PGSE Is a Novel Enhancer Regulating the Proteoglycan Pathway of the Mammalian Golgi Stress Response

DOI Web Site PubMed 2 Citations 54 References Open Access
  • Sasaki Kanae
    Department of Molecular Biochemistry, Graduate School of Life Science, University of Hyogo
  • Komori Ryota
    Department of Molecular Biochemistry, Graduate School of Life Science, University of Hyogo
  • Taniguchi Mai
    Department of Molecular Biochemistry, Graduate School of Life Science, University of Hyogo
  • Shimaoka Akie
    Department of Molecular Biochemistry, Graduate School of Life Science, University of Hyogo
  • Midori Sachiko
    Department of Molecular Biochemistry, Graduate School of Life Science, University of Hyogo
  • Yamamoto Mayu
    Department of Molecular Biochemistry, Graduate School of Life Science, University of Hyogo
  • Okuda Chiho
    Department of Molecular Biochemistry, Graduate School of Life Science, University of Hyogo
  • Tanaka Ryuya
    Department of Molecular Biochemistry, Graduate School of Life Science, University of Hyogo
  • Sakamoto Miyu
    Department of Molecular Biochemistry, Graduate School of Life Science, University of Hyogo
  • Wakabayashi Sadao
    Department of Molecular Biochemistry, Graduate School of Life Science, University of Hyogo
  • Yoshida Hiderou
    Department of Molecular Biochemistry, Graduate School of Life Science, University of Hyogo

Search this article

Abstract

<p>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.</p><p>Key words: Golgi stress, proteoglycan, ER stress, organelle zone, organelle autoregulation</p>

Journal

Citations (2)*help

See more

References(54)*help

See more

Related Projects

See more

Keywords

Details

Report a problem

Back to top