ArticleBMC structural biology2016
The C-terminal domain of TPX2 is made of alpha-helical tandem repeats.
Article in BMC structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- Article
- Diverse microtubule-binding repeats regulate TPX2 activities at distinct locations within the spindle.The Journal of cell biology · 2025Article
- PARP1 proximity proteomics reveals interaction partners at stressed replication forks.Nucleic acids research · 2022Article
- Article
- Structural bioinformatics predicts that the Retinitis Pigmentosa-28 protein of unknown function FAM161A is a homologue of the microtubule nucleation factor Tpx2.F1000Research · 2020Article
- Article
- Structural analysis of the role of TPX2 in branching microtubule nucleation.The Journal of cell biology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 4 countries.
Funding
Abstract
backgroundTPX2 (Targeting Protein for Xklp2) is essential for spindle assembly, activation of the mitotic kinase Aurora A and for triggering microtubule nucleation. Homologs of TPX2 in Chordata and plants were previously identified. Currently, proteins of the TPX2 family have little structural information and only small parts are covered by defined protein domains.
methodsWe have used computational sequence analyses and structural predictions of proteins of the TPX2 family, supported with Circular Dichroism (CD) measurements.
resultsHere, we report our finding that the C-terminal domain of TPX2, which is responsible of its microtubule nucleation capacity and is conserved in all members of the family, is actually formed by tandem repeats, covering well above 2/3 of the protein. We propose that this region forms a flexible solenoid involved in protein-protein interactions. Structural prediction and molecular modeling, combined with Circular Dichroism (CD) measurements reveal a predominant alpha-helical content. Furthermore, we identify full length homologs in fungi and shorter homologs with a different domain organization in diptera (including a paralogous expansion in Drosophila).
conclusionsOur results, represent the first computational and biophysical analysis of the TPX2 proteins family and help understand the structure and evolution of this conserved protein family to direct future structural studies.
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