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Dynein light chain binding to a 3′-untranslated sequence mediates parathyroid hormone mRNA association with microtubules
Eyal Epstein, … , Justin Silver, Tally Naveh-Many
Eyal Epstein, … , Justin Silver, Tally Naveh-Many
Published February 15, 2000
Citation Information: J Clin Invest. 2000;105(4):505-512. https://doi.org/10.1172/JCI8557.
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Article

Dynein light chain binding to a 3′-untranslated sequence mediates parathyroid hormone mRNA association with microtubules

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Abstract

The 3′-untranslated region (UTR) of mRNAs binds proteins that determine mRNA stability and localization. The 3′-UTR of parathyroid hormone (PTH) mRNA specifically binds cytoplasmic proteins. We screened an expression library for proteins that bind the PTH mRNA 3′-UTR, and the sequence of 1 clone was identical to that of the dynein light chain LC8, a component of the dynein complexes that translocate cytoplasmic components along microtubules. Recombinant LC8 binds PTH mRNA 3′-UTR, as shown by RNA electrophoretic mobility shift assay. We showed that PTH mRNA colocalizes with microtubules in the parathyroid gland, as well as with a purified microtubule preparation from calf brain, and that this association was mediated by LC8. To our knowledge, this is the first report of a dynein complex protein binding an mRNA. The dynein complex may be the motor that is responsible for transporting mRNAs to specific locations in the cytoplasm and for the consequent is asymmetric distribution of translated proteins in the cell.

Authors

Eyal Epstein, Alin Sela-Brown, Israel Ringel, Rachel Kilav, Stephen M. King, Sharon E. Benashski, Joel K. Yisraeli, Justin Silver, Tally Naveh-Many

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