SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis.
Article Details
- CitationCopy to clipboard
Zhang XD, Goeres J, Zhang H, Yen TJ, Porter AC, Matunis MJ
SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis.
Mol Cell. 2008 Mar 28;29(6):729-41. doi: 10.1016/j.molcel.2008.01.013.
- PubMed ID
- 18374647 [ View in PubMed]
- Abstract
SUMOylation is essential for cell-cycle regulation in invertebrates; however, its functions during the mammalian cell cycle are largely uncharacterized. Mammals express three SUMO paralogs: SUMO-1, SUMO-2, and SUMO-3 (SUMO-2 and SUMO-3 are 96% identical and referred to as SUMO-2/3). We found that SUMO-2/3 localize to centromeres and condensed chromosomes, whereas SUMO-1 localizes to the mitotic spindle and spindle midzone, indicating that SUMO paralogs regulate distinct mitotic processes in mammalian cells. Consistent with this, global inhibition of SUMOylation caused a prometaphase arrest due to defects in targeting the microtubule motor protein CENP-E to kinetochores. CENP-E was found to be modified specifically by SUMO-2/3 and to possess SUMO-2/3 polymeric chain-binding activity essential for kinetochore localization. Our findings indicate that SUMOylation is a key regulator of the mammalian cell cycle, with SUMO-1 and SUMO-2/3 modification of different proteins regulating distinct processes.