Další formáty:
BibTeX
LaTeX
RIS
@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 a Zdenek LANSKY. Microtubule lattice spacing governs cohesive envelope formation of tau family proteins. \textit{Nature Chemical Biology}. 2022, roč.~18, č.~11, s.~1224-1235. ISSN~1552-4450. Dostupné z: https://dx.doi.org/10.1038/s41589-022-01096-2.
|