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Microtubule lattice spacing governs cohesive envelope formation of tau family proteins

V. Siahaan, R. Tan, T. Humhalova, L. Libusova, SE. Lacey, T. Tan, M. Dacy, KM. Ori-McKenney, RJ. McKenney, M. Braun, Z. Lansky

. 2022 ; 18 (11) : 1224-1235. [pub] 20220822

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc22032877

Grantová podpora
R35 GM124889 NIGMS NIH HHS - United States
R35 GM133688 NIGMS NIH HHS - United States

E-zdroje Online Plný text

NLK ProQuest Central od 2005-06-01 do Před 1 rokem
Health & Medicine (ProQuest) od 2005-06-01 do Před 1 rokem

Odkazy

PubMed 35996000
DOI 10.1038/s41589-022-01096-2
Knihovny.cz E-zdroje

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.

Citace poskytuje Crossref.org

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