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

Autor: Alin Sela-Brown, Tally Naveh-Many, E. Epstein, Rachel Kilav, Justin Silver, Sharon E. Benashski, Israel Ringel, Joel K. Yisraeli, Stephen M. King
Rok vydání: 2000
Předmět:
Zdroj: Journal of Clinical Investigation. 105:505-512
ISSN: 0021-9738
DOI: 10.1172/jci8557
Popis: 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.
Databáze: OpenAIRE