PIGN spatiotemporally regulates the spindle assembly checkpoint proteins in leukemia transformation and progression
Abstract Phosphatidylinositol glycan anchor biosynthesis class N (PIGN) has been linked to the suppression of chromosomal instability. The spindle assembly checkpoint complex is responsible for proper chromosome segregation during mitosis to prevent chromosomal instability. In this study, the novel...
Guardado en:
Autores principales: | , , , , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/de2cadc6ed4e4474b1a7633bdd7d1cd8 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:de2cadc6ed4e4474b1a7633bdd7d1cd8 |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:de2cadc6ed4e4474b1a7633bdd7d1cd82021-12-02T15:14:48ZPIGN spatiotemporally regulates the spindle assembly checkpoint proteins in leukemia transformation and progression10.1038/s41598-021-98218-y2045-2322https://doaj.org/article/de2cadc6ed4e4474b1a7633bdd7d1cd82021-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-98218-yhttps://doaj.org/toc/2045-2322Abstract Phosphatidylinositol glycan anchor biosynthesis class N (PIGN) has been linked to the suppression of chromosomal instability. The spindle assembly checkpoint complex is responsible for proper chromosome segregation during mitosis to prevent chromosomal instability. In this study, the novel role of PIGN as a regulator of the spindle assembly checkpoint was unveiled in leukemic patient cells and cell lines. Transient downregulation or ablation of PIGN resulted in impaired mitotic checkpoint activation due to the dysregulated expression of spindle assembly checkpoint-related proteins including MAD1, MAD2, BUBR1, and MPS1. Moreover, ectopic overexpression of PIGN restored the expression of MAD2. PIGN regulated the spindle assembly checkpoint by forming a complex with the spindle assembly checkpoint proteins MAD1, MAD2, and the mitotic kinase MPS1. Thus, PIGN could play a vital role in the spindle assembly checkpoint to suppress chromosomal instability associated with leukemic transformation and progression.Emmanuel K. TeyeShasha LuFangyuan ChenWenrui YangThomas AbrahamDouglas B. StairsHong-Gang WangGregory S. YochumRobert A. BrodskyJeffrey J. PuNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Medicine R Science Q |
spellingShingle |
Medicine R Science Q Emmanuel K. Teye Shasha Lu Fangyuan Chen Wenrui Yang Thomas Abraham Douglas B. Stairs Hong-Gang Wang Gregory S. Yochum Robert A. Brodsky Jeffrey J. Pu PIGN spatiotemporally regulates the spindle assembly checkpoint proteins in leukemia transformation and progression |
description |
Abstract Phosphatidylinositol glycan anchor biosynthesis class N (PIGN) has been linked to the suppression of chromosomal instability. The spindle assembly checkpoint complex is responsible for proper chromosome segregation during mitosis to prevent chromosomal instability. In this study, the novel role of PIGN as a regulator of the spindle assembly checkpoint was unveiled in leukemic patient cells and cell lines. Transient downregulation or ablation of PIGN resulted in impaired mitotic checkpoint activation due to the dysregulated expression of spindle assembly checkpoint-related proteins including MAD1, MAD2, BUBR1, and MPS1. Moreover, ectopic overexpression of PIGN restored the expression of MAD2. PIGN regulated the spindle assembly checkpoint by forming a complex with the spindle assembly checkpoint proteins MAD1, MAD2, and the mitotic kinase MPS1. Thus, PIGN could play a vital role in the spindle assembly checkpoint to suppress chromosomal instability associated with leukemic transformation and progression. |
format |
article |
author |
Emmanuel K. Teye Shasha Lu Fangyuan Chen Wenrui Yang Thomas Abraham Douglas B. Stairs Hong-Gang Wang Gregory S. Yochum Robert A. Brodsky Jeffrey J. Pu |
author_facet |
Emmanuel K. Teye Shasha Lu Fangyuan Chen Wenrui Yang Thomas Abraham Douglas B. Stairs Hong-Gang Wang Gregory S. Yochum Robert A. Brodsky Jeffrey J. Pu |
author_sort |
Emmanuel K. Teye |
title |
PIGN spatiotemporally regulates the spindle assembly checkpoint proteins in leukemia transformation and progression |
title_short |
PIGN spatiotemporally regulates the spindle assembly checkpoint proteins in leukemia transformation and progression |
title_full |
PIGN spatiotemporally regulates the spindle assembly checkpoint proteins in leukemia transformation and progression |
title_fullStr |
PIGN spatiotemporally regulates the spindle assembly checkpoint proteins in leukemia transformation and progression |
title_full_unstemmed |
PIGN spatiotemporally regulates the spindle assembly checkpoint proteins in leukemia transformation and progression |
title_sort |
pign spatiotemporally regulates the spindle assembly checkpoint proteins in leukemia transformation and progression |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/de2cadc6ed4e4474b1a7633bdd7d1cd8 |
work_keys_str_mv |
AT emmanuelkteye pignspatiotemporallyregulatesthespindleassemblycheckpointproteinsinleukemiatransformationandprogression AT shashalu pignspatiotemporallyregulatesthespindleassemblycheckpointproteinsinleukemiatransformationandprogression AT fangyuanchen pignspatiotemporallyregulatesthespindleassemblycheckpointproteinsinleukemiatransformationandprogression AT wenruiyang pignspatiotemporallyregulatesthespindleassemblycheckpointproteinsinleukemiatransformationandprogression AT thomasabraham pignspatiotemporallyregulatesthespindleassemblycheckpointproteinsinleukemiatransformationandprogression AT douglasbstairs pignspatiotemporallyregulatesthespindleassemblycheckpointproteinsinleukemiatransformationandprogression AT honggangwang pignspatiotemporallyregulatesthespindleassemblycheckpointproteinsinleukemiatransformationandprogression AT gregorysyochum pignspatiotemporallyregulatesthespindleassemblycheckpointproteinsinleukemiatransformationandprogression AT robertabrodsky pignspatiotemporallyregulatesthespindleassemblycheckpointproteinsinleukemiatransformationandprogression AT jeffreyjpu pignspatiotemporallyregulatesthespindleassemblycheckpointproteinsinleukemiatransformationandprogression |
_version_ |
1718387602970640384 |