RT Journal Article
SR Electronic
T1 Anillin directly cross-links microtubules with filamentous actin
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2025.01.07.631698
DO 10.1101/2025.01.07.631698
A1 Bareja, Ilina
A1 Kučera, Ondřej
A1 Petitjean, Irene Istúriz
A1 Sabo, Jan
A1 Braun, Marcus
A1 Lansky, Zdenek
A1 Koenderink, Gijsje H.
A1 Dogterom, Marileen
YR 2025
UL http://biorxiv.org/content/early/2025/01/10/2025.01.07.631698.abstract
AB 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 and bundling 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 to observe anillin-mediated interactions with actin filaments and dynamic microtubules using 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, can cause sliding of actin filaments on the microtubule lattice, and can 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.