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@article{1834217,
author = {Kuzmić, M. and Castro Linares, G. and Leischner Fialová, Jindřiška and Iv, F. and Salaün, D. and Llewellyn, A. and Gomes, M. and Belhabib, M. and Liu, Y. and Asano, K. and Rodrigues, M. and Isnardon, D. and Tachibana, T. and Koenderink, G. H. and Badache, A. and Mavrakis, M. and VerdierandPinard, P.},
article_location = {CAMBRIDGE},
article_number = {1},
doi = {http://dx.doi.org/10.1242/jcs.258850},
keywords = {Actin; Cytoskeleton; Microtubule; Septin; SEPT9},
language = {eng},
issn = {0021-9533},
journal = {Journal of Cell Science},
title = {Septin-microtubule association via a motif unique to isoform 1 of septin 9 tunes stress fibers},
url = {https://journals.biologists.com/jcs/article-abstract/135/1/jcs258850/273936/Septin-microtubule-association-via-a-motif-unique},
volume = {135},
year = {2022}
}
TY - JOUR
ID - 1834217
AU - Kuzmić, M. - Castro Linares, G. - Leischner Fialová, Jindřiška - 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.
PY - 2022
TI - Septin-microtubule association via a motif unique to isoform 1 of septin 9 tunes stress fibers
JF - Journal of Cell Science
VL - 135
IS - 1
SP - 1-18
EP - 1-18
PB - COMPANY BIOLOGISTS LTD
SN - 00219533
KW - Actin
KW - Cytoskeleton
KW - Microtubule
KW - Septin
KW - SEPT9
UR - https://journals.biologists.com/jcs/article-abstract/135/1/jcs258850/273936/Septin-microtubule-association-via-a-motif-unique
N2 - 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.
ER -
KUZMI$\backslash$'C, M., G. CASTRO LINARES, Jindřiška LEISCHNER FIALOVÁ, F. IV, D. SALAÜN, A. LLEWELLYN, M. GOMES, M. BELHABIB, Y. LIU, K. ASANO, M. RODRIGUES, D. ISNARDON, T. TACHIBANA, G. H. KOENDERINK, A. BADACHE, M. MAVRAKIS and P. VERDIER-PINARD. Septin-microtubule association via a motif unique to isoform 1 of septin 9 tunes stress fibers. \textit{Journal of Cell Science}. CAMBRIDGE: COMPANY BIOLOGISTS LTD, 2022, vol.~135, No~1, p.~1-18. ISSN~0021-9533. Available from: https://dx.doi.org/10.1242/jcs.258850.
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