| Autor: |
Alexandra Hencz, Edina Szabó-Meleg, Muhammad Yaqoob Dayo, Ardora Bilibani, Szilvia Barkó, Miklós Nyitrai, Dávid Szatmári |
| Rok vydání: |
2022 |
| Předmět: |
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| Zdroj: |
International Journal of Molecular Sciences; Volume 23; Issue 16; Pages: 9078 |
| ISSN: |
1422-0067 |
| Popis: |
Long-term cellular stress maintains high intracellular Ca2+ concentrations which ultimately initiates apoptosis. Our interest is focused on how the gelsolin (GSN) and junctional mediating and regulating Y protein (JMY) play important roles in stress response. Both of these proteins can bind p53 and actin. We investigated using in vitro fluorescence spectroscopy and found that the p53 competes with actin in GSN to inhibit p53–JMY complex formation. A high Ca2+ level initializes p53 dimerization; the dimer competes with actin on JMY, which can lead to p53–JMY cotransport into the nucleus. Here we investigated how the motility and division rate of HeLa cells changes due to low-voltage electroporation of GSN or JMY in scratching assays. We revealed that JMY inhibits their motion, but that it can accelerate the cell division. GSN treatment slows down cell division but does not affect cell motility. HeLa cells fully recovered the gap 20 h after the electroporation with JMY and then started to release from the glass slides. Taken together, our in vitro results indicate that GSN and JMY may play an important role in the cellular stress response. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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