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Histone H3 lysine 4 methyltransferase subunits regulate cytokinesis (LB191)
Author(s) -
Bailey Jeffrey,
Fields Alexander,
Cheng Kaijian,
Lee Albert,
Wagenaar Eric,
Lagrois Remy,
Schmidt Bailey,
Xia Bin,
Ma Dzwokai
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.lb191
Subject(s) - midbody , cytokinesis , abscission , microbiology and biotechnology , nocodazole , microtubule , biology , chemistry , cell division , cytoskeleton , cell , biochemistry , genetics
Cytokinesis, the physical separation of two dividing cells, occurs at the midbody and affects the growth and development of all organisms. As the final step of cytokinesis, abscission requires membrane fission and cytoskeletal rearrangement at a specific midbody region called the secondary ingression. Here, we report that histone H3 lysine 4 methytransferase (H3K4MT) subunits reside at the midbody. Knockdown of individual H3K4MT subunits increases the incidence of multinucleated cells, slows cell proliferation, and impairs cytokinesis at the abscission step. Further investigation shows that the abscission delay is due to slower formation of secondary ingressions in the knockdown cells. Importantly, the midbody microtubules in H3K4MT knockdown cells display enhanced resistance to depolymerization by nocodazole and the abscission defect in these cells can be partially rescued by drug‐induced microtubule disassembly. We propose that a midbody‐localized H3K4MT complex or subcomplex promotes abscission, at least partially, by facilitating midbody microtubule disassembly. Grant Funding Source : 5R21‐MH086853‐02