AI Article Synopsis
- Interphase mitochondria are connected to microtubules, but during mitosis, they detach from spindle microtubules and move to the cell's outer edges.
- The detachment of mitochondria is not due to active transport but rather because motor proteins like kinesin and dynein are removed from the mitochondria’s surface, a process influenced by CDK1 and Aurora A phosphorylation.
- This removal is crucial for ensuring proper distribution of mitochondria to daughter cells; disrupting it can lead to cell cycle issues and abnormalities like binucleate cells.
Article Abstract
While interphase mitochondria associate with microtubules, mitotic mitochondria dissociate from spindle microtubules and localize in the cell periphery. Here, we show that this redistribution is not mediated by mitochondrial active transport or tethering to the cytoskeleton. Instead, kinesin and dynein, which link mitochondria to microtubules, are shed from the mitochondrial surface. Shedding is driven by phosphorylation of mitochondrial and cytoplasmic targets by CDK1 and Aurora A. Forced recruitment of motor proteins to mitotic mitochondria to override this shedding prevents their proper symmetrical distribution and disrupts the balanced inheritance of mitochondria to daughter cells. Moreover, when mitochondria with bound dynein bind to the mitotic spindle, they arrest cell-cycle progression and produce binucleate cells. Thus, our results show that the regulated release of motor proteins from the mitochondrial surface is a critical mitotic event.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5001922 | PMC |
| http://dx.doi.org/10.1016/j.celrep.2016.07.055 | DOI Listing |
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