies on the precise assembly and function of the meiotic spindle, a dynamic structure primarily composed of microtubules. Despite the crucial role of microtubule dynamics in this process, the relationship between microtubule length and spindle size remains elusive. Leveraging Caenorhabditis elegans as a model system, we combined electron
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Temperature‐dependent augmentation of ciliary motility by the TRP2 channel in Chlamydomonas reinhardtii Cytoskeleton (IF 2.9) Pub Date : 2024-03-01 Shunta Fueki, Taro Kaneko, Haruka Matsuki, Yuki Hashimoto, Megumi Yoshida, Atsuko Isu, Ken‐ichi Wakabayashi, Kenjiro Yoshimura
Temperature is a critical factor for living organisms. Many microorganisms migrate toward preferable temperatures, and this behavior is called thermotaxis. In this study, the molecular and physiological bases for thermotaxis are examined in Chlamydomonas reinhardtii. A mutant with knockout of a transient receptor potential (TRP) channel, trp2‐3, showed defective thermotaxis. The swimming velocity and
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The ability of the LIMD1 and TRIP6 LIM domains to bind strained f‐actin is critical for their tension dependent localization to adherens junctions and association with the Hippo pathway kinase LATS1 Cytoskeleton (IF 2.9) Pub Date : 2024-03-01 Samriddha Ray, Chamika DeSilva, Ishani Dasgupta, Sebastian Mana‐Capelli, Natasha Cruz‐Calderon, Dannel McCollum
A key step in regulation of Hippo pathway signaling in response to mechanical tension is recruitment of the LIM domain proteins TRIP6 and LIMD1 to adherens junctions. Mechanical tension also triggers TRIP6 and LIMD1 to bind and inhibit the Hippo pathway kinase LATS1. How TRIP6 and LIMD1 are recruited to adherens junctions in response to tension is not clear, but previous studies suggested that they
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Sequences in the myosin A rod interact with UNC‐89/obscurin and the zinc‐finger protein UNC‐98 during thick filament assembly and M‐line formation in C. elegans striated muscle Cytoskeleton (IF 2.9) Pub Date : 2024-02-24 Sarah A. Almuhanna, Humayra Z. Oishi, Kar Men Lee, Pamela E. Hoppe
The M‐line of striated muscle is a complex structure that anchors myosin‐containing thick filaments and also participates in signaling and proteostasis. While the physical associations among many M‐line components have been defined, the mechanism of thick filament attachment is not completely understood. In Caenorhabditis elegans, myosin A is essential for viability and forms the site of M‐line attachment
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Metastasis‐associated 1 localizes to the sarcomeric Z‐disc and is implicated in skeletal muscle pathology Cytoskeleton (IF 2.9) Pub Date : 2024-02-23 Hongsheng Xue, Li Han, Haidi Sun, Zhe Piao, Wenjun Cao, Haili Qian, Zhilong Zhao, Ming‐Fei Lang, Chundong Gu
Metastasis‐associated 1 (MTA1), a subunit of the nucleosome remodeling and histone deacetylation (NuRD) corepressor complex, was reported to be expressed in the cytoplasm of skeletal muscles. However, the exact subcellular localization and the functional implications of MTA1 in skeletal muscles have not been examined. This study aims to demonstrate the subcellular localization of MTA1 in skeletal muscles
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Ionic strength alters crosslinker‐driven self‐organization of microtubules Cytoskeleton (IF 2.9) Pub Date : 2024-02-22 Prashali Chauhan, Hong Beom Lee, Niaz Goodbee, Sophia Martin, Ruell Branch, Sumon Sahu, Jennifer M. Schwarz, Jennifer L. Ross
The microtubule cytoskeleton is a major structural element inside cells that directs self‐organization using microtubule‐associated proteins and motors. It has been shown that finite‐sized, spindle‐like microtubule organizations, called “tactoids,” can form in vitro spontaneously from mixtures of tubulin and the antiparallel crosslinker, MAP65, from the MAP65/PRC1/Ase family. Here, we probe the ability
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Microstructure-based nuclear lamina constitutive model Cytoskeleton (IF 2.9) Pub Date : 2024-02-12 Nima Mostafazadeh, Zhangli Peng
The nuclear lamina is widely recognized as the most crucial component in providing mechanical stability to the nucleus. However, it is still a significant challenge to model the mechanics of this multilayered protein network. We developed a constitutive model of the nuclear lamina network based on its microstructure, which accounts for the deformation phases at the dimer level, as well as the orientational
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Rearrangement of GUV-confined actin networks in response to micropipette aspiration Cytoskeleton (IF 2.9) Pub Date : 2024-02-07 Nadab H. Wubshet, Cole J. Young, Allen P. Liu
Although diverse actin network architectures found inside the cell have been individually reconstituted outside of the cell, how different types of actin architectures reorganize under applied forces is not entirely understood. Recently, bottom-up reconstitution has enabled studies where dynamic and phenotypic characteristics of various actin networks can be recreated in an isolated cell-like environment
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Topographical depth reveals contact guidance mechanism distinct from focal adhesion confinement Cytoskeleton (IF 2.9) Pub Date : 2024-01-16 Michael C. Robitaille, Chunghwan Kim, Joseph A. Christodoulides, Patrick J. Calhoun, Wonmo Kang, Jinny Liu, Jeff M. Byers, Marc P. Raphael
Cellular response to the topography of their environment, known as contact guidance, is a crucial aspect to many biological processes yet remains poorly understood. A prevailing model to describe cellular contact guidance involves the lateral confinement of focal adhesions (FA) by topography as an underlying mechanism governing how cells can respond to topographical cues. However, it is not clear how
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Assembly of FAP93 at the proximal axoneme in Chlamydomonas cilia Cytoskeleton (IF 2.9) Pub Date : 2024-01-15 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
To identify proteins specific to the proximal ciliary axoneme, we used iTRAQ to compare short (~2 μm) and full-length (~11 μm) axonemes of Chlamydomonas. Known compoents 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
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Duchenne and Becker muscular dystrophy: Cellular mechanisms, image analysis, and computational models: A review Cytoskeleton (IF 2.9) Pub Date : 2024-01-15 J. F. Escobar-Huertas, Juan Jairo Vaca-González, Johana María Guevara, Angelica M. Ramirez-Martinez, Olfa Trabelsi, D. A. Garzón-Alvarado
The muscle is the principal tissue that is capable to transform potential energy into kinetic energy. This process is due to the transformation of chemical energy into mechanical energy to enhance the movements and all the daily activities. However, muscular tissues can be affected by some pathologies associated with genetic alterations that affect the expression of proteins. As the muscle is a highly
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Functional and structural significance of the inner-arm-dynein subspecies d in ciliary motility Cytoskeleton (IF 2.9) Pub Date : 2024-01-12 Ryosuke Yamamoto, Takahide Kon
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
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Titin takes centerstage among cytoskeletal contributions to myocardial passive stiffness Cytoskeleton (IF 2.9) Pub Date : 2023-12-29 Christine M. Loescher, Wolfgang A. Linke
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
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Intraflagellar transport: A critical player in photoreceptor development and the pathogenesis of retinal degenerative diseases Cytoskeleton (IF 2.9) Pub Date : 2023-12-23 Mohona Gupta, Gregory J. Pazour
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
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Myosin 1e deficiency affects migration of 4T1 breast cancer cells Cytoskeleton (IF 2.9) Pub Date : 2023-12-23 Michael E. Garone, Sharon E. Chase, Chunling Zhang, Mira Krendel
Metastasis of breast cancer cells to distant tissue sites is responsible for the majority of deaths associated with breast cancer. Previously we have examined the role of class I myosin motor protein, myosin 1e (myo1e), in cancer metastasis using the Mouse Mammary Tumor Virus-Polyoma Middle T Antigen (MMTV-PyMT) mouse model. Mice deficient in myo1e formed tumors with a more differentiated phenotype
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Tau and Alzheimer's disease: Past, present and future Cytoskeleton (IF 2.9) Pub Date : 2023-12-21 Khalid Iqbal
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.
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‘10th cell architecture in development and disease (CADD)’: Meeting report Cytoskeleton (IF 2.9) Pub Date : 2023-12-16 Thomas Fath, Vladimir Sytnyk, Ramón Martínez-Mármol
CONFLICT OF INTEREST STATEMENT The author declares no conflict of interest.
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Tau here, tau there, tau almost everywhere: Clarifying the distribution of tau in the adult CNS Cytoskeleton (IF 2.9) Pub Date : 2023-12-16 Nicholas M. Kanaan
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
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The cilium like region of the Drosophila bifurca spermatocyte: Elongation of a giant axoneme without intraflagellar transport Cytoskeleton (IF 2.9) Pub Date : 2023-12-10 Maria Giovanna Riparbelli, Ambra Pratelli, Giuliano Callaini
The growth of the ciliary axonemes mainly depends on the evolutionary conserved intraflagellar transport (IFT) machinery. However, insect spermatocytes are characterized by cilium-like regions (CLRs) that elongate in the absence of IFT. It is generally believed that the dynamics of these structures relies on the free diffusion of soluble tubulin from the cytoplasm. However, this passive process could
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Tau and neurodegeneration Cytoskeleton (IF 2.9) Pub Date : 2023-12-10 Michel Goedert, R. Anthony Crowther, Sjors H. W. Scheres, Maria Grazia Spillantini
First identified in 1975, tau was implicated in Alzheimer's disease 10 years later. Filamentous tangle inclusions were known to be made of hyperphosphorylated tau by 1991, with similar inclusions gaining recognition for being associated with other neurodegenerative diseases. In 1998, mutations in MAPT, the gene that encodes tau, were identified as the cause of a dominantly inherited form of frontotemporal
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Cevipabulin induced abnormal tubulin protofilaments polymerization by binding to Vinblastine site and The Seventh site Cytoskeleton (IF 2.9) Pub Date : 2023-12-05 Peng Bai, Wei Yan, Jianhong Yang
Microtubules, composed of αβ-tubulin heterodimers, are crucial targets for chemotherapeutic agents and possess eight binding sites. Our previous study identified cevipabulin as the only one agent capable of simultaneously binding to two different sites (Vinblastine site and The Seventh site). Binding to The Seventh site by cevipabulin induces tubulin degradation. This study aimed to investigate whether
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Tau and signal transduction Cytoskeleton (IF 2.9) Pub Date : 2023-12-06 Gloria Lee
The discovery of tau by the Kirschner lab was based on its ability to associate with microtubules and to promote microtubule assembly (Weingarten et al., 1975). After the primary sequence of tau and MAP2 were reported and functional studies performed, it became clear that both proteins contained a similar microtubule binding domain in the carboxy terminal portion of the protein (Butner & Kirschner
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UNC-82/NUAK kinase is required by myosin A, but not myosin B, to assemble and function in the thick filament arms of C. elegans striated muscle Cytoskeleton (IF 2.9) Pub Date : 2023-11-20 NaTasha R. Schiller, Sarah A. Almuhanna, Pamela E. Hoppe
The mechanisms that ensure proper assembly, activity, and turnover of myosin II filaments are fundamental to a diverse range of cellular processes. In Caenorhabditis elegans striated muscle, thick filaments contain two myosins that are functionally distinct and spatially segregated. Using transgenic double mutants, we demonstrate that the ability of increased myosin A expression to restore muscle structure
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Emergence of diverse patterns driven by molecular motors in the motility assay Cytoskeleton (IF 2.9) Pub Date : 2023-11-10 Brandon Slater, Wonyeong Jung, Taeyoon Kim
Actomyosin contractility originating from interactions between F-actin and myosin motors in the actin cytoskeleton generates mechanical forces and drives a wide range of cellular processes including cell migration and cytokinesis. To probe the interactions between F-actin and myosin motors, the myosin motility assay has been popularly employed, which consists of myosin heads attached to a glass surface
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Travels with tau prions Cytoskeleton (IF 2.9) Pub Date : 2023-11-11 Marc I. Diamond
Tau was originally identified as a microtubule associated protein, and subsequently recognized to constitute the fibrillar assemblies found in Alzheimer disease and related neurodegenerative tauopathies. Point mutations in the microtubule associated protein tau (MAPT) gene cause dominantly inherited tauopathies, and most predispose it to aggregate. This indicates tau aggregation underlies pathogenesis
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Dehydroleucodine and xanthatin, two natural anti-inflammatory lactones, inhibit mast cell degranulation by affecting the actin cytoskeleton Cytoskeleton (IF 2.9) Pub Date : 2023-11-06 Paula A. Wetten, Andrea Celeste Arismendi Sosa, María Laura Mariani, Patricia M. Vargas, Marcela Alejandra Michaut, Alicia Beatriz Penissi
Actin remodeling is a critical regulator of mast cell secretion. In previous work, we have shown that dehydroleucodine and xanthatin, two natural α,β-unsaturated lactones, exhibit anti-inflammatory and mast cell stabilizing properties. Based on this background, this study aimed to determine whether the mast cell stabilizing action of these lactones is associated with changes in the actin cytoskeleton
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Mapping the cytoskeletal architecture of renal tubules and surrounding peritubular capillaries in the kidney Cytoskeleton (IF 2.9) Pub Date : 2023-11-08 Girishkumar Kaitholil Kumaran, Israel Hanukoglu
The human kidney includes ~1 million nephrons which are long U-shaped tubules with convoluted segments that serve as filtration units. During the passage of the ultrafiltrate through a nephron, electrolytes and nutrients are re-absorbed into peritubular capillaries. The fluid remaining in the distal end of the renal tubules flows through the collecting ducts into the ureter. In this study, we generated
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Regulation of mitochondrial structure by the actin cytoskeleton Cytoskeleton (IF 2.9) Pub Date : 2023-11-06 Yihe Wu, Xiaoyu Ren, Peng Shi, Congying Wu
Mitochondria are the powerhouse of the cell and play important roles in multiple cellular processes including cell metabolism, proliferation, and programmed cell death. Mitochondria are double-membrane organelles with the inner membrane folding inward to form cristae. Mitochondria networks undergo dynamic fission and fusion. Deregulation of mitochondrial structure has been linked to perturbed mitochondrial
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Evidence for microtubule nucleation at the Golgi in breast cancer cells Cytoskeleton (IF 2.9) Pub Date : 2023-10-31 Laura A. Zahn, Sarah Lundin-Schiller
Golgi-derived microtubule (MT) arrays are essential to directionally persistent cell migration and vesicle transport. In this study, we have examined MT nucleation sites in two breast cancer cell lines, MDA-MB-231 and MCF-7, with the hypothesis that only the migratory invasive MDA-MB-231 cells exhibit MTs originating from the Golgi. MTs were disassembled and allowed to slightly regrow so individual
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An interview with Shu Yao Leong-Winner of the Cytoskeleton best presentation prize at the European Plant Cytoskeleton Club, 29-30th June, 2023, Halle, Germany. Cytoskeleton (IF 2.9) Pub Date : 2023-10-19 Paul Trevorrow,Shu Yao Leong
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The fidgetin family: Shaking things up among the microtubule-severing enzymes Cytoskeleton (IF 2.9) Pub Date : 2023-10-12 Karishma Smart, David J. Sharp
The microtubule cytoskeleton is required for several crucial cellular processes, including chromosome segregation, cell polarity and orientation, and intracellular transport. These functions rely on microtubule stability and dynamics, which are regulated by microtubule-binding proteins (MTBPs). One such type of regulator is the microtubule-severing enzymes (MSEs), which are ATPases Associated with
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The discovery of tau protein Cytoskeleton (IF 2.9) Pub Date : 2023-10-12 Marc Kirschner
In January of this year I received an unexpected request from George Bloom to contribute an historical perspective on “the discovery of tau protein,” an event that occurred roughly 50 years ago. My first thought was that it could not have been that long ago, as the memories of what was my first independent scientific discovery are still fresh in my mind today. But 50 years is half a century and, as
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Tau: More than a microtubule-binding protein in neurons Cytoskeleton (IF 2.9) Pub Date : 2023-10-11 Alejandra del Carmen Alonso, Abdeslem El Idrissi, Robert Candia, Viktoriya Morozova, Frida Esther Kleiman
Tau protein was discovered as a microtubule-associated protein nearly 50 years ago, and our understanding of tau has revolved around that role. Even with tau's rise to stardom as a central player in neurodegenerative disease, therapeutic efforts have largely been targeted toward cytoskeletal changes. While some studies hinted toward non-cytoskeletal roles for tau, it is only fairly recently that these
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Reevaluating tau reduction as a therapeutic approach for tauopathies: Insights and perspectives Cytoskeleton (IF 2.9) Pub Date : 2023-10-11 Xiaohuan Sun, Victor C. Ogbolu, Peter W. Baas, Liang Qiang
Tau, one of the most abundant microtubule-associated protein in neurons plays a role in regulating microtubule dynamics in axons, as well as shaping the overall morphology of the axon. Recent studies challenge the traditional view of tau as a microtubule stabilizer and shed new light on the complexity of its role in regulating various properties of the microtubule. While reducing tau levels shows therapeutic
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Latrunculin resistance mechanism of non-conventional actin NAP1 uncovered by molecular dynamics simulations Cytoskeleton (IF 2.9) Pub Date : 2023-10-10 Rikuri Morita, Yasuteru Shigeta, Ryuhei Harada
Monomeric G-actin polymerizes into F-actin to perform various cellular functions. Actin depolymerization drugs, such as latrunculin-A (Lat-A), inhibit filament formation and disrupt the cytoskeleton. Interestingly, the green algae Chlamydomonas alternatively produces a non-conventional actin, NAP1, that responds to inhibition by latrunculin. However, the molecular mechanism underlying latrunculin resistance
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Sliding of antiparallel microtubules drives bipolarization of monoastral spindles Cytoskeleton (IF 2.9) Pub Date : 2023-10-09 James R. LaFountain Jr, Catherine E. Seaman, Christopher S. Cohan, Rudolf Oldenbourg
Time-lapse imaging with liquid crystal polarized light (LC-PolScope) and fluorescent speckle microscopy (FSM) enabled this study of spindle microtubules in monoastral spindles that were produced in crane-fly spermatocytes through flattening-induced centrosome displacement. Monoastral spindles are found in several other contexts: after laser ablation of one of a cell's two centrosomes (in the work of
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Genetic and sporadic forms of tauopathies—TAU as a disease driver for the majority of patients but the minority of tauopathies Cytoskeleton (IF 2.9) Pub Date : 2023-10-05 Hans Zempel
Ageing-associated tauopathies like frontotemporal dementia (FTD), variants thereof (like progressive supranuclear palsy (PSP), pick diseases (PiD), corticobasal degeneration (CBD)), and of course the most prevalent form of dementia, Alzheimer Disease (AD), are widely recognized forms of tauopathies. The list of tauopathies is expanding. We now include: (i) tauopathies where the disease cause or trigger
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Segregated localization of two calponin-related proteins within sarcomeric thin filaments in Caenorhabditis elegans striated muscle Cytoskeleton (IF 2.9) Pub Date : 2023-10-04 Shoichiro Ono
The calponin family proteins are expressed in both muscle and non-muscle cells and involved in the regulation of cytoskeletal dynamics and cell contractility. In the nematode Caenorhabditis elegans, UNC-87 and CLIK-1 are calponin-related proteins with 42% identical amino acid sequences containing seven calponin-like motifs. Genetic studies demonstrated that UNC-87 and CLIK-1 have partially redundant
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Tau and the hard problem faceoff Cytoskeleton (IF 2.9) Pub Date : 2023-09-29 Kenneth S. Kosik
Tau has attracted the attention of fundamental cell biologists for its control over microtubules and Alzheimer biologists for its tendency to form pathological inclusions. While an extensive and insightful literature exists on the tauopathies and vulnerable cell populations, we should acknowledge that a core problem remains—how the individually variable experience of dementia is embodied, how it is
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A-Band assembly in avian skeletal muscles observed with super-resolution microscopy Cytoskeleton (IF 2.9) Pub Date : 2023-09-28 Matthew Welchons, Jushuo Wang, Yingli Fan, Jean M. Sanger, Joseph W. Sanger
Myofibrils in vertebrate skeletal muscle are organized in aligned arrays of filaments formed from multiple protein components. Despite considerable information describing individual proteins, how they assemble de novo into mature myofibrils is still a challenge. Studies in our lab of sarcomeric protein localization during myofibril assembly led us to propose a three-step progression: premyofibrils
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Tau oligomerization on microtubules in health and disease. Cytoskeleton (IF 2.9) Pub Date : 2023-09-25 Kassandra M Ori-McKenney,Richard J McKenney
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