Yumi Uetake
University of Massachusetts Medical School
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Featured researches published by Yumi Uetake.
Journal of Cell Biology | 2004
Yumi Uetake; Greenfield Sluder
Failure of cells to cleave at the end of mitosis is dangerous to the organism because it immediately produces tetraploidy and centrosome amplification, which is thought to produce genetic imbalances. Using normal human and rat cells, we reexamined the basis for the attractive and increasingly accepted proposal that normal mammalian cells have a “tetraploidy checkpoint” that arrests binucleate cells in G1, thereby preventing their propagation. Using 10 μM cytochalasin to block cleavage, we confirm that most binucleate cells arrest in G1. However, when we use lower concentrations of cytochalasin, we find that binucleate cells undergo DNA synthesis and later proceed through mitosis in >80% of the cases for the hTERT-RPE1 human cell line, primary human fibroblasts, and the REF52 cell line. These observations provide a functional demonstration that the tetraploidy checkpoint does not exist in normal mammalian somatic cells.
Journal of Cell Biology | 2007
Yumi Uetake; Jadranka Loncarek; Joshua J. Nordberg; Christopher N. English; Sabrina La Terra; Alexey Khodjakov; Greenfield Sluder
How centrosome removal or perturbations of centrosomal proteins leads to G1 arrest in untransformed mammalian cells has been a mystery. We use microsurgery and laser ablation to remove the centrosome from two types of normal human cells. First, we find that the cells assemble centrioles de novo after centrosome removal; thus, this phenomenon is not restricted to transformed cells. Second, normal cells can progress through G1 in its entirety without centrioles. Therefore, the centrosome is not a necessary, integral part of the mechanisms that drive the cell cycle through G1 into S phase. Third, we provide evidence that centrosome loss is, functionally, a stress that can act additively with other stresses to arrest cells in G1 in a p38-dependent fashion.
Journal of Cell Biology | 2002
Ryoko Kuriyama; C. Gustus; Yasuhiko Terada; Yumi Uetake; Jurgita Matuliene
CHO1 is a kinesin-like protein of the mitotic kinesin-like protein (MKLP)1 subfamily present in central spindles and midbodies in mammalian cells. It is different from other subfamily members in that it contains an extra ∼300 bp in the COOH-terminal tail. Analysis of the chicken genomic sequence showed that heterogeneity is derived from alternative splicing, and exon 18 is expressed in only the CHO1 isoform. CHO1 and its truncated isoform MKLP1 are coexpressed in a single cell. Surprisingly, the sequence encoded by exon 18 possesses a capability to interact with F-actin, suggesting that CHO1 can associate with both microtubule and actin cytoskeletons. Microinjection of exon 18–specific antibodies did not result in any inhibitory effects on karyokinesis and early stages of cytokinesis. However, almost completely separated daughter cells became reunited to form a binulceate cell, suggesting that the exon 18 protein may not have a role in the formation and ingression of the contractile ring in the cortex. Rather, it might be involved directly or indirectly in the membrane events necessary for completion of the terminal phase of cytokinesis.
Journal of Cell Biology | 2002
Toshiro Ohta; Russell Essner; Jung Hwa Ryu; Robert E. Palazzo; Yumi Uetake; Ryoko Kuriyama
By using monoclonal antibodies raised against isolated clam centrosomes, we have identified a novel 135-kD centrosomal protein (Cep135), present in a wide range of organisms. Cep135 is located at the centrosome throughout the cell cycle, and localization is independent of the microtubule network. It distributes throughout the centrosomal area in association with the electron-dense material surrounding centrioles. Sequence analysis of cDNA isolated from CHO cells predicted a protein of 1,145–amino acid residues with extensive α-helical domains. Expression of a series of deletion constructs revealed the presence of three independent centrosome-targeting domains. Overexpression of Cep135 resulted in the accumulation of unique whorl-like particles in both the centrosome and the cytoplasm. Although their size, shape, and number varied according to the level of protein expression, these whorls were composed of parallel dense lines arranged in a 6-nm space. Altered levels of Cep135 by protein overexpression and/or suppression of endogenous Cep135 by RNA interference caused disorganization of interphase and mitotic spindle microtubules. Thus, Cep135 may play an important role in the centrosomal function of organizing microtubules in mammalian cells.
Journal of Cell Biology | 2003
Yasuhiko Terada; Yumi Uetake; Ryoko Kuriyama
A mitosis-specific Aurora-A kinase has been implicated in microtubule organization and spindle assembly in diverse organisms. However, exactly how Aurora-A controls the microtubule nucleation onto centrosomes is unknown. Here, we show that Aurora-A specifically binds to the COOH-terminal domain of a Drosophila centrosomal protein, centrosomin (CNN), which has been shown to be important for assembly of mitotic spindles and spindle poles. Aurora-A and CNN are mutually dependent for localization at spindle poles, which is required for proper targeting of γ-tubulin and other centrosomal components to the centrosome. The NH2-terminal half of CNN interacts with γ-tubulin, and induces cytoplasmic foci that can initiate microtubule nucleation in vivo and in vitro in both Drosophila and mammalian cells. These results suggest that Aurora-A regulates centrosome assembly by controlling the CNNs ability to targeting and/or anchoring γ-tubulin to the centrosome and organizing microtubule-nucleating sites via its interaction with the COOH-terminal sequence of CNN.
Current Biology | 2010
Yumi Uetake; Greenfield Sluder
The mitotic checkpoint maintains genomic stability by blocking the metaphase-anaphase transition until all kinetochores attach to spindle microtubules [1, 2]. However, some defects are not detected by this checkpoint. With low concentrations of microtubule-targeting agents, the checkpoint eventually becomes satisfied, though the spindles may be short and/or multipolar [3, 4] and the fidelity of chromosome distribution and cleavage completion are compromised. In real life, environmental toxins, radiation, or chemotherapeutic agents may lead to completed but inaccurate mitoses. It has been assumed that once the checkpoint is satisfied and cells divide, the daughter cells would proliferate regardless of prometaphase duration. However, when continuously exposed to microtubule inhibitors, untransformed cells eventually slip out of mitosis after 12-48 hr and arrest in G1 [5-8] (see also [9]). Interestingly, transient but prolonged treatments with nocodazole allow completion of mitosis, but the daughter cells arrest in interphase [10, 11] (see also [9, 12]). Here we characterize the relationship between prometaphase duration and the proliferative capacity of daughter cells. Our results reveal the existence of a mechanism that senses prometaphase duration; if prometaphase lasts >1.5 hr, this mechanism triggers a durable p38- and p53-dependent G1 arrest of the daughter cells despite normal division of their mothers.
Journal of Cell Biology | 2015
Bramwell G. Lambrus; Yumi Uetake; Kevin M. Clutario; Vikas Daggubati; Michael Snyder; Greenfield Sluder; Andrew J. Holland
Reversible depletion of centrioles uncovers a p53-dependent pathway that protects against genome instability following centriole duplication failure.
Journal of Cell Biology | 2016
Bramwell G. Lambrus; Vikas Daggubati; Yumi Uetake; Phillip Scott; Kevin M. Clutario; Greenfield Sluder; Andrew J. Holland
Lambrus et al. show that centrosome loss or a prolonged mitosis activates a USP28–53BP1–p53–p21 signaling axis that prevents the growth of cells with an increased propensity for mitotic errors.
Biomedical Optical Phase Microscopy and Nanoscopy | 2012
Yumi Uetake; Greenfield Sluder
This chapter provides an overview of the commonly used methods for long-term live cell time-lapse analysis of individual untransformed human cells. A detailed discussion on phase contrast and differential interference contrast (DIC) microscopy is presented. It provides information on illumination, temperature control, and focus stability. This is followed by some general considerations of the optical systems suitable for live cell time-lapse analysis. It discusses the construction and preparation of culture chamber for the use of sealed cell preparations. It also provides brief information on phototoxicity of live cells under observation. Finally, the chapter concludes with a discussion on correlative immunofluorescence characterization of cells previously followed in vivo.
Current Biology | 2007
Yumi Uetake; Greenfield Sluder