Microtubule posttranslational modifications provide unique recognition patterns for associated proteins
Abstract
Microtubules are key components of the eukaryotic cytoskeleton involved in vital functions in virtually every cell. Among the emerging molecular mechanisms to adapt microtubules to their diverse functions is the biochemical diversification of tubulin molecules by posttranslational modifications (PTMs) and differential gene expression, a concept known as the 'tubulin code'. A key question remains whether the tubulin code has the potential to selectively control microtubule interactions of different microtubule-associated proteins (MAPs) to act as a specific signalling system. To answer this question, we used a mediumthroughput in vitro approach to screen 46 proteins for their binding preferences to microtubules with altered PTM or isotype composition. We demonstrate that subsets of these MAPs have unique sensitivities to PTMs, while other proteins are not affected. As a result, PTMs, or combinations of them, differentially attract or repulse individual MAPs to microtubules. Our findings offer mechanistic proof for a key hypothesis of the tubulin code-the capacity to selectively and differentially regulate MAP-microtubule interactions.
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BibTeX
@article{krishnan2026microtubule,
title = {{Microtubule posttranslational modifications provide unique recognition patterns for associated proteins}},
author = {Arya Krishnan and Eva Desvigne-Hansch and Véronique Henriot and Alica Dodoková and Sinda Khanfir and Mariya Genova and Lenka Grycova and Maria M Magiera and Marcus Braun and Zdenek Lansky and Carsten Janke},
journal = {The EMBO Journal},
year = {2026},
month = sep,
doi = {10.1038/s44318-026-00908-8},
url = {https://hal.science/hal-05768453v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Microtubule posttranslational modifications provide unique recognition patterns for associated proteins
AU - Arya Krishnan
AU - Eva Desvigne-Hansch
AU - Véronique Henriot
AU - Alica Dodoková
AU - Sinda Khanfir
AU - Mariya Genova
AU - Lenka Grycova
AU - Maria M Magiera
AU - Marcus Braun
AU - Zdenek Lansky
AU - Carsten Janke
PY - 2026
DA - 2026/09/12
JO - The EMBO Journal
DO - 10.1038/s44318-026-00908-8
UR - https://hal.science/hal-05768453v1
AB - Microtubules are key components of the eukaryotic cytoskeleton involved in vital functions in virtually every cell. Among the emerging molecular mechanisms to adapt microtubules to their diverse functions is the biochemical diversification of tubulin molecules by posttranslational modifications (PTMs) and differential gene expression, a concept known as the 'tubulin code'. A key question remains whether the tubulin code has the potential to selectively control microtubule interactions of different microtubule-associated proteins (MAPs) to act as a specific signalling system. To answer this question, we used a mediumthroughput in vitro approach to screen 46 proteins for their binding preferences to microtubules with altered PTM or isotype composition. We demonstrate that subsets of these MAPs have unique sensitivities to PTMs, while other proteins are not affected. As a result, PTMs, or combinations of them, differentially attract or repulse individual MAPs to microtubules. Our findings offer mechanistic proof for a key hypothesis of the tubulin code-the capacity to selectively and differentially regulate MAP-microtubule interactions.
SN - 0261-4189
SN - 1460-2075
ER -