Unknown

Dataset Information

0

Alignment of Mitotic Chromosomes in Human Cells Involves SR-Like Splicing Factors Btf and TRAP150.


ABSTRACT: Serine-arginine-rich (SR) or SR-like splicing factors interact with exon junction complex proteins during pre-mRNA processing to promote mRNA packaging into mature messenger ribonucleoproteins (mRNPs) and to dictate mRNA stability, nuclear export, and translation. The SR protein family is complex, and while many classical SR proteins have well-defined mRNA processing functions, those of other SR-like proteins is unclear. Here, we show that depletion of the homologous non-classical serine-arginine-rich (SR) splicing factors Bcl2-associated transcription factor (Btf or BCLAF) and thyroid hormone receptor-associated protein of 150 kDa (TRAP150) causes mitotic defects. We hypothesized that the depletion of these SR-like factors affects mitosis indirectly through an altered expression of mitotic checkpoint regulator transcripts. We observed an altered abundance of transcripts that encode mitotic regulators and mitotic chromosome misalignment defects following Btf and/or TRAP150 depletion. We propose that, in addition to their previously reported roles in maintaining mRNA distribution, Btf and TRAP150 control the abundance of transcripts encoding mitotic regulators, thereby affecting mitotic progression in human cells.

SUBMITTER: Varia S 

PROVIDER: S-EPMC5618605 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Alignment of Mitotic Chromosomes in Human Cells Involves SR-Like Splicing Factors Btf and TRAP150.

Varia Sapna S   Cheedu Divya D   Markey Michael M   Torres-Shafer Keshia K   Battini Vishnu Priya VP   Bubulya Athanasios A   Bubulya Paula A PA  

International journal of molecular sciences 20170912 9


Serine-arginine-rich (SR) or SR-like splicing factors interact with exon junction complex proteins during pre-mRNA processing to promote mRNA packaging into mature messenger ribonucleoproteins (mRNPs) and to dictate mRNA stability, nuclear export, and translation. The SR protein family is complex, and while many classical SR proteins have well-defined mRNA processing functions, those of other SR-like proteins is unclear. Here, we show that depletion of the homologous non-classical serine-arginin  ...[more]

Similar Datasets

2017-10-04 | GSE102465 | GEO
| S-EPMC9117150 | biostudies-literature
| S-EPMC6118306 | biostudies-literature
| S-EPMC3235224 | biostudies-literature
| S-EPMC3594322 | biostudies-literature
| S-EPMC6349114 | biostudies-literature
| S-EPMC8571045 | biostudies-literature
| S-EPMC420091 | biostudies-literature
| S-EPMC394518 | biostudies-other
| EMPIAR-11953 | biostudies-other