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Larp6 Regulates Collagen mRNA by Targeted Unwinding of a Conserved Stem‐Loop
Author(s) -
Baggs Eric,
Warner Lisa
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.09740
Subject(s) - ribonucleoprotein , messenger rna , translation (biology) , microbiology and biotechnology , rna , extracellular matrix , rna binding protein , messenger rnp , chemistry , biology , biochemistry , gene
Collagen is the most abundant protein in the human body and a key component of the extracellular matrix. Regulation of collagen production in key to the development of fibroproliferative disorders; everything from scarring to cardiovascular disease. La ribonucleoprotein 6 (Larp6) is an RNA binding protein which has recently been shown to regulate collagen production by binding to a conserved region at the translation start site of collagen mRNA. This interaction appears to be critical to directing RNA to the rough ER for translation initiation. Additionally, LARP6 interaction with a number of molecular chaperones appears to be important for regulating collagen production. We hypothesize that LARP6 utilizes conformational selection in the recognition and discrimination of collagen mRNAs and that tertiary interactions dictate mRNA fate. In vitro RNA chaperone assays, translation assays, RNAi, confocal microscopy, and NMR and SAX structural studies are employed to interrogate these interactions. New information regarding the structures and dynamics that determine the Larp6 interaction with collagen mRNA may inform novel therapeutic targets that can mitigate fibroproliferative disease. Support or Funding Information P20GM109095