Abstract
ABSTRACTCell division ends when two daughter cells physically separate via abscission, the cleavage of the intercellular bridge. It is not clear how the anti-parallel microtubule bundles bridging daughter cells are severed. Here, we present a novel abscission mechanism. We identified chromokinesin KIF4A, which is adjacent to the midbody during cytokinesis, as being required for efficient abscission. KIF4A is regulated by post-translational modifications. We evaluated modification of KIF4A by the ubiquitin-like protein SUMO. We mapped lysine 460 in KIF4A as the SUMO acceptor site and employed CRISPR-Cas9-mediated genome editing to block SUMO conjugation of endogenous KIF4A. Failure to SUMOylate this site in KIF4A delayed cytokinesis. SUMOylation of KIF4A enhanced the affinity for the microtubule destabilizer stathmin 1 (STMN1). We here present a new level of abscission regulation through the dynamic interactions between KIF4A and STMN1 as controlled by SUMO modification of KIF4A.
Highlights
Abscission is the final step of cell division in which the two daughter cells are separated to start their own independent life
The human chromokinesin KIF4A is modified by one small ubiquitin-like modifier (SUMO) moiety We aimed to understand the mechanisms and effects of SUMOylation of the chromokinesin KIF4A (Cubeñas-Potts et al, 2015; Kurasawa et al, 2004) to obtain more detailed understanding of how SUMO regulates this important process of mitosis (Fig. 1A)
We identify an important role of SUMOylated KIF4A in the regulation of abscission as this controls the interaction with the MT destabilizer stathmin 1 (STMN1)
Summary
Abscission is the final step of cell division in which the two daughter cells are separated to start their own independent life. The cortex of the intercellular bridge is narrowed to a single stalk of 17-nm-diameter filaments (Guizetti et al, 2011). This process involves the ESCRT-III complex and spastin-mediated microtubule (MT) disassembly
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