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

One of the morphological hallmarks of terminally differentiated secretory cells is highly proliferated membrane of the rough endoplasmic reticulum (ER), but the molecular basis for the high rate of protein biosynthesis in these cells remains poorly documented. An important aspect of ER translational...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2019-05, Vol.116 (19), p.9340-9349
Main Authors: Ueno, Tomonori, Taga, Yuki, Yoshimoto, Rei, Mayeda, Akila, Hattori, Shunji, Ogawa-Goto, Kiyoko
Format: Article
Language:English
Subjects:
Assembly
Biological Sciences
Biosynthesis
Collagen
Endoplasmic reticulum
Endoplasmic Reticulum - genetics
Endoplasmic Reticulum - metabolism
Fibronectin
Humans
Membrane proteins
mRNA
PNAS Plus
Polyribosomes
Polyribosomes - genetics
Polyribosomes - metabolism
Protein Biosynthesis
Proteins
Receptors, Cytoplasmic and Nuclear - genetics
Receptors, Cytoplasmic and Nuclear - metabolism
RNA Splicing
RNA Splicing Factors - genetics
RNA Splicing Factors - metabolism
RNA, Messenger - genetics
RNA, Messenger - metabolism
RNA-binding protein
Splicing
Splicing factors
Translation
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Summary:One of the morphological hallmarks of terminally differentiated secretory cells is highly proliferated membrane of the rough endoplasmic reticulum (ER), but the molecular basis for the high rate of protein biosynthesis in these cells remains poorly documented. An important aspect of ER translational control is the molecular mechanism that supports efficient use of targeted mRNAs in polyribosomes. Here, we identify an enhancement system for ER translation promoted by p180, an integral ER membrane protein we previously reported as an essential factor for the assembly of ER polyribosomes. We provide evidence that association of target mRNAs with p180 is critical for efficient translation, and that SF3b4, an RNA-binding protein in the splicing factor SF3b, functions as a cofactor for p180 at the ER and plays a key role in enhanced translation of secretory proteins. A cis-element in the 5′ untranslated region of collagen and fibronectin genes is important to increase translational efficiency in the presence of p180 and SF3b4. These data demonstrate that a unique system comprising a p180–SF3b4–mRNA complex facilitates the selective assembly of polyribosomes on the ER.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1901742116