Proteomic profiling of microtubule self-organization in M-phase.

Rosas-Salvans, M.; Cavazza, T.; Espadas, G.; Sabido, E.; Vernos, I.

doi:10.1074/mcp.RA118.000745

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Proteomic profiling of microtubule self-organization in M-phase.

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Cavazza, T.
Department of Meiosis, MPI for Biophysical Chemistry, Max Planck Society;

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Rosas-Salvans, M., Cavazza, T., Espadas, G., Sabido, E., & Vernos, I. (2018). Proteomic profiling of microtubule self-organization in M-phase. Molecular and Cellular Proteomics, 17(10), 1991-2004. doi:10.1074/mcp.RA118.000745.

Cite as: https://hdl.handle.net/21.11116/0000-0002-5FD5-4

Abstract

Microtubules (MTs) and associated proteins can self-organize into complex structures such as the bipolar spindle, a process in which RanGTP plays a major role. Addition of RanGTP to M-phase Xenopus egg extracts promotes the nucleation and self-organization of MTs into asters and bipolar-like structures in the absence of centrosomes or chromosomes. We show here that the complex proteome of these RanGTP-induced MT assemblies is similar to that of mitotic spindles. Using proteomic profiling we show that MT self-organization in the M-phase cytoplasm involves the non-linear and non-stoichiometric recruitment of proteins from specific functional groups. Our study provides for the first time a temporal understanding of the protein dynamics driving MT self-organization in M-phase.