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Age-related SUMOylation of PLK1 is essential to meiosis progression in mouse oocytes.
Mo, Xiao-Long; Liu, Feng; Xing, Chun-Hua; Shan, Meng-Meng; Yao, Bo; Sun, Qi-Qi; Zou, Yuan-Jing; Zhang, Kun-Huan; Tan, Jun; Sun, Shao-Chen; Ren, Yan-Ping.
Afiliación
  • Mo XL; Department of Histology and Embryology, School of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou, China.
  • Liu F; Department of Histology and Embryology, School of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou, China.
  • Xing CH; College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu, China.
  • Shan MM; College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu, China.
  • Yao B; Department of Histology and Embryology, School of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou, China.
  • Sun QQ; Department of Histology and Embryology, School of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou, China.
  • Zou YJ; College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu, China.
  • Zhang KH; College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu, China.
  • Tan J; Department of Histology and Embryology, School of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou, China.
  • Sun SC; College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu, China.
  • Ren YP; Department of Histology and Embryology, School of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou, China.
J Cell Physiol ; 237(12): 4580-4590, 2022 12.
Article en En | MEDLINE | ID: mdl-36317691
Polo like kinase 1 (PLK1) is a protein kinase involved in regulating the spindle assembly and cell cycle control in mammalian oocytes. SUMOylation, one way of post-translational modification, regulates oocyte meiosis by controlling several substrates. However, the relation between PLK1 and SUMOylation in oocytes is still unknown. In this study, we investigated that whether PLK1 was modified by SUMOylation in oocytes and its potential relationship with age-related meiotic abnormalities. We showed that PLK1 had colocalization and protein interaction with Small Ubiquitin-Like Modifier (SUMO)-1 and SUMO-2/3 in mouse oocytes, indicating that PLK1 could be modified by SUMO-1 and SUMO-2/3. Overexpression of PLK1 SUMOylation site mutants PLK1K178R and PLK1K191R caused the increase of the abnormal spindle rate of oocytes and the decline of the first polar body extrusion rate with the abnormal localization of PLK1, suggesting that the SUMOylation modification of PLK1 is essential for normal meiosis in oocytes. Compared with young mice, the expression of PLK1 protein increased and the expression of SUMO-1 and SUMO-2/3 protein decreased in the oocytes of aged mice, indicating that the SUMOylation of PLK1 might be related to the mouse aging. Therefore, our data suggested that PLK1 could be SUMOylated by SUMO-1 and SUMO-2/3 in mouse oocytes and SUMOylation of PLK1 regulated the meiosis progression of oocytes which was related with aging.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oocitos / Proteínas Serina-Treonina Quinasas / Proteínas de Ciclo Celular / Sumoilación / Meiosis Límite: Animals Idioma: En Revista: J Cell Physiol Año: 2022 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oocitos / Proteínas Serina-Treonina Quinasas / Proteínas de Ciclo Celular / Sumoilación / Meiosis Límite: Animals Idioma: En Revista: J Cell Physiol Año: 2022 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos