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

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.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-5FD5-4 Version Permalink: http://hdl.handle.net/21.11116/0000-0004-4299-5
Genre: Journal Article

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 Creators:
Rosas-Salvans, M., Author
Cavazza, T.1, Author              
Espadas, G., Author
Sabido, E., Author
Vernos, I., Author
Affiliations:
1Department of Meiosis, MPI for Biophysical Chemistry, Max Planck Society, ou_2205654              

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Free keywords: Mitosis; Cell division; Cell biology; Protein complex analysis; Protein-Protein Interactions; Microtubule; Proteomic profiling; RanGTP; Self-organization; Spindle
 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.

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Language(s): eng - English
 Dates: 2018-07-032018-10-01
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1074/mcp.RA118.000745
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Title: Molecular and Cellular Proteomics
Source Genre: Journal
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Pages: - Volume / Issue: 17 (10) Sequence Number: - Start / End Page: 1991 - 2004 Identifier: -