Hof1 and Chs4 Interact via F-BAR Domain and Sel1-like Repeats to Control Extracellular Matrix Deposition during Cytokinesis

Localized extracellular matrix (ECM) remodeling is thought to stabilize the cleavage furrow and maintain cell shape during cytokinesis [1–14]. This remodeling is spatiotemporally coordinated with a cytoskeletal structure pertaining to a kingdom of life, for example the FtsZ ring in bacteria [15], th...

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Published in:Current biology 2017-09, Vol.27 (18), p.2878-2886.e5
Main Authors: Oh, Younghoon, Schreiter, Jennifer H., Okada, Hiroki, Wloka, Carsten, Okada, Satoshi, Yan, Di, Duan, Xudong, Bi, Erfei
Format: Article
Language:English
Subjects:
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
budding yeast
chitin
Chitin Synthase - genetics
Chitin Synthase - metabolism
Chs2
Chs3
Chs4
cytokinesis
Cytokinesis - physiology
Extracellular Matrix - metabolism
F-BAR
Hof1
Microtubule-Associated Proteins - genetics
Microtubule-Associated Proteins - metabolism
Protein Binding
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Sel1-like repeats
septum formation
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Summary:Localized extracellular matrix (ECM) remodeling is thought to stabilize the cleavage furrow and maintain cell shape during cytokinesis [1–14]. This remodeling is spatiotemporally coordinated with a cytoskeletal structure pertaining to a kingdom of life, for example the FtsZ ring in bacteria [15], the phragmoplast in plants [16], and the actomyosin ring in fungi and animals [17, 18]. Although the cytoskeletal structures have been analyzed extensively, the mechanisms of ECM remodeling remain poorly understood. In the budding yeast Saccharomyces cerevisiae, ECM remodeling refers to sequential formations of the primary and secondary septa that are catalyzed by chitin synthase-II (Chs2) and chitin synthase-III (the catalytic subunit Chs3 and its activator Chs4), respectively [18, 19]. Surprisingly, both Chs2 and Chs3 are delivered to the division site at the onset of cytokinesis [6, 20]. What keeps Chs3 inactive until secondary septum formation remains unknown. Here, we show that Hof1 binds to the Sel1-like repeats (SLRs) of Chs4 via its F-BAR domain and inhibits Chs3-mediated chitin synthesis during cytokinesis. In addition, Hof1 is required for rapid accumulation as well as efficient removal of Chs4 at the division site. This study uncovers a mechanism by which Hof1 controls timely activation of Chs3 during cytokinesis and defines a novel interaction and function for the conserved F-BAR domain and SLR that are otherwise known for their abilities to bind membrane lipids [21, 22] and scaffold protein complex formation [23]. [Display omitted] •Hof1 and Chs4 interact via the conserved F-BAR domain and Sel1-like repeats•Hof1 and Chs3 compete for binding to the SLR of Chs4•Hof1 regulates the localization dynamics of Chs4 at the division site•Hof1 regulates Chs3-mediated chitin synthesis during cytokinesis ECM remodeling during cytokinesis occurs in a spatiotemporally controlled manner. Oh et al. report that the F-BAR protein Hof1 interacts with the SLR protein Chs4 to ensure that secondary septum formation occurs after actomyosin ring constriction and primary septum formation during cytokinesis in budding yeast.
ISSN:0960-9822
1879-0445
DOI:10.1016/j.cub.2017.08.032