scholarly journals Nuclear Mitotic Apparatus Protein 1

2020 ◽  
Author(s):  
2014 ◽  
Vol 443 (1) ◽  
pp. 259-265 ◽  
Author(s):  
Jae Sung Seo ◽  
Ha Na Kim ◽  
Sun-Jick Kim ◽  
Jiyoung Bang ◽  
Eun-A Kim ◽  
...  

1992 ◽  
Vol 3 (11) ◽  
pp. 1259-1267 ◽  
Author(s):  
C H Yang ◽  
M Snyder

The formation and maintenance of the bipolar mitotic spindle apparatus require a complex and balanced interplay of several mechanisms, including the stabilization and separation of polar microtubules and the action of various microtubule motors. Nonmicrotubule elements are also present throughout the spindle apparatus and have been proposed to provide a structural support for the spindle. The Nuclear-Mitotic Apparatus protein (NuMA) is an abundant 240 kD protein that is present in the nucleus of interphase cells and concentrates in the polar regions of the spindle apparatus during mitosis. Sequence analysis indicates that NuMA possesses an unusually long alpha-helical central region characteristic of many filament forming proteins. In this report we demonstrate that microinjection of anti-NuMA antibodies into interphase and prophase cells results in a failure to form a mitotic spindle apparatus. Furthermore, injection of metaphase cells results in the collapse of the spindle apparatus into a monopolar microtubule array. These results identify for the first time a nontubulin component important for both the establishment and stabilization of the mitotic spindle apparatus in multicellular organisms. We suggest that nonmicrotubule structural components may be important for these processes.


Author(s):  
Tomomi Kiyomitsu ◽  
Susan Boerner

The nuclear mitotic apparatus (NuMA) protein is well conserved in vertebrates, and dynamically changes its subcellular localization from the interphase nucleus to the mitotic/meiotic spindle poles and the mitotic cell cortex. At these locations, NuMA acts as a key structural hub in nuclear formation, spindle assembly, and mitotic spindle positioning, respectively. To achieve its variable functions, NuMA interacts with multiple factors, including DNA, microtubules, the plasma membrane, importins, and cytoplasmic dynein. The binding of NuMA to dynein via its N-terminal domain drives spindle pole focusing and spindle positioning, while multiple interactions through its C-terminal region define its subcellular localizations and functions. In addition, NuMA can self-assemble into high-ordered structures which likely contribute to spindle positioning and nuclear formation. In this review, we summarize recent advances in NuMA’s domains, functions and regulations, with a focus on human NuMA, to understand how and why vertebrate NuMA participates in these functions in comparison with invertebrate NuMA-related proteins.


Genomics ◽  
1993 ◽  
Vol 17 (1) ◽  
pp. 222-224 ◽  
Author(s):  
Cynthia A. Sparks ◽  
Peter L. Bangs ◽  
Gerard P. McNeil ◽  
Jeanne B. Lawrence ◽  
Edward G. Fey

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