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mTORC1 phosphorylates LARP6 to stimulate type I collagen expression.

Sci Rep. 2017 Jan 23;7:41173
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摘要


Excessive deposition of type I collagen causes fibrotic diseases. Binding of La ribonucleoprotein domain family, member 6 to collagen mRNAs regulates their translation and is necessary for high type I collagen expression. Here we show that mTORC1 phosphorylates on S348 and S409. The S348A/S409A mutant of Lduanyu376 acts as a dominant negative protein in collagen biosynthesis, which retards secretion of type I collagen and causes excessive posttranslational modifications. Similar effects are seen using mTORC1 inhibitor rapamycin or by knocking down raptor. The S348A/S409A mutant weakly interacts with the accessory protein STRAP, needed for coordinated translation of collagen mRNAs. The interaction of wt Lduanyu376 and STRAP is also attenuated by rapamycin and by raptor knockdown. Additionally, in the absence of S348/S409 phosphorylation Lduanyu376 is sequestered in increasing amounts at the ER membrane. We postulate that phosphorylation of S348/S409 by mTORC1 stimulates the interaction of Lduanyu376 and STRAP to coordinate translation of collagen mRNAs and to release Lduanyu376 from the ER for new round of translation. These mechanisms contribute to high level of collagen expression in fibrosis.

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