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.
journal_name
Cell Repjournal_title
Cell reportsauthors
Chung JY,Steen JA,Schwarz TLdoi
10.1016/j.celrep.2016.07.055subject
Has Abstractpub_date
2016-08-23 00:00:00pages
2142-2155issue
8issn
2211-1247pii
S2211-1247(16)30986-Xjournal_volume
16pub_type
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