AI Article Synopsis
- During mitosis in mammalian cells, the Golgi apparatus fragments to ensure proper distribution into daughter cells.
- Golgin45, a protein associated with the Golgi, plays a key role in recruiting PLK1 to the kinetochores, which are essential for chromosome separation.
- A mutation in Golgin45 disrupts its interaction with importin β2, stopping PLK1 from properly localizing to the kinetochores and causing a mitotic arrest, highlighting a new function of Golgin45 in mitosis.
Article Abstract
In mammalian cells, the Golgi apparatus undergoes fragmentation for its correct partition into two daughter cells during mitosis. Several Golgi structural proteins have been demonstrated to regulate Golgi disassembly/reassembly and spindle formation. However, it is largely unknown whether Golgi proteins mediate other major events in mitosis. Here, we report that Golgin45, a Golgi tethering protein, participates in recruiting PLK1 to the kinetochores. Upon entry into mitosis, Golgin45 binds PLK1 and a nuclear import protein, importin β2. Enriched RanGTP at kinetochores in prometaphase and metaphase sequesters importin β2 from Golgin45 and liberates Golgin45-PLK1 complex, which then gets further delivered to the kinetochores by Golgin45-KNL1 interaction. R375A mutation in Golgin45 that specifically disrupts Golgin45-importin β2 interaction impairs PLK1 localization to the kinetochores, leading to mitotic arrest. Our findings reveal a novel role of a golgin tether protein in mediating Ran-dependent PLK1 enrichment on the kinetochores for proper progression of mitosis.
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| http://dx.doi.org/10.1016/j.bbrc.2024.150845 | DOI Listing |
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