scholarly journals The J Domain of Tpr2 Regulates Its Interaction with the Proapoptotic and Cell-Cycle Checkpoint Protein, Rad9

2001 ◽  
Vol 287 (4) ◽  
pp. 932-940 ◽  
Author(s):  
Shuang-Lin Xiang ◽  
Tomoyasu Kumano ◽  
Shu-ichi Iwasaki ◽  
Xiangao Sun ◽  
Kastuji Yoshioka ◽  
...  
1999 ◽  
Vol 145 (3) ◽  
pp. 425-435 ◽  
Author(s):  
Hong-Guo Yu ◽  
Michael G. Muszynski ◽  
R. Kelly Dawe

We have identified a maize homologue of yeast MAD2, an essential component in the spindle checkpoint pathway that ensures metaphase is complete before anaphase begins. Combined immunolocalization of MAD2 and a recently cloned maize CENPC homologue indicates that MAD2 localizes to an outer domain of the prometaphase kinetochore. MAD2 staining was primarily observed on mitotic kinetochores that lacked attached microtubules; i.e., at prometaphase or when the microtubules were depolymerized with oryzalin. In contrast, the loss of MAD2 staining in meiosis was not correlated with initial microtubule attachment but was correlated with a measure of tension: the distance between homologous or sister kinetochores (in meiosis I and II, respectively). Further, the tension-sensitive 3F3/2 phosphoepitope colocalized, and was lost concomitantly, with MAD2 staining at the meiotic kinetochore. The mechanism of spindle assembly (discussed here with respect to maize mitosis and meiosis) is likely to affect the relative contributions of attachment and tension. We support the idea that MAD2 is attachment-sensitive and that tension stabilizes microtubule attachments.


1996 ◽  
Vol 93 (7) ◽  
pp. 2850-2855 ◽  
Author(s):  
K. A. Cimprich ◽  
T. B. Shin ◽  
C. T. Keith ◽  
S. L. Schreiber

2006 ◽  
Vol 172 (5) ◽  
pp. 655-662 ◽  
Author(s):  
Dileep Varma ◽  
Denis L. Dujardin ◽  
Stephanie A. Stehman ◽  
Richard B. Vallee

Zeste white 10 (ZW10) is a mitotic checkpoint protein and the anchor for cytoplasmic dynein at mitotic kinetochores, though it is expressed throughout the cell cycle. We find that ZW10 localizes to pericentriolar membranous structures during interphase and cosediments with Golgi membranes. Dominant-negative ZW10, anti-ZW10 antibody, and ZW10 RNA interference (RNAi) caused Golgi dispersal. ZW10 RNAi also dispersed endosomes and lysosomes. Live imaging of Golgi, endosomal, and lysosomal markers after reduced ZW10 expression showed a specific decrease in the frequency of minus end–directed movements. Golgi membrane–associated dynein was markedly decreased, suggesting a role for ZW10 in dynein cargo binding during interphase. We also find ZW10 enriched at the leading edge of migrating fibroblasts, suggesting that ZW10 serves as a general regulator of dynein function throughout the cell cycle.


Nature ◽  
2018 ◽  
Vol 559 (7713) ◽  
pp. 274-278 ◽  
Author(s):  
Claudio Alfieri ◽  
Leifu Chang ◽  
David Barford

2016 ◽  
Vol 3 (6) ◽  
pp. 255-256 ◽  
Author(s):  
Liselot Dewachter ◽  
Natalie Verstraeten ◽  
Maarten Fauvart ◽  
Jan Michiels

2017 ◽  
Vol 72 (7-8) ◽  
pp. 325-334 ◽  
Author(s):  
Rui Li ◽  
Wenguo Wang ◽  
Fosheng Li ◽  
Qingwei Wang ◽  
Shenghua Wang ◽  
...  

AbstractRad9protein plays an important role in cell-cycle checkpoint signal transduction in human and yeast cells, but knowledge aboutRad9in plants is limited. This study reports that theRad9gene of rice can generate the transcript productsOsRad9.1andOsRad9.2through alternative splicing.OsRad9.1, with all nine exons, is the main cell-cycle checkpoint protein involved in the response of rice to genotoxic stresses (ultraviolet radiation and antibiotic stress), environmental stresses (drought, salt, and heavy metal stress), and auxin stimuli (2,4-D, IAA, and IBA). Meanwhile, transcript isoformOsRad9.2, which lost exon7 and exon8, showed different preferential stimulation effects on these stresses and pollen development duration. These results might indicat that besides the monitoring and repair of DNA damage,Rad9might involve in the development of pollen.


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