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

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  • Mira Kuzmić
    Centre de Recherche en Cancérologie de Marseille (CRCM), INSERM, Institut Paoli-Calmettes, Aix Marseille Univ, CNRS 1 , 13009 Marseille , France
  • Gerard Castro Linares
    Kavli Institute of Nanoscience Delft, Delft University of Technology 2 Department of Bionanoscience , , 2629 HZ Delft , The Netherlands
  • Jindřiška Leischner Fialová
    Centre de Recherche en Cancérologie de Marseille (CRCM), INSERM, Institut Paoli-Calmettes, Aix Marseille Univ, CNRS 1 , 13009 Marseille , France
  • François Iv
    Institut Fresnel, CNRS UMR7249, Aix Marseille Univ, Centrale Marseille 4 , 13013 Marseille , France
  • Danièle Salaün
    Centre de Recherche en Cancérologie de Marseille (CRCM), INSERM, Institut Paoli-Calmettes, Aix Marseille Univ, CNRS 1 , 13009 Marseille , France
  • Alex Llewellyn
    Institut Fresnel, CNRS UMR7249, Aix Marseille Univ, Centrale Marseille 4 , 13013 Marseille , France
  • Maxime Gomes
    Institut Fresnel, CNRS UMR7249, Aix Marseille Univ, Centrale Marseille 4 , 13013 Marseille , France
  • Mayssa Belhabib
    Institut Fresnel, CNRS UMR7249, Aix Marseille Univ, Centrale Marseille 4 , 13013 Marseille , France
  • Yuxiang Liu
    Graduate School of Engineering, Osaka City University 5 Department of Bioengineering , , 558-8585 Osaka , Japan
  • Keisuke Asano
    Graduate School of Engineering, Osaka City University 5 Department of Bioengineering , , 558-8585 Osaka , Japan
  • Magda Rodrigues
    Centre de Recherche en Cancérologie de Marseille (CRCM), INSERM, Institut Paoli-Calmettes, Aix Marseille Univ, CNRS 1 , 13009 Marseille , France
  • Daniel Isnardon
    Centre de Recherche en Cancérologie de Marseille (CRCM), INSERM, Institut Paoli-Calmettes, Aix Marseille Univ, CNRS 1 , 13009 Marseille , France
  • Taro Tachibana
    Graduate School of Engineering, Osaka City University 5 Department of Bioengineering , , 558-8585 Osaka , Japan
  • Gijsje H. Koenderink
    Kavli Institute of Nanoscience Delft, Delft University of Technology 2 Department of Bionanoscience , , 2629 HZ Delft , The Netherlands
  • Ali Badache
    Centre de Recherche en Cancérologie de Marseille (CRCM), INSERM, Institut Paoli-Calmettes, Aix Marseille Univ, CNRS 1 , 13009 Marseille , France
  • Manos Mavrakis
    Institut Fresnel, CNRS UMR7249, Aix Marseille Univ, Centrale Marseille 4 , 13013 Marseille , France
  • Pascal Verdier-Pinard
    Centre de Recherche en Cancérologie de Marseille (CRCM), INSERM, Institut Paoli-Calmettes, Aix Marseille Univ, CNRS 1 , 13009 Marseille , France

説明

<jats:title>ABSTRACT</jats:title> <jats:p>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.</jats:p> <jats:p>This article has an associated First Person interview with the first author of the paper.</jats:p>

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