Microtubule lattice spacing governs cohesive envelope formation of tau family proteins

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A90043%2F22%3A00140009" target="_blank" >RIV/00216224:90043/22:00140009 - isvavai.cz</a>
Alternative codes found
RIV/86652036:_____/22:00563713 RIV/00216208:11310/22:10450927
Result on the web
<a href="https://www.nature.com/articles/s41589-022-01096-2" target="_blank" >https://www.nature.com/articles/s41589-022-01096-2</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41589-022-01096-2" target="_blank" >10.1038/s41589-022-01096-2</a>

Result language
angličtina
Original language name
Microtubule lattice spacing governs cohesive envelope formation of tau family proteins
Original language description
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
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology

Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
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Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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