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

Yanzhang Luo, ShengQi Xiang, Peter Jan Hooikaas, Laura Bezouwen, A. S. Jijumon, Carsten Janke, Friedrich Förster, Anna Akhmanova () and Marc Baldus ()
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Yanzhang Luo: Utrecht University
ShengQi Xiang: Utrecht University
Peter Jan Hooikaas: Utrecht University
Laura Bezouwen: Utrecht University
A. S. Jijumon: Institut Curie, PSL Research University, CNRS UMR3348
Carsten Janke: Institut Curie, PSL Research University, CNRS UMR3348
Friedrich Förster: Utrecht University
Anna Akhmanova: Utrecht University
Marc Baldus: Utrecht University

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract 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 [13C, 15N]-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 time-scale 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.

Date: 2020
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DOI: 10.1038/s41467-019-13876-x

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