The MIS12 complex is a protein interaction hub for outer kinetochore assembly
| Autor: | Andrea Musacchio, Jenny Keller, Arsen Petrovic, Alessio Maiolica, Stefano Santaguida, Silvia Monzani, Davide Cittaro, Prakash Dube, Sebastiano Pasqualato, Lucia Massimiliano, Holger Stark, Veronica Krenn, Aldo Tarricone |
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| Přispěvatelé: | Petrovic, A, Pasqualato, S, Dube, P, Krenn, V, Santaguida, S, Cittaro, D, Monzani, S, Massimiliano, L, Keller, J, Tarricone, A, Maiolica, A, Stark, H, Musacchio, A |
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Protein subunit
Recombinant Fusion Proteins Kinetochore assembly Molecular Sequence Data Mitosis Microtubule Biology Chromosome HeLa Cell Microtubules Ndc80 complex Article Chromosomes 03 medical and health sciences 0302 clinical medicine DSN1 Escherichia coli Humans Amino Acid Sequence Kinetochores Protein Subunit Research Articles Nuclear Protein 030304 developmental biology 0303 health sciences Kinetochore Microtubule-Associated Protein BIO/13 - BIOLOGIA APPLICATA Nuclear Proteins Cell Biology Mitosi Spindle apparatus Cell biology Protein Structure Tertiary NDC80 Molecular Weight Protein Subunits Kinetochore organization Biologie Microtubule-Associated Proteins 030217 neurology & neurosurgery Human HeLa Cells |
| Zdroj: | The Journal of Cell Biology Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | The NSL1 subunit structures interactions between the MIS12, NDC80, and KNL1 kinetochore complexes (see also a related paper by Maskell et al. in this issue). Kinetochores are nucleoprotein assemblies responsible for the attachment of chromosomes to spindle microtubules during mitosis. The KMN network, a crucial constituent of the outer kinetochore, creates an interface that connects microtubules to centromeric chromatin. The NDC80, MIS12, and KNL1 complexes form the core of the KMN network. We recently reported the structural organization of the human NDC80 complex. In this study, we extend our analysis to the human MIS12 complex and show that it has an elongated structure with a long axis of ∼22 nm. Through biochemical analysis, cross-linking–based methods, and negative-stain electron microscopy, we investigated the reciprocal organization of the subunits of the MIS12 complex and their contacts with the rest of the KMN network. A highlight of our findings is the identification of the NSL1 subunit as a scaffold supporting interactions of the MIS12 complex with the NDC80 and KNL1 complexes. Our analysis has important implications for understanding kinetochore organization in different organisms. |
| Databáze: | OpenAIRE |
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