@article{PreciadoLopezHuberGrigorievetal.2014, author = {Preciado L{\´o}pez, Magdalena and Huber, Florian and Grigoriev, Ilya and Steinmetz, Michel O. and Akhmanova, Anna and Dogterom, Marileen and Koenderink, Gijsje H.}, title = {In vitro reconstitution of dynamic microtubules interacting with actin filament networks}, series = {Methods in Enzymology}, volume = {540}, journal = {Methods in Enzymology}, publisher = {Elsevier}, issn = {1557-7988}, doi = {10.1016/B978-0-12-397924-7.00017-0}, pages = {301 -- 320}, year = {2014}, language = {en} } @article{PreciadoLopezHuberGrigorievetal.2014, author = {Preciado L{\´o}pez, Magdalena and Huber, Florian and Grigoriev, Ilya and Steinmetz, Michel O. and Akhmanova, Anna and Koenderink, Gijsje H. and Dogterom, Marileen}, title = {Actin-microtubule coordination at growing microtubule ends}, series = {Nature Communications}, volume = {5}, journal = {Nature Communications}, publisher = {Springer Nature}, issn = {2041-1723}, doi = {10.1038/ncomms5778}, url = {http://nbn-resolving.de/urn:nbn:de:hbz:due62-opus-34878}, pages = {4778}, year = {2014}, abstract = {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.}, language = {en} } @article{KokHuberKalischetal.2025, author = {Kok, Maurits and Huber, Florian and Kalisch, Svenja-Marei and Dogterom, Marileen}, title = {EB3-informed dynamics of the microtubule stabilizing cap during stalled growth}, series = {Biophysical Journal}, volume = {124}, journal = {Biophysical Journal}, number = {2}, publisher = {Elsevier}, issn = {1542-0086}, doi = {10.1016/j.bpj.2024.11.3314}, url = {http://nbn-resolving.de/urn:nbn:de:hbz:due62-opus-53164}, pages = {227 -- 244}, year = {2025}, abstract = {Microtubule stability is known to be governed by a stabilizing GTP/GDP-Pi cap, but the exact relation between growth velocity, GTP hydrolysis, and catastrophes remains unclear. We investigate the dynamics of the stabilizing cap through in vitro reconstitution of microtubule dynamics in contact with microfabricated barriers, using the plus-end binding protein GFP-EB3 as a marker for the nucleotide state of the tip. The interaction of growing microtubules with steric objects is known to slow down microtubule growth and accelerate catastrophes. We show that the lifetime distributions of stalled microtubules, as well as the corresponding lifetime distributions of freely growing microtubules, can be fully described with a simple phenomenological 1D model based on noisy microtubule growth and a single EB3-dependent hydrolysis rate. This same model is furthermore capable of explaining both the previously reported mild catastrophe dependence on microtubule growth rates and the catastrophe statistics during tubulin washout experiments.}, subject = {Mikrotubulus}, language = {en} }