Prothymosin α interacts with SET, ANP32A and ANP32B and other cytoplasmic and mitochondrial proteins in proliferating cells
| Autor: | Carmen Freire-Cobo, Pablo Barbeito, Cristina Díaz-Jullien, David Moreira, Guillermo Covelo, Manuel Freire, C.S. Sarandeses, Juan Muras |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Cytoplasm Cell Survival Biophysics Biology Prothymosin Alpha Biochemistry Mitochondrial Proteins Jurkat Cells 03 medical and health sciences Protein Interaction Mapping Humans Histone Chaperones Protein Precursors Molecular Biology Cell Proliferation Cell growth Intracellular Signaling Peptides and Proteins Nuclear Proteins RNA-Binding Proteins Chromatin Cell biology DNA-Binding Proteins Thymosin 030104 developmental biology Histone Apoptosis biology.protein Apoptosome Function (biology) Signal Transduction Transcription Factors |
| Zdroj: | Archives of Biochemistry and Biophysics. 635:74-86 |
| ISSN: | 0003-9861 |
| Popis: | Prothymosin α (ProTα) is an acidic protein with a nuclear role related to the chromatin activity through its interaction with histones in mammalian cells. ProTα acts as an anti-apoptotic factor involved in the control of the apoptosome activity in the cytoplasm, however the mechanisms underlying this function are still known. ProTα shares similar biological functions with acidic nuclear-cytoplasmic shuttling proteins included in SET and ANP32 family members. Using affinity chromatography, co-immunoprecipitation and chemical cross-linking, we demonstrate that ProTα interacts with SET, ANP32A and ANP32B proteins. The study by mass spectrometry of the complexes stabilized by chemical cross-linking showed that associations of ProTα consist of six highly acidic ProTα-complexes, which corresponds to differentiated interactions of ProTα either with SET or ANP32 proteins. The presence in the ProTα-complexes of cytoplasmic proteins involved in membrane remodeling and proteins implicated in the mitochondrial permeability, seems to indicate that they could be related to a cytoplasmic-mitochondrial activity. According to the cellular function of the characterized targets of ProTα, and the evolution in the composition of the diverse ProTα-complexes when proliferation activity was reduced or apoptosis induced, leads to hypothesized that ProTα interactions might be related to the proliferation activity and control of the cell survival. |
| Databáze: | OpenAIRE |
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