徳島大学 教育・研究者情報データベース(EDB)

1. (英) Yamashita Koichiro

   役割	任意
   貢献度	任意
   学籍番号	推奨

2. (英) Tamura Shigehiko

   役割	任意
   貢献度	任意
   学籍番号	推奨

3. (英) Honsho Masanori

   役割	任意
   貢献度	任意
   学籍番号	推奨

4. (英) Yada Hiroto

   役割	任意
   貢献度	任意
   学籍番号	推奨

5. (英) Yagita Yuichi

   役割	任意
   貢献度	任意
   学籍番号	推奨

6. 小迫 英尊([徳島大学.先端酵素学研究所.基幹研究部門])

   役割	任意
   貢献度	任意
   学籍番号	推奨

7. (英) Fujiki Yukio

   役割	任意
   貢献度	任意
   学籍番号	推奨

(英) Mitotic phosphorylation of Pex14p regulates peroxisomal import machinery.

(英) Peroxisomal matrix proteins are imported into peroxisomes via membrane-bound docking/translocation machinery. One central component of this machinery is Pex14p, a peroxisomal membrane protein involved in the docking of Pex5p, the receptor for peroxisome targeting signal type 1 (PTS1). Studies in several yeast species have shown that Pex14p is phosphorylated in vivo, whereas no function has been assigned to Pex14p phosphorylation in yeast and mammalian cells. Here, we investigated peroxisomal protein import and its dynamics in mitotic mammalian cells. In mitotically arrested cells, Pex14p is phosphorylated at Ser-232, resulting in a lower import efficiency of catalase, but not the majority of proteins including canonical PTS1 proteins. Conformational change induced by the mitotic phosphorylation of Pex14p more likely increases homomeric interacting affinity and suppresses topological change of its N-terminal part, thereby giving rise to the retardation of Pex5p export in mitotic cells. Taken together, these data show that mitotic phosphorylation of Pex14p and consequent suppression of catalase import are a mechanism of protecting DNA upon nuclear envelope breakdown at mitosis.

1. (英) Article.ELocationID: e202001003

2. (英) Article.ELocationID: 10.1083/jcb.202001003

3. (英) Article.PublicationTypeList.PublicationType: Journal Article