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Chromokinesin KIF4A teams up with Stathmin 1 to regulate abscission in a SUMO-dependent manner

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Original languageEnglish
JournalJournal of Cell Science
Publication statusPublished - 24 Jul 2020


Cell 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 the chromokinesin
KIF4A adjacent to the midbody during cytokinesis which is 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
enhances affinity for the microtubule destabilizer Stathmin1. We here present a new level of
abscission regulation through the dynamic interactions between KIF4A and Stathmin 1 as
controlled by SUMO modification of KIF4A.

    Research areas

  • mitosis, abscission, cytokinesis, KIF4A, post-translational modification, SUMO, stathmin 1

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