Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 9340-9349 |
| Number of pages | 10 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 116 |
| Issue number | 19 |
| DOIs | |
| Publication status | Published - 07-05-2019 |
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Component of splicing factor SF3b plays a key role in translational control of polyribosomes on the endoplasmic reticulum. / Ueno, Tomonori; Taga, Yuki; Yoshimoto, Rei; Mayeda, Akila; Hattori, Shunji; Ogawa-Goto, Kiyoko.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 116, No. 19, 07.05.2019, p. 9340-9349.Research output: Contribution to journal › Article
TY - JOUR
T1 - Component of splicing factor SF3b plays a key role in translational control of polyribosomes on the endoplasmic reticulum
AU - Ueno, Tomonori
AU - Taga, Yuki
AU - Yoshimoto, Rei
AU - Mayeda, Akila
AU - Hattori, Shunji
AU - Ogawa-Goto, Kiyoko
PY - 2019/5/7
Y1 - 2019/5/7
N2 - 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.
AB - 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.
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U2 - 10.1073/pnas.1901742116
DO - 10.1073/pnas.1901742116
M3 - Article
C2 - 31004060
AN - SCOPUS:85065615352
VL - 116
SP - 9340
EP - 9349
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 19
ER -