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@article{2262571,
author = {Siahaan, Valerie and Tan, Ruensern and Humhalova, Tereza and Libusova, Lenka and Lacey, Samuel E and Tan, Tracy and Dacy, Mariah and OriandMcKenney, Kassandra M and McKenney, Richard J and Braun, Marcus and Lansky, Zdenek},
article_number = {11},
doi = {http://dx.doi.org/10.1038/s41589-022-01096-2},
keywords = {Humans; Microtubule-Associated Proteins; Microtubules; Neurodegenerative Diseases; Proteins; tau Proteins; Tubulin},
language = {eng},
issn = {1552-4450},
journal = {Nature Chemical Biology},
title = {Microtubule lattice spacing governs cohesive envelope formation of tau family proteins},
url = {https://www.nature.com/articles/s41589-022-01096-2},
volume = {18},
year = {2022}
}
TY - JOUR
ID - 2262571
AU - Siahaan, Valerie - Tan, Ruensern - Humhalova, Tereza - Libusova, Lenka - Lacey, Samuel E - Tan, Tracy - Dacy, Mariah - Ori-McKenney, Kassandra M - McKenney, Richard J - Braun, Marcus - Lansky, Zdenek
PY - 2022
TI - Microtubule lattice spacing governs cohesive envelope formation of tau family proteins
JF - Nature Chemical Biology
VL - 18
IS - 11
SP - 1224-1235
EP - 1224-1235
SN - 15524450
KW - Humans
KW - Microtubule-Associated Proteins
KW - Microtubules
KW - Neurodegenerative Diseases
KW - Proteins
KW - tau Proteins
KW - Tubulin
UR - https://www.nature.com/articles/s41589-022-01096-2
N2 - Tau is an intrinsically disordered microtubule-associated protein (MAP) implicated in neurodegenerative disease. On microtubules, tau molecules segregate into two kinetically distinct phases, consisting of either independently diffusing molecules or interacting molecules that form cohesive 'envelopes' around microtubules. Envelopes differentially regulate lattice accessibility for other MAPs, but the mechanism of envelope formation remains unclear. Here we find that tau envelopes form cooperatively, locally altering the spacing of tubulin dimers within the microtubule lattice. Envelope formation compacted the underlying lattice, whereas lattice extension induced tau envelope disassembly. Investigating other members of the tau family, we find that MAP2 similarly forms envelopes governed by lattice spacing, whereas MAP4 cannot. Envelopes differentially biased motor protein movement, suggesting that tau family members could spatially divide the microtubule surface into functionally distinct regions. We conclude that the interdependent allostery between lattice spacing and cooperative envelope formation provides the molecular basis for spatial regulation of microtubule-based processes by tau and MAP2. Keywords
ER -
SIAHAAN, Valerie, Ruensern TAN, Tereza HUMHALOVA, Lenka LIBUSOVA, Samuel E LACEY, Tracy TAN, Mariah DACY, Kassandra M ORI-MCKENNEY, Richard J MCKENNEY, Marcus BRAUN and Zdenek LANSKY. Microtubule lattice spacing governs cohesive envelope formation of tau family proteins. \textit{Nature Chemical Biology}. 2022, vol.~18, No~11, p.~1224-1235. ISSN~1552-4450. Available from: https://dx.doi.org/10.1038/s41589-022-01096-2.
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