ZW10

Centromere/kinetochore protein zw10 homolog is a is_associated_with::protein that in humans is encoded by the ZW10 is_associated_with::gene. This gene encodes a protein that is one of many involved in mechanisms to ensure proper is_associated_with::chromosome segregation during is_associated_with::cell division. The encoded protein binds to is_associated_with::centromeres during the is_associated_with::prophase, is_associated_with::metaphase, and early is_associated_with::anaphase cell division stages and to is_associated_with::kinetochore is_associated_with::microtubules during metaphase.

Function
Zeste white 10 (ZW10) was initially identified as a mitotic checkpoint is_associated_with::protein involved in is_associated_with::chromosome segregation, and then implicated in targeting is_associated_with::cytoplasmic is_associated_with::dynein and dynactin to mitotic kinetochores, but it is also important in non-dividing cells. These include is_associated_with::cytoplasmic dynein targeting to Golgi and other membranes, and SNARE-mediated ER-Golgi trafficking. Dominant-negative ZW10, anti-ZW10 antibody, and ZW10 RNA interference (RNAi) cause Golgi dispersal. ZW10 RNAi also disperse is_associated_with::endosomes and is_associated_with::lysosomes.

is_associated_with::Drosophila kinetochore components Rough deal (Rod) and Zw10 are required for the proper functioning of the metaphase checkpoint in flies. The is_associated_with::eukaryotic spindle assembly checkpoint (SAC) monitors is_associated_with::microtubule attachment to kinetochores and prevents anaphase onset until all kinetochores are aligned on the metaphase plate. It is an essential surveillance mechanism that ensures high fidelity is_associated_with::chromosome segregation during is_associated_with::mitosis. In higher eukaryotes, cytoplasmic dynein is involved in silencing the SAC by removing the checkpoint is_associated_with::proteins Mad2 and the Rod-Zw10-Zwilch complex (RZZ) from aligned kinetochores.

Interactions
ZW10 has been shown to interact with is_associated_with::RINT1