Septin-microtubule association requires a MAP-like motif unique to Sept9 isoform 1 embedded into septin octamers - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Cell Science Année : 2022

Septin-microtubule association requires a MAP-like motif unique to Sept9 isoform 1 embedded into septin octamers

Francois Iv
Alex Llewellyn
Mayssa Belhabib
Yuxiang Liu
  • Fonction : Auteur
Manos Mavrakis

Résumé

Septins, a family of GTP-binding proteins assembling into higher order structures, interface with the membrane, actin filaments and microtubules, which positions them as 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 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 abrogates 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.
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Dates et versions

hal-03192486 , version 1 (06-10-2021)
hal-03192486 , version 2 (02-12-2021)

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Mira Kuzmić, Gerard Castro Linares, Jindřiška Leischner Fialová, Francois Iv, Danièle Salaün, et al.. Septin-microtubule association requires a MAP-like motif unique to Sept9 isoform 1 embedded into septin octamers. Journal of Cell Science, 2022, 135 (1), ⟨10.1242/jcs.258850⟩. ⟨hal-03192486v2⟩
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