Septin-microtubule association via a motif unique to isoform 1 of septin 9 tunes stress fibers

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14110%2F22%3A00125367" target="_blank" >RIV/00216224:14110/22:00125367 - isvavai.cz</a>
Result on the web
<a href="https://journals.biologists.com/jcs/article-abstract/135/1/jcs258850/273936/Septin-microtubule-association-via-a-motif-unique" target="_blank" >https://journals.biologists.com/jcs/article-abstract/135/1/jcs258850/273936/Septin-microtubule-association-via-a-motif-unique</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1242/jcs.258850" target="_blank" >10.1242/jcs.258850</a>

Result language
angličtina
Original language name
Septin-microtubule association via a motif unique to isoform 1 of septin 9 tunes stress fibers
Original language description
Septins, a family of GTP-binding proteins that assemble into higher order structures, interface with the membrane, actin filaments and microtubules, and are thus important regulators of cytoarchitecture. Septin 9 (SEPT9), which is frequently overexpressed in tumors and mutated in hereditary neuralgic amyotrophy (HNA), mediates the binding of septins to microtubules, but the molecular determinants of this interaction remained uncertain. We demonstrate that a short microtubule-associated protein (MAP)-like motif unique to SEPT9 isoform 1 (SEPT9_i1) drives septin octamer-microtubule interaction in cells and in vitro reconstitutions. Septin-microtubule association requires polymerizable septin octamers harboring SEPT9_i1. Although outside of the MAP-like motif, HNA mutations abrogate this association, identifying a putative regulatory domain. Removal of this domain from SEPT9_i1 sequesters septins on microtubules, promotes microtubule stability and alters actomyosin fiber distribution and tension. Thus, we identify key molecular determinants and potential regulatory roles of septin-microtubule interaction, paving the way to deciphering the mechanisms underlying septin-associated pathologies.
Czech name
—
Czech description
—

Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10601 - Cell biology

Project
—
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Similar results(10)