Abnormal mitotic spindle assembly and cytokinesis induced by D-Limonene in cultured mammalian cells

M. Mauro; I. Catanzaro; F. Naselli; G. Sciandrello; F. Caradonna

doi:10.1093/mutage/get040

Abnormal mitotic spindle assembly and cytokinesis induced by D-Limonene in cultured mammalian cells

Mutagenesis ◽

10.1093/mutage/get040 ◽

2013 ◽

Vol 28 (6) ◽

pp. 631-635 ◽

Cited By ~ 10

Author(s):

M. Mauro ◽

I. Catanzaro ◽

F. Naselli ◽

G. Sciandrello ◽

F. Caradonna

Keyword(s):

Mitotic Spindle ◽

Mammalian Cells ◽

Spindle Assembly ◽

Mitotic Spindle Assembly

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The deubiquitinating enzyme complex BRISC is required for proper mitotic spindle assembly in mammalian cells

The Journal of Cell Biology ◽

10.1083/jcb.201503039 ◽

2015 ◽

Vol 210 (2) ◽

pp. 209-224 ◽

Cited By ~ 33

Author(s):

Kaowen Yan ◽

Li Li ◽

Xiaojian Wang ◽

Ruisha Hong ◽

Ying Zhang ◽

...

Keyword(s):

Mitotic Spindle ◽

Mammalian Cells ◽

Critical Role ◽

Spindle Assembly ◽

Mitotic Division ◽

Deubiquitinating Enzymes ◽

Mitotic Apparatus ◽

Protein Ubiquitination ◽

Assembly Factor ◽

Mitotic Spindle Assembly

Deubiquitinating enzymes (DUBs) negatively regulate protein ubiquitination and play an important role in diverse physiological processes, including mitotic division. The BRCC36 isopeptidase complex (BRISC) is a DUB that is specific for lysine 63–linked ubiquitin hydrolysis; however, its biological function remains largely undefined. Here, we identify a critical role for BRISC in the control of mitotic spindle assembly in cultured mammalian cells. BRISC is a microtubule (MT)-associated protein complex that predominantly localizes to the minus ends of K-fibers and spindle poles and directly binds to MTs; importantly, BRISC promotes the assembly of functional bipolar spindle by deubiquitinating the essential spindle assembly factor nuclear mitotic apparatus (NuMA). The deubiquitination of NuMA regulates its interaction with dynein and importin-β, which are required for its function in spindle assembly. Collectively, these results uncover BRISC as an important regulator of the mitotic spindle assembly and cell division, and have important implications for the development of anticancer drugs targeting BRISC.

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A homologue of the human regulator of mitotic spindle assembly protein (RMSA-1) is present in crane fly and is associated with meiotic chromosomes

Journal of Cell Science ◽

10.1242/jcs.107.7.1845 ◽

1994 ◽

Vol 107 (7) ◽

pp. 1845-1851

Author(s):

J.P. Yeo ◽

A. Forer ◽

B.H. Toh

Keyword(s):

Sex Chromosomes ◽

Mitotic Spindle ◽

Mammalian Cells ◽

Animal Species ◽

Spindle Assembly ◽

Meiotic Spindle ◽

Chromosomal Protein ◽

Meiotic Chromosomes ◽

Mitotic Spindle Assembly ◽

Cdc 2

In a previous study, we have shown that a newly identified chromosomal protein, RMSA-1 (Regulator of Mitotic Spindle Assembly-1), identified and cloned using a human autoimmune, serum, is essential for mitotic spindle assembly; we proposed that RMSA-1 was a previously unknown physiological substrate for cdc 2 kinase. In the present study, we show that this protein is present in crane fly and is associated with the chromosomes of spermatocytes. A 31 kDa molecule in extracts from crane-fly nuclei, isolated from larvae, pupae and adults, reacts with affinity-purified anti-RMSA-1 autoantibody, shown by immunoblotting. The autoantibody reacts, as shown by immunofluorescence, with crane-fly spermatocyte chromosomes in prophase through anaphase of both meiosis-1 and meiosis-II but does not react with preprophase or telophase nuclei or with spermatid nuclei. In all meiotic stages, the crane-fly sex chromosomes stain more intensely than the autosomes. We conclude that, since RMSA-1 is present in insect and mammalian cells, it is conserved across a variety of animal species. Further, since RMSA-1 binds to chromosomes in meiotic cells, it also may be essential for assembly of the meiotic spindle.

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