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HTRA1-Dependent Cell Cycle Proteomics
- Source :
- Journal of Proteome Research. 17:2679-2694
- Publication Year :
- 2018
- Publisher :
- American Chemical Society (ACS), 2018.
-
Abstract
- The HTRA1 gene encoding an evolutionary conserved protein quality-control factor can be epigenetically silenced or inactivated by mutation under pathologic conditions such as cancer. Recent evidence suggests that the loss of HTRA1 function causes multiple phenotypes, including the acceleration of cell growth, delayed onset of senescence, centrosome amplification, and polyploidy, suggesting an implication in the regulation of the cell cycle. To address this model, we performed a large-scale proteomics study to correlate the abundance of proteins and HTRA1 levels in various cell cycle phases using label-free-quantification mass spectrometry. These data indicate that the levels of 4723 proteins fluctuated in a cell-cycle-dependent manner, 2872 in a HTRA1-dependent manner, and 1530 in a cell-cycle- and HTRA1-dependent manner. The large number of proteins affected by the modulation of HTRA1 levels supports its general role in protein homeostasis. Moreover, the detected changes in protein abundance, in combination with pull-down data, implicate HTRA1 in various cell cycle events such as DNA replication, chromosome segregation, and cell-cycle-dependent apoptosis. These results highlight the wide implications of HTRA1 in cellular physiology.
- Subjects :
- DNA Replication
Proteomics
0301 basic medicine
Cell physiology
Senescence
Apoptosis
Biology
medicine.disease_cause
Biochemistry
Mass Spectrometry
03 medical and health sciences
0302 clinical medicine
Chromosome Segregation
medicine
Homeostasis
Humans
Analysis of Variance
Mutation
Cell growth
Cell Cycle
DNA replication
Proteins
High-Temperature Requirement A Serine Peptidase 1
General Chemistry
Cell cycle
eye diseases
Cell biology
030104 developmental biology
Gene Expression Regulation
Centrosome
030220 oncology & carcinogenesis
Biologie
Subjects
Details
- ISSN :
- 15353907 and 15353893
- Volume :
- 17
- Database :
- OpenAIRE
- Journal :
- Journal of Proteome Research
- Accession number :
- edsair.doi.dedup.....7be8b624f087070a775b341a1fdc73af