TY - JOUR A1 - Adamatzky, Andrew A1 - Schnauß, Jörg A1 - Huber, Florian T1 - Actin droplet machine JF - Royal Society Open Science N2 - The actin droplet machine is a computer model of a three-dimensional network of actin bundles developed in a droplet of a physiological solution, which implements mappings of sets of binary strings. The actin bundle network is conductive to travelling excitations, i.e. impulses. The machine is interfaced with an arbitrary selected set of k electrodes through which stimuli, binary strings of length k represented by impulses generated on the electrodes, are applied and responses are recorded. The responses are recorded in a form of impulses and then converted to binary strings. The machine's state is a binary string of length k: if there is an impulse recorded on the ith electrode, there is a '1' in the ith position of the string, and '0' otherwise. We present a design of the machine and analyse its state transition graphs. We envisage that actin droplet machines could form an elementary processor of future massive parallel computers made from biopolymers. Y1 - 2019 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:hbz:due62-opus-34675 UR - http://www.ncbi.nlm.nih.gov/pubmed/31903204 SN - 2054-5703 N1 - A.A. was partially supported by EPSRC grant no. EP/P016677/1. The authors declare that they have no competing interests. VL - 6 IS - 12 PB - Royal Soc. Publ. ER - TY - JOUR A1 - Adamatzky, Andrew A1 - Huber, Florian A1 - Schnauß, Jörg T1 - Computing on actin bundles network JF - Scientific Reports N2 - Actin filaments are conductive to ionic currents, mechanical and voltage solitons. These travelling localisations can be utilised to generate computing circuits from actin networks. The propagation of localisations on a single actin filament is experimentally unfeasible to control. Therefore, we consider excitation waves propagating on bundles of actin filaments. In computational experiments with a two-dimensional slice of an actin bundle network we show that by using an arbitrary arrangement of electrodes, it is possible to implement two-inputs-one-output circuits. Y1 - 2019 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:hbz:due62-opus-34665 UR - http://www.ncbi.nlm.nih.gov/pubmed/31685834 SN - 2045-2322 VL - 9 IS - 1 PB - Springer Nature ER - TY - JOUR A1 - Migueles, Jairo H. A1 - Rowlands, Alex V. A1 - Huber, Florian A1 - Sabia, Séverine A1 - van Hees, Vincent T. T1 - GGIR: A Research Community–Driven Open Source R Package for Generating Physical Activity and Sleep Outcomes From Multi-Day Raw Accelerometer Data JF - Journal for the Measurement of Physical Behaviour Y1 - 2019 U6 - https://doi.org/10.1123/jmpb.2018-0063 SN - 2575-6605 VL - 2 IS - 3 SP - 188 EP - 196 PB - Human Kinetics ER - TY - JOUR A1 - Beniddir, Mehdi A. A1 - Kang, Kyo Bin A1 - Genta-Jouve, Grégory A1 - Huber, Florian A1 - Rogers, Simon A1 - van der Hooft, Justin J. J. T1 - Advances in decomposing complex metabolite mixtures using substructure- and network-based computational metabolomics approaches JF - Natural Product Reports Y1 - 2021 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:hbz:due62-opus-34772 SN - 1460-4752 VL - 38 IS - 11 SP - 1967 EP - 1993 PB - The Royal Society of Chemistry ER - TY - JOUR A1 - Huber, Florian A1 - Strehle, Dan A1 - Schnauß, Jörg A1 - Käs, Josef T1 - Formation of regularly spaced networks as a general feature of actin bundle condensation by entropic forces JF - New Journal of Physics KW - DOAJ Y1 - 2015 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:hbz:due62-opus-34833 SN - 1367-2630 VL - 17 IS - 4 PB - IOP Publishing ER - TY - JOUR A1 - Huber, Florian A1 - Verhoeven, Stefan A1 - Meijer, Christiaan A1 - Spreeuw, Hanno A1 - Castilla, Efraín A1 - Geng, Cunliang A1 - van der Hooft, Justin J. J. A1 - Rogers, Simon A1 - Belloum, Adam A1 - Diblen, Faruk A1 - Spaaks, Jurriaan H. T1 - matchms - processing and similarity evaluation of mass spectrometry data JF - Journal of Open Source Software KW - DOAJ Y1 - 2020 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:hbz:due62-opus-34856 SN - 2475-9066 VL - 5 IS - 52 PB - Cold Spring Harbor Laboratory ER - TY - JOUR A1 - Huber, Florian A1 - Käs, Josef A1 - Stuhrmann, Björn T1 - Growing actin networks form lamellipodium and lamellum by self-assembly JF - Biophysical Journal N2 - Many different cell types are able to migrate by formation of a thin actin-based cytoskeletal extension. Recently, it became evident that this extension consists of two distinct substructures, designated lamellipodium and lamellum, which differ significantly in their kinetic and kinematic properties as well as their biochemical composition. We developed a stochastic two-dimensional computer simulation that includes chemical reaction kinetics, G-actin diffusion, and filament transport to investigate the formation of growing actin networks in migrating cells. Model parameters were chosen based on experimental data or theoretical considerations. In this work, we demonstrate the system's ability to form two distinct networks by self-organization. We found a characteristic transition in mean filament length as well as a distinct maximum in depolymerization flux, both within the first 1-2 microm. The separation into two distinct substructures was found to be extremely robust with respect to initial conditions and variation of model parameters. We quantitatively investigated the complex interplay between ADF/cofilin and tropomyosin and propose a plausible mechanism that leads to spatial separation of, respectively, ADF/cofilin- or tropomyosin-dominated compartments. Tropomyosin was found to play an important role in stabilizing the lamellar actin network. Furthermore, the influence of filament severing and annealing on the network properties is explored, and simulation data are compared to existing experimental data. KW - Open Archive Y1 - 2008 UR - http://www.ncbi.nlm.nih.gov/pubmed/18708450 U6 - https://doi.org/10.1529/biophysj.108.134817 SN - 1542-0086 VL - 95 IS - 12 SP - 5508 EP - 5523 PB - Biophysical Society ER - TY - JOUR A1 - Huber, Florian A1 - Käs, Josef T1 - Self-regulative organization of the cytoskeleton JF - Cytoskeleton N2 - Despite its impressive complexity the cytoskeleton succeeds to persistently organize itself and thus the cells' interior. In contrast to classical man-made machines, much of the cellular organization originates from inherent self-assembly and self-organization allowing a high degree of autonomy for various functional units. Recent experimental and theoretical studies revealed numerous examples of cytoskeleton components that arrange and organize in a self-regulative way. In the present review we want to shortly summarize some of the principle mechanisms that are able to inherently trigger and regulate the cytoskeleton organization. Although taken individually most of these regulative principles are rather simple with intuitively predictable consequences, combinations of two or more of these mechanisms can quickly give rise to very complex, unexpected behavior and might even be able to explain the formation of different functional units out of a common pool of available building blocks. Y1 - 2011 UR - http://www.ncbi.nlm.nih.gov/pubmed/21438165 U6 - https://doi.org/10.1002/cm.20509 SN - 1949-3592 N1 - Acknowledgment We would like to thank Dan Strehle for critical reading ofthis manuscript. This work was funded by the Leipzig School of Natural Sciences ‘‘BuildMoNa’’ as well as bythe Sa¨chsische Aufbaubank project number 13403 VL - 68 IS - 5 SP - 259 EP - 265 PB - Wiley ER - TY - JOUR A1 - Stuhrmann, Björn A1 - Huber, Florian A1 - Käs, Josef T1 - Robust organizational principles of protrusive biopolymer networks in migrating living cells JF - Plos One N2 - Cell migration is associated with the dynamic protrusion of a thin actin-based cytoskeletal extension at the cell front, which has been shown to consist of two different substructures, the leading lamellipodium and the subsequent lamellum. While the formation of the lamellipodium is increasingly well understood, organizational principles underlying the emergence of the lamellum are just beginning to be unraveled. We report here on a 1D mathematical model which describes the reaction-diffusion processes of a polarized actin network in steady state, and reproduces essential characteristics of the lamellipodium-lamellum system. We observe a steep gradient in filament lengths at the protruding edge, a local depolymerization maximum a few microns behind the edge, as well as a differential dominance of the network destabilizer ADF/cofilin and the stabilizer tropomyosin. We identify simple and robust organizational principles giving rise to the derived network characteristics, uncoupled from the specifics of any molecular implementation, and thus plausibly valid across cell types. An analysis of network length dependence on physico-chemical system parameters implies that to limit array treadmilling to cellular dimensions, network growth has to be truncated by mechanisms other than aging-induced depolymerization, e.g., by myosin-associated network dissociation at the transition to the cell body. Our work contributes to the analytical understanding of the cytoskeletal extension's bisection into lamellipodium and lamellum and sheds light on how cells organize their molecular machinery to achieve motility. KW - DOAJ Y1 - 2011 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:hbz:due62-opus-34901 SN - 1932-6203 N1 - Funding: This work has been supported by the Leipzig Graduate College ‘‘GK 1097 InterNeuro - Interdisciplinary Approaches in Cellular Neuroscience’’ (http:// www.uni-leipzig.de/˜ineuro/) and the Graduate School ‘‘Leipzig School of Natural Sciences - Building with Molecules and Nano-objects (BuildMoNa)’’ (http://www. buildmona.de/). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. VL - 6 IS - 1 PB - Public Library of Science (PLoS) ER - TY - JOUR A1 - Preciado López, Magdalena A1 - Huber, Florian A1 - Grigoriev, Ilya A1 - Steinmetz, Michel O. A1 - Akhmanova, Anna A1 - Koenderink, Gijsje H. A1 - Dogterom, Marileen T1 - Actin-microtubule coordination at growing microtubule ends JF - Nature Communications N2 - To power dynamic processes in cells, the actin and microtubule cytoskeletons organize into complex structures. Although it is known that cytoskeletal coordination is vital for cell function, the mechanisms by which cross-linking proteins coordinate actin and microtubule activities remain poorly understood. In particular, it is unknown how the distinct mechanical properties of different actin architectures modulate the outcome of actin-microtubule interactions. To address this question, we engineered the protein TipAct, which links growing microtubule ends via end-binding proteins to actin filaments. We show that growing microtubules can be captured and guided by stiff actin bundles, leading to global actin-microtubule alignment. Conversely, growing microtubule ends can transport, stretch and bundle individual actin filaments, thereby globally defining actin filament organization. Our results provide a physical basis to understand actin-microtubule cross-talk, and reveal that a simple cross-linker can enable a mechanical feedback between actin and microtubule organization that is relevant to diverse biological contexts. KW - DOAJ Y1 - 2014 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:hbz:due62-opus-34878 SN - 2041-1723 VL - 5 PB - Springer Nature ER -