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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.<\/jats:p>\n                  <jats:p>This article has an associated First Person interview with the first author of the paper.<\/jats:p>","DOI":"10.1242\/jcs.258850","type":"journal-article","created":{"date-parts":[[2021,12,2]],"date-time":"2021-12-02T09:17:46Z","timestamp":1638436666000},"source":"Crossref","is-referenced-by-count":40,"title":["Septin-microtubule association via a motif unique to isoform 1 of septin 9 tunes stress fibers"],"prefix":"10.1242","volume":"135","author":[{"given":"Mira","family":"Kuzmi\u0107","sequence":"first","affiliation":[{"name":"Centre de Recherche en Canc\u00e9rologie de Marseille (CRCM), INSERM, Institut Paoli-Calmettes, Aix Marseille Univ, CNRS 1 , 13009 Marseille , 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