ANKRD53 interacts with DDA3 and regulates chromosome integrity during mitosis
- Authors
- Kim, Seul; Jang, Chang-Young
- Issue Date
- Feb-2016
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- ANKRD53; DDA3; Mitotic spindle; Chromosome movement; Spindle dynamics
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.470, no.3, pp 484 - 491
- Pages
- 8
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 470
- Number
- 3
- Start Page
- 484
- End Page
- 491
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/9945
- DOI
- 10.1016/j.bbrc.2016.01.144
- ISSN
- 0006-291X
1090-2104
- Abstract
- Spindle dynamics drives chromosome movement and mitotic progression during mitosis. Microtubule (MT)-associated proteins (MAPs) regulate MT stabilization/destabilization and MT polymerization/depolymerization for congression of sister chromatids at the mitotic equator and subsequent segregation toward the spindle poles. Here, we identified ANKRD53 as a novel DDA3-interacting protein through proteomic analysis. Based on expression profiles, ANKRD53 is phosphorylated by mitotic kinases during mitosis. In ANKRD53-depleted HeLa cells, the progression of mitosis was delayed and the number of unaligned chromosomes increased substantially. In addition, spindle MT polymerization decreased and the spindle assembly checkpoint (SAC) was concomitantly activated by the decreased spindle dynamics in ANKRD53-depleted cells. Although ANKRD53 is recruited to the mitotic spindle by DDA3, it counteracts the activity of DDA3 for spindle MT polymerization. Furthermore, ANKRD53 depletion increased the number of bi-nuclei and polylobed nuclei. Thus, ANKRD53 is recruited to the mitotic spindle by DDA3 and acts as a regulator of spindle dynamics and cytokinesis. (C) 2016 Elsevier Inc. All rights reserved.
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