A regulatory effect of INMAP on centromere proteins: antisense INMAP induces CENP-B variation and centromeric halo.
CENP-B is a highly conserved protein that facilitates the assembly of specific centromere structures both in interphase nuclei and on mitotic chromosomes. INMAP is a conserved protein that localizes at nucleus in interphase cells and at mitotic apparatus in mitotic cells. Our previous results showed...
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doaj-9bcc410224f14e9dab4c7b3de95251ad2020-11-24T21:54:40ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0193e9193710.1371/journal.pone.0091937A regulatory effect of INMAP on centromere proteins: antisense INMAP induces CENP-B variation and centromeric halo.Tan TanZhe ChenYan LeiYan ZhuQianjin LiangCENP-B is a highly conserved protein that facilitates the assembly of specific centromere structures both in interphase nuclei and on mitotic chromosomes. INMAP is a conserved protein that localizes at nucleus in interphase cells and at mitotic apparatus in mitotic cells. Our previous results showed that INMAP over-expression leads to spindle defects, mitotic arrest and formation of polycentrosomal and multinuclear cells, indicating that INMAP may modulate the function of (a) key protein(s) in mitotic apparatus. In this study, we demonstrate that INMAP interacts with CENP-B and promotes cleavage of the N-terminal DNA binding domain from CENP-B. The cleaved CENP-B cannot associate with centromeres and thus lose its centromere-related functions. Consistent with these results, CENP-B in INMAP knockdown cells becomes more diffused around kinetochores. Although INMAP knockdown cells do not exhibit gross defects in mitotic spindle formation, these cells go through mitosis, especially prophase and metaphase, with different relative timing, indicating subtle abnormality. These results identify INMAP as a model regulator of CENP-B and support the notion that INMAP regulates mitosis through modulating CENP-B-mediated centromere organization.http://europepmc.org/articles/PMC3954832?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Tan Tan Zhe Chen Yan Lei Yan Zhu Qianjin Liang |
spellingShingle |
Tan Tan Zhe Chen Yan Lei Yan Zhu Qianjin Liang A regulatory effect of INMAP on centromere proteins: antisense INMAP induces CENP-B variation and centromeric halo. PLoS ONE |
author_facet |
Tan Tan Zhe Chen Yan Lei Yan Zhu Qianjin Liang |
author_sort |
Tan Tan |
title |
A regulatory effect of INMAP on centromere proteins: antisense INMAP induces CENP-B variation and centromeric halo. |
title_short |
A regulatory effect of INMAP on centromere proteins: antisense INMAP induces CENP-B variation and centromeric halo. |
title_full |
A regulatory effect of INMAP on centromere proteins: antisense INMAP induces CENP-B variation and centromeric halo. |
title_fullStr |
A regulatory effect of INMAP on centromere proteins: antisense INMAP induces CENP-B variation and centromeric halo. |
title_full_unstemmed |
A regulatory effect of INMAP on centromere proteins: antisense INMAP induces CENP-B variation and centromeric halo. |
title_sort |
regulatory effect of inmap on centromere proteins: antisense inmap induces cenp-b variation and centromeric halo. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2014-01-01 |
description |
CENP-B is a highly conserved protein that facilitates the assembly of specific centromere structures both in interphase nuclei and on mitotic chromosomes. INMAP is a conserved protein that localizes at nucleus in interphase cells and at mitotic apparatus in mitotic cells. Our previous results showed that INMAP over-expression leads to spindle defects, mitotic arrest and formation of polycentrosomal and multinuclear cells, indicating that INMAP may modulate the function of (a) key protein(s) in mitotic apparatus. In this study, we demonstrate that INMAP interacts with CENP-B and promotes cleavage of the N-terminal DNA binding domain from CENP-B. The cleaved CENP-B cannot associate with centromeres and thus lose its centromere-related functions. Consistent with these results, CENP-B in INMAP knockdown cells becomes more diffused around kinetochores. Although INMAP knockdown cells do not exhibit gross defects in mitotic spindle formation, these cells go through mitosis, especially prophase and metaphase, with different relative timing, indicating subtle abnormality. These results identify INMAP as a model regulator of CENP-B and support the notion that INMAP regulates mitosis through modulating CENP-B-mediated centromere organization. |
url |
http://europepmc.org/articles/PMC3954832?pdf=render |
work_keys_str_mv |
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