Journal article
Septins mediate a microtubule-actin crosstalk that enables actin growth on microtubules
Proceedings of the National Academy of Sciences - PNAS, v 119(50), pp e2202803119-e2202803119
13 Dec 2022
PMID: 36475946
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Cellular morphogenesis and processes such as cell division and migration require the coordination of the microtubule and actin cytoskeletons. Microtubule-actin crosstalk is poorly understood and largely regarded as the capture and regulation of microtubules by actin. Septins are filamentous guanosine-5'-triphosphate (GTP) binding proteins, which comprise the fourth component of the cytoskeleton along microtubules, actin, and intermediate filaments. Here, we report that septins mediate microtubule-actin crosstalk by coupling actin polymerization to microtubule lattices. Superresolution and platinum replica electron microscopy (PREM) show that septins localize to overlapping microtubules and actin filaments in the growth cones of neurons and non-neuronal cells. We demonstrate that recombinant septin complexes directly crosslink microtubules and actin filaments into hybrid bundles. In vitro reconstitution assays reveal that microtubule-bound septins capture and align stable actin filaments with microtubules. Strikingly, septins enable the capture and polymerization of growing actin filaments on microtubule lattices. In neuronal growth cones, septins are required for the maintenance of the peripheral actin network that fans out from microtubules. These findings show that septins directly mediate microtubule interactions with actin filaments, and reveal a mechanism of microtubule-templated actin growth with broader significance for the self-organization of the cytoskeleton and cellular morphogenesis.
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Details
- Title
- Septins mediate a microtubule-actin crosstalk that enables actin growth on microtubules
- Creators
- Konstantinos Nakos - Drexel UniversityMd Noor A Alam - Drexel UniversityMegan R Radler - Drexel UniversityIlona A Kesisova - Drexel UniversityChangsong Yang - University of PennsylvaniaJoshua Okletey - Drexel UniversityMeagan R Tomasso - Drexel UniversityShae B Padrick - Drexel UniversityTatyana M Svitkina - University of PennsylvaniaElias T Spiliotis - Drexel University
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, v 119(50), pp e2202803119-e2202803119
- Publisher
- PNAS
- Grant note
- R35 GM136337 / NIGMS NIH HHS R35 GM140832 / NIGMS NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology; Biology
- Web of Science ID
- WOS:000964669800001
- Scopus ID
- 2-s2.0-85143570876
- Other Identifier
- 991020100063704721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Cell Biology