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Dual localized kinesin‐12 POK 2 plays multiple roles during cell division and interacts with MAP 65‐3
Author(s) -
Herrmann Arvid,
Livanos Pantelis,
Lipka Elisabeth,
Gadeyne Astrid,
Hauser MarieTheres,
Van Damme Daniël,
Müller Sabine
Publication year - 2018
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201846085
Subject(s) - library science , biology , computer science
Kinesins are versatile nano‐machines that utilize variable non‐motor domains to tune specific motor microtubule encounters. During plant cytokinesis, the kinesin‐12 orthologs, PHRAGMOPLAST ORIENTING KINESIN ( POK )1 and POK 2, are essential for rapid centrifugal expansion of the cytokinetic apparatus, the phragmoplast, toward a pre‐selected cell plate fusion site at the cell cortex. Here, we report on the spatio‐temporal localization pattern of POK 2, mediated by distinct protein domains. Functional dissection of POK 2 domains revealed the association of POK 2 with the site of the future cell division plane and with the phragmoplast during cytokinesis. Accumulation of POK 2 at the phragmoplast midzone depends on its functional POK 2 motor domain and is fine‐tuned by its carboxy‐terminal region that also directs POK 2 to the division site. Furthermore, POK 2 likely stabilizes the phragmoplast midzone via interaction with the conserved microtubule‐associated protein MAP 65‐3/ PLEIADE , a well‐established microtubule cross‐linker. Collectively, our results suggest that dual localized POK 2 plays multiple roles during plant cell division.