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Kuzmić M, Linares GC, Fialová JL, et al. Septin-microtubule association via a motif unique to the isoform 1 of septin 9 tunes stress fibers. J Cell Sci. 2021;doi: 10.1242/jcs.258850.
Kuzmić, M., Linares, G. C., Fialová, J. L., Iv, F., Salaün, D., Llewellyn, A., Gomes, M., Belhabib, M., Liu, Y., Asano, K., Rodrigues, M., Isnardon, D., Tachibana, T., Koenderink, G. H., Badache, A., Mavrakis, M., & Verdier-Pinard, P. (2021). Septin-microtubule association via a motif unique to the isoform 1 of septin 9 tunes stress fibers. Journal of cell science, . https://doi.org/10.1242/jcs.258850
Kuzmić, Mira, et al. "Septin-microtubule association via a motif unique to the isoform 1 of septin 9 tunes stress fibers." Journal of cell science vol. (2021). doi: https://doi.org/10.1242/jcs.258850
Kuzmić M, Linares GC, Fialová JL, Iv F, Salaün D, Llewellyn A, Gomes M, Belhabib M, Liu Y, Asano K, Rodrigues M, Isnardon D, Tachibana T, Koenderink GH, Badache A, Mavrakis M, Verdier-Pinard P. Septin-microtubule association via a motif unique to the isoform 1 of septin 9 tunes stress fibers. J Cell Sci. 2021 Dec 02; doi: 10.1242/jcs.258850. Epub 2021 Dec 02. PMID: 34854883.
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J Cell Sci. 2021 Dec 02; doi: 10.1242/jcs.258850. Epub 2021 Dec 02.

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

Journal of cell science

Mira Kuzmić, Gerard Castro Linares, Jindřiška Leischner Fialová, François Iv, Danièle Salaün, Alex Llewellyn, Maxime Gomes, Mayssa Belhabib, Yuxiang Liu, Keisuke Asano, Magda Rodrigues, Daniel Isnardon, Taro Tachibana, Gijsje H Koenderink, Ali Badache, Manos Mavrakis, Pascal Verdier-Pinard

Affiliations

  1. Centre de Recherche en Cancérologie de Marseille (CRCM), INSERM, Institut Paoli-Calmettes, Aix Marseille Univ, CNRS, 13009 Marseille, France.
  2. Department of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, 2629 HZ Delft, The Netherlands.
  3. Department of Pathological Physiology, Faculty of Medicine, Masaryk University, Brno, Czech Republic.
  4. Institut Fresnel, CNRS UMR7249, Aix Marseille Univ, Centrale Marseille, 13013 Marseille, France.
  5. Department of Bioengineering, Graduate School of Engineering, Osaka City University, Osaka, Japan.
  6. Cell Engineering Corporation, Osaka, Japan.

PMID: 34854883 DOI: 10.1242/jcs.258850

Abstract

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.

© 2021. Published by The Company of Biologists Ltd.

Keywords: Actin; Cytoskeleton; Microtubule; SEPT9s; Septin

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