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

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

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.

Original languageEnglish
Pages (from-to)505-512
Number of pages8
JournalJournal of Clinical Investigation
Volume105
Issue number4
DOIs
StatePublished - Feb 2000

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