Cell Structure and Function
Online ISSN : 1347-3700
Print ISSN : 0386-7196
最新号
選択された号の論文の1件中1~1を表示しています
  • Kanae Sasaki, Ryota Komori, Mai Taniguchi, Akie Shimaoka, Sachiko Mido ...
    原稿種別: Full Article
    2019 年 44 巻 1 号 p. 1-19
    発行日: 2019年
    公開日: 2019/01/11
    [早期公開] 公開日: 2018/11/28
    ジャーナル オープンアクセス HTML

    The Golgi stress response is a homeostatic mechanism that augments the functional capacity of the Golgi apparatus when Golgi function becomes insufficient (Golgi stress). Three response pathways of the Golgi stress response have been identified in mammalian cells, the TFE3, HSP47 and CREB3 pathways, which augment the capacity of specific Golgi functions such as N-glycosylation, anti-apoptotic activity and pro-apoptotic activity, respectively. On the contrary, glycosylation of proteoglycans (PGs) is another important function of the Golgi, although the response pathway upregulating expression of glycosylation enzymes for PGs in response to Golgi stress remains unknown. Here, we found that expression of glycosylation enzymes for PGs was induced upon insufficiency of PG glycosylation capacity in the Golgi (PG-Golgi stress), and that transcriptional induction of genes encoding glycosylation enzymes for PGs was independent of the known Golgi stress response pathways and ER stress response. Promoter analyses of genes encoding these glycosylation enzymes revealed the novel enhancer elements PGSE-A and PGSE-B (the consensus sequences are CCGGGGCGGGGCG and TTTTACAATTGGTC, respectively), which regulate their transcriptional induction upon PG-Golgi stress. From these observations, the response pathway we discovered is a novel Golgi stress response pathway, which we have named the PG pathway.

    Key words: Golgi stress, proteoglycan, ER stress, organelle zone, organelle autoregulation

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