Article ; Online: Context-dependent spindle pole focusing.
2018 Volume 62, Issue 6, Page(s) 803–813
Abstract: The formation of a robust, bi-polar spindle apparatus, capable of accurate chromosome segregation, is a complex process requiring the co-ordinated nucleation, sorting, stabilization and organization of microtubules (MTs). Work over the last 25 years has ... ...
| Abstract | The formation of a robust, bi-polar spindle apparatus, capable of accurate chromosome segregation, is a complex process requiring the co-ordinated nucleation, sorting, stabilization and organization of microtubules (MTs). Work over the last 25 years has identified protein complexes that act as functional modules to nucleate spindle MTs at distinct cellular sites such as centrosomes, kinetochores, chromatin and pre-existing MTs themselves. There is clear evidence that the extent to which these different MT nucleating pathways contribute to spindle mass both during mitosis and meiosis differs not only between organisms, but also in different cell types within an organism. This plasticity contributes the robustness of spindle formation; however, whether such plasticity is present in other aspects of spindle formation is less well understood. Here, we review the known roles of the protein complexes responsible for spindle pole focusing, investigating the evidence that these, too, act co-ordinately and differentially, depending on cellular context. We describe relationships between MT minus-end directed motors dynein and HSET/Ncd, depolymerases including katanin and MCAK, and direct minus-end binding proteins such as nuclear-mitotic apparatus protein, ASPM and Patronin/CAMSAP. We further explore the idea that the focused spindle pole acts as a non-membrane bound condensate and suggest that the metaphase spindle pole be treated as a transient organelle with context-dependent requirements for function. |
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| MeSH term(s) | Animals ; Humans ; Kinetochores/metabolism ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Mitosis ; Nuclear Proteins/metabolism ; Spindle Poles/metabolism |
| Chemical Substances | Microtubule-Associated Proteins ; Nuclear Proteins |
| Language | English |
| Publishing date | 2018-12-07 |
| Publishing country | England |
| Document type | Journal Article ; Review |
| ISSN | 1744-1358 ; 0071-1365 |
| ISSN (online) | 1744-1358 |
| ISSN | 0071-1365 |
| DOI | 10.1042/EBC20180034 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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