Cytoskeletal proteins articles within Nature Communications

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  • Article
    | Open Access

    F-actin architecture modulates transmission and generation of stresses in cells, yet its impact on myosin ATP hydrolysis remains unknown. The authors perform experiments measuring myosin ATP hydrolysis rates, showing that F-actin architecture can control myosin energy consumption.

    • Ryota Sakamoto
    •  & Michael P. Murrell

  • Article
    | Open Access

    Integrated structural data show that the MAP7 microtubule binding domain stabilizes the microtubule lattice through binding along protofilaments. Both strong and weak interactions between MAP7 and the lattice extend beyond a single tubulin dimer and include the tubulin C-terminal tails.

    • Agnes Adler
    • , Mamata Bangera
    •  & Marc Baldus

  • Article
    | Open Access

    TPX2 is a key factor stimulating branching microtubule (MT) nucleation. TPX2 forms condensates on MTs critical for branching. In this work, the authors report the atomic-level structure of TPX2 C-terminal minimal active domain on MT lattice and its binding interface, determined by magic-angle-spinning NMR.

    • Changmiao Guo
    • , Raymundo Alfaro-Aco
    •  & Tatyana Polenova

  • Comment
    | Open Access

    Cell division critically requires amplification of microtubules (MTs) in the bipolar mitotic spindle. This relies on the filamentous augmin complex that enables MT branching. Studies by Gabel et al., Zupa et al. and Travis et al. describe consistent integrated atomic models of the extraordinarily flexible augmin complex. Their work prompts the question: what is this flexibility really needed for?

    • Szymon W. Manka

  • Article
    | Open Access

    Many microtubules in the mitotic spindle are made through microtubule branching. Here, the authors report a structural model of the augmin complex and insights into its role in microtubule branching.

    • Sophie M. Travis
    • , Brian P. Mahon
    •  & Sabine Petry

  • Article
    | Open Access

    While the impact of F-actin architecture on stress transmission is well studied, the role of architecture on stress generation remains unclear. Here authors use in vitro model and show that distinct organizations constrain myosin motion.

    • Camelia G. Muresan
    • , Zachary Gao Sun
    •  & Michael P. Murrell

  • Article
    | Open Access

    In this work the authors report the structure of nucleotide-free kinesin-1 motor domain (apo-KIF5B) in complex with paclitaxel-stabilized microtubules using magic-angle-spinning (MAS) NMR spectroscopy. The study provides insights into the dynamic changes under which the neck linker goes upon binding to ADP.

    • Chunting Zhang
    • , Changmiao Guo
    •  & Tatyana Polenova

  • Article
    | Open Access

    The formation of branched microtubule networks in mitotic spindles depends on the augmin complex. Zupa, Würtz et al. elucidate the molecular architecture and conformational plasticity of the augmin complex using integrative structural biology, providing structural insights into microtubule branching.

    • Erik Zupa
    • , Martin Würtz
    •  & Stefan Pfeffer

  • Article
    | Open Access

    The eight-subunit augmin complex is required to nucleate branching microtubules and create a robust mitotic spindle during cell division. Here, the authors use cryo-EM, crosslinking mass spectrometry, and computational tools to build a structural model of the human augmin complex.

    • Clinton A. Gabel
    • , Zhuang Li
    •  & Leifu Chang

  • Article
    | Open Access

    Release of the ATP hydrolysis product orthophosphate (Pi) from the myosin active site is central in force generation but is poorly understood. Here, Moretto et al. present evidence for multistep Pi-release reconciling apparently contradictory results.

    • Luisa Moretto
    • , Marko Ušaj
    •  & Alf Månsson

  • Article
    | Open Access

    In E. coli, FtsA and FtsZ control the place and time of cell division. Here, the authors use in vitro experiments to show how FtsA can follow FtsZ treadmilling and that downstream proteins form dynamic copolymers with FtsA to initiate division.

    • Philipp Radler
    • , Natalia Baranova
    •  & Martin Loose

  • Article
    | Open Access

    Despite their relevance as regulators of actin severing and filament disassembly, few structural insights into the mechanism of cofilin-isoform-specific severing activity are reported. Here, the authors provide structural insights towards actin severing activity by human cofilin-2 obtained by MAS NMR and all-atom MD simulations. The results reveal an isoform-specific binding mode unique to CFL2 that may be related to its potent severing properties in-vivo.

    • Jodi Kraus
    • , Ryan W. Russell
    •  & Tatyana Polenova

  • Article
    | Open Access

     The Arp2/3 complex inhibitor Arpin controls cell migration by interrupting a feedback loop involving Rac-WAVE-Arp2/3 complex Here, the authors use structural, biochemical, and cellular studies to reveal Arpin’s mechanism of inhibition.

    • Fred E. Fregoso
    • , Trevor van Eeuwen
    •  & Roberto Dominguez

  • Article
    | Open Access

    Cancer cells proliferate and invade via cytoskeletal proteins such as WASp, exclusively expressed in hematopoietic cells. Here the authors show a specific small molecule compound inhibiting cancer cell activity by WASp degradation and demonstrating its therapeutic potential in vitro and in vivo.

    • Guy Biber
    • , Aviad Ben-Shmuel
    •  & Mira Barda-Saad

  • Article
    | Open Access

    The assembly of branched actin networks depends on the heterodimeric capping protein CP/CapZ. Combining cryoEM, in vitro reconstitution and cell biological assays, the authors show that CP not only prevents actin filament elongation but also selectively masks actin filament ends to promote nucleation.

    • Johanna Funk
    • , Felipe Merino
    •  & Peter Bieling

  • Article
    | Open Access

    Existing methods for multimeric protein complex quantification in single cells suffer from limited selectivity and sensitivity. Here the authors report Single-cell protein Interaction Fractionation Through Electrophoresis and immunoassay Readout (SIFTER) and use this to probe the effects of cellular stress.

    • Julea Vlassakis
    • , Louise L. Hansen
    •  & Amy E. Herr

  • Article
    | Open Access

    Mutations in the LaminA gene are the second most common inherited cause of Dilated Cardiomyopathy, a major form of heart failure. Here the authors show that disruption of the nuclear protein SUN1 in cardiomyocytes, by AAV mediated transduction of a SUN1 inhibitor, significantly suppress cardiomyopathy progression, providing a potential therapeutic route to treat this disease.

    • Ruth Jinfen Chai
    • , Hendrikje Werner
    •  & Colin L. Stewart

  • Article
    | Open Access

    Mitochondrial transport toward both the plus- and minus-ends of microtubules is mediated by motor proteins linked to mitochondria by TRAK adaptor proteins. Here the authors investigate the role of TRAK2 as a bidirectional motor adaptor, and propose a model where TRAK2 coordinates the activities of opposing kinesin-1 and cytoplasmic dynein motors as a single interdependent motor complex.

    • Adam R. Fenton
    • , Thomas A. Jongens
    •  & Erika L. F. Holzbaur

  • Article
    | Open Access

    Calcium signals initiated by IP3 receptors in ER membranes regulate most cellular activities. Here, the authors show that KRas-induced actininteracting protein (KRAP) tethers a small subset of IP3 receptors to actin and licenses them to evoke cytosolic calcium signals.

    • Nagendra Babu Thillaiappan
    • , Holly A. Smith
    •  & Colin W. Taylor

  • Article
    | Open Access

    Intracellular trafficking of organelles is driven by kinesin-1 stepping along microtubules, but crowding conditions impede kinesin-1 motility. Here authors demonstrate that TRAK1, an adaptor protein essential for mitochondrial trafficking, activates kinesin-1 and increases robustness of kinesin-1 stepping on crowded microtubule surfaces.

    • Verena Henrichs
    • , Lenka Grycova
    •  & Zdenek Lansky

  • Article
    | Open Access

    The mechanisms of Z-ring assembly and regulation in bacteria are poorly understood, particularly in non-model organisms. Here, Sogues et al. study the interaction between FtsZ and SepF in Corynebacterium glutamicum, showing an essential interdependence of these proteins for formation of a functional Z-ring.

    • Adrià Sogues
    • , Mariano Martinez
    •  & Pedro M. Alzari

  • Article
    | Open Access

    The cofilin family proteins are actin disassembly factors but the disassembly mechanism is poorly understood. Here authors show that cyclase-associated-protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold and reveal how CAP destabilizes the interface between terminal actin subunits.

    • Tommi Kotila
    • , Hugo Wioland
    •  & Pekka Lappalainen

  • Article
    | Open Access

    Lamin A is critical for nuclear architecture but its structure and assembly are not fully understood. Here, the authors use quantitative cross-linking mass spectrometry to map intra- and intermolecular interactions within lamin homomers, providing insights into the molecular basis for lamin’s mechanical properties.

    • Alex A. Makarov
    • , Juan Zou
    •  & Eric C. Schirmer

  • Article
    | Open Access

    The kinesin-3 KIF1C transports dense core vesicles in neurons and delivers integrins to cell adhesions sites. Here the authors show that KIF1C's autoinhibitory interactions are released upon binding of protein tyrosine phosphatase PTPN21 or cargo adapter Hook3 resulting in cargo-activated transport.

    • Nida Siddiqui
    • , Alexander James Zwetsloot
    •  & Anne Straube

  • Article
    | Open Access

    Collagen proteins assemble into trimers from distinct monomers with high specificity, yet the molecular basis for this specificity remains unclear. Here the authors demonstrate the crucial role of conserved C-terminal domain cysteine residues and calcium in homotrimeric procollagen assembly.

    • Andrew S. DiChiara
    • , Rasia C. Li
    •  & Matthew D. Shoulders

  • Article
    | Open Access

    The kinesin-13 family of microtubule (MT) depolymerases are major regulators of MT dynamics. Here the authors provide insights into the MT depolymerization mechanism by solving the crystal structure of a kinesin-13 monomer (Kif2A) in complex with two bent αβ-tubulin heterodimers.

    • Daria Trofimova
    • , Mohammadjavad Paydar
    •  & John S. Allingham

  • Article
    | Open Access

    Cofilin is a small actin-binding protein that accelerates actin turnover by disassembling actin filaments. Here the authors present the 3.8 Å cryo-EM structure of a cofilin-decorated actin filament and discuss mechanistic implications.

    • Kotaro Tanaka
    • , Shuichi Takeda
    •  & Akihiro Narita

  • Article
    | Open Access

    Motor and non-motor microtubule-associated proteins (MAPs) bind to the microtubule lattice, but it is unclear how their binding activities are coordinated and how this impacts motor transport. Here the authors show how MAP competition controls microtubule access to determine the distribution and balance of motor activity.

    • Brigette Y. Monroy
    • , Danielle L. Sawyer
    •  & Kassandra M. Ori-McKenney

  • Article
    | Open Access

    The actomyosin cytoskeleton plays an important role in polarised cell migration. Here the authors identify lymphocyte-specific protein (LSP)-1 as a regulator of actomyosin contractility in macrophages, by competing with supervillin for myosin IIA activators acting specifically on the β-actin isoform.

    • Pasquale Cervero
    • , Christiane Wiesner
    •  & Stefan Linder

  • Article
    | Open Access

    MICAL Redox enzymes post-translationally modify F-actin to promote its cellular destabilization. Here, the authors present a 3.9Å cryoEM structure of Mical-oxidized F-actin, showing its nucleotide-state dependent dynamic instability and susceptibility to cofilin-induced severing in the presence of inorganic phosphate.

    • Elena E. Grintsevich
    • , Peng Ge
    •  & Emil Reisler

  • Article
    | Open Access

    Microtubules are vital and highly conserved components of the cytoskeleton. Here the authors carry out a structural analysis of fission yeast microtubules in the presence and absence of the microtubule end-binding protein Mal3 that demonstrates structural plasticity amongst microtubule polymers.

    • Ottilie von Loeffelholz
    • , Neil A. Venables
    •  & Carolyn A. Moores

  • Article
    | Open Access

    Myosin VI (MVI) is known to interact with RNA Polymerase II and to play non-cytoplasmic roles in cells. Here, the authors provide evidence that the transcription co-activator NDP52 regulates MVI binding to DNA and that MVI interacts with nuclear receptors to drive gene expression.

    • Natalia Fili
    • , Yukti Hari-Gupta
    •  & Christopher P. Toseland

  • Article
    | Open Access

    Cilia are hair-like appendages involved in cell motility and sensory reception. Here, the authors report a high resolution cryo-EM structure of the microtubule doublet from motile cilia and identify microtubule inner proteins (MIPs) bound to the inner surface of the doublet that appear to stabilize its structure.

    • Muneyoshi Ichikawa
    • , Dinan Liu
    •  & Khanh Huy Bui

  • Article
    | Open Access

    Microtubule assembly and disassembly is the target of many anticancer therapies, with β-tubulin the most-frequent target. Here, the authors used biochemical and biophysical techniques to demonstrate pironetin binds to α-tubulin and thereby inhibits microtubule polymerization providing a basis for the rational design of novel anticancer drugs.

    • Jianhong Yang
    • , Yuxi Wang
    •  & Lijuan Chen

  • Article
    | Open Access

    Centralspindlin consists of dimeric kinesin-6 and dimeric RacGAP, and is involved in the organization of anaphase midzone microtubules. Here, the authors show that the RacGAP is needed for motor activity at the plus-end of microtubules, but not for the bundling activity associated with kinesin-6.

    • Li Tao
    • , Barbara Fasulo
    •  & William Sullivan

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