Anillin directly crosslinks microtubules with actin filaments

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F25%3A00638781" target="_blank" >RIV/86652036:_____/25:00638781 - isvavai.cz</a>
Result on the web
<a href="https://www.embopress.org/doi/epdf/10.1038/s44318-025-00492-3" target="_blank" >https://www.embopress.org/doi/epdf/10.1038/s44318-025-00492-3</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s44318-025-00492-3" target="_blank" >10.1038/s44318-025-00492-3</a>

Result language
angličtina
Original language name
Anillin directly crosslinks microtubules with actin filaments
Original language description
Complex morphogenetic processes such as cell division require a tight coordination of the activities of microtubules and actin filaments. There is evidence that anillin, conventionally known as an actin-binding andbundling protein, regulates microtubule/actin crosstalk during cell division. However, it is unknown whether anillin binds directly to microtubules and whether it is sufficient to establish crosslinking between microtubules and actin filaments. Here we address both questions by developing an in vitro system for observing anillin-mediated interactions with actin filaments and dynamic microtubules via total internal-reflection fluorescence microscopy. We find that anillin can interact directly with microtubules and promote microtubule bundling. We confirm that anillin binds and bundles actin filaments, and find that it has a strong preference for actin bundles over individual filaments. Moreover, we show that anillin can directly crosslink microtubules and actin filaments, cause sliding of actin filaments on the microtubule lattice, and transport actin filaments by the growing microtubule tip. Our findings indicate that anillin can potentially serve as a direct regulator of microtubule/actin crosstalk, e.g., during cell division.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10608 - Biochemistry and molecular biology

Project
<a href="/en/project/GA23-07703S" target="_blank" >GA23-07703S: Label-free super-resolution microscopy based on single-protein fluctuations to study the assembly of tau protein envelopes</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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