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Article Dans Une Revue Nature Communications Année : 2020

Direct observation of dynamic protein interactions involving human microtubules using solid-state NMR spectroscopy

Résumé

Microtubules are important components of the eukaryotic cytoskeleton. Their structural organization is regulated by nucleotide binding and many microtubule-associated proteins (MAPs). While cryo-EM and X-ray crystallography have provided detailed views of interactions between MAPs with the microtubule lattice, little is known about how MAPs and their intrinsically disordered regions interact with the dynamic microtubule surface. NMR carries the potential to directly probe such interactions but so far has been precluded by the low tubulin yield. We present a protocol to produce [ 13 C, 15 N]-labeled, functional microtubules (MTs) from human cells for solid-state NMR studies. This approach allowed us to demonstrate that MAPs can differently modulate the fast timescale dynamics of C-terminal tubulin tails, suggesting distinct interaction modes. Our results pave the way for in-depth NMR studies of protein dynamics involved in MT assembly and their interactions with other cellular components.
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Dates et versions

hal-03006404 , version 1 (15-11-2020)

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Yanzhang Luo, Shengqi Xiang, Peter Jan Hooikaas, Laura S. van Bezouwen, Jijumon A.S., et al.. Direct observation of dynamic protein interactions involving human microtubules using solid-state NMR spectroscopy. Nature Communications, 2020, 11 (1), ⟨10.1038/s41467-019-13876-x⟩. ⟨hal-03006404⟩
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