| First Author | Vukmirovic M | Year | 2013 |
| Journal | Mol Cell Biol | Volume | 33 |
| Issue | 19 | Pages | 3893-906 |
| PubMed ID | 23918805 | Mgi Jnum | J:205011 |
| Mgi Id | MGI:5543870 | Doi | 10.1128/MCB.00195-13 |
| Citation | Vukmirovic M, et al. (2013) Serine-threonine kinase receptor-associated protein (STRAP) regulates translation of type I collagen mRNAs. Mol Cell Biol 33(19):3893-906 |
| abstractText | Type I collagen is the most abundant protein in the human body and is composed of two alpha1(I) and one alpha2(I) polypeptides which assemble into a triple helix. For the proper assembly of the collagen triple helix, the individual polypeptides must be translated in coordination. Here, we show that serine-threonine kinase receptor-associated protein (STRAP) is tethered to collagen mRNAs by interaction with LARP6. LARP6 is a protein which directly binds the 5' stem-loop (5'SL) present in collagen alpha1(I) and alpha2(I) mRNAs, but it interacts with STRAP with its C-terminal domain, which is not involved in binding 5'SL. Being tethered to collagen mRNAs, STRAP prevents unrestricted translation, primarily that of collagen alpha2(I) mRNAs, by interacting with eukaryotic translation initiation factor 4A (eIF4A). In the absence of STRAP, more collagen alpha2(I) mRNA can be pulled down with eIF4A, and collagen alpha2(I) mRNA is unrestrictedly loaded onto the polysomes. This results in an imbalance of synthesis of alpha1(I) and alpha2(I) polypeptides, in hypermodifications of alpha1(I) polypeptide, and in inefficient assembly of the polypeptides into a collagen trimer and their secretion as monomers. These defects can be partially restored by supplementing STRAP. Thus, we discovered STRAP as a novel regulator of the coordinated translation of collagen mRNAs. |
