Component of splicing factor SF3b plays a key role in translational control of polyribosomes on the endoplasmic reticulum

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  • Tomonori Ueno
    Nippi Research Institute of Biomatrix, Toride, 302-0017 Ibaraki, Japan;
  • Yuki Taga
    Nippi Research Institute of Biomatrix, Toride, 302-0017 Ibaraki, Japan;
  • Rei Yoshimoto
    Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, 470-1192 Aichi, Japan;
  • Akila Mayeda
    Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, 470-1192 Aichi, Japan;
  • Shunji Hattori
    Nippi Research Institute of Biomatrix, Toride, 302-0017 Ibaraki, Japan;
  • Kiyoko Ogawa-Goto
    Nippi Research Institute of Biomatrix, Toride, 302-0017 Ibaraki, Japan;

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<jats:title>Significance</jats:title> <jats:p> p180/ <jats:italic>RRBP1</jats:italic> is an essential factor for high-rate protein synthesis on the endoplasmic reticulum (ER) in terminally differentiated secretory cells. A unique system for selectively enhanced translation has been proposed for p180-associated polyribosomes. Here we provide evidence that SF3b4, an RNA-binding protein in the splicing factor, plays a key and unexpected role in translation control as a cofactor for p180. It appears that abundant expression of both SF3b4 and p180 is critical for increased ER mRNA targeting, and consequently leads to the heavy polyribosome assembly. This discovery could shed light on the pathogenesis of Nager syndrome caused by <jats:italic>SF3B4</jats:italic> mutation, as such mutations may result in abnormal collagen biosynthesis, potentially affecting bone morphogenesis in patients with this disease. </jats:p>

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