Quantitative analysis of argonaute protein reveals microRNA-dependent localization to stress granules

Anthony K.L. Leung, J. Mauro Calabrese, Phillip A. Sharp

Research output: Contribution to journalArticlepeer-review

Abstract

Argonaute proteins associate with microRNAs (miRNAs) that bind mRNAs through partial base-pairings to primarily repress translation in animals. A fraction of Argonaute proteins and miRNAs biochemically cosediment with polyribosomes, yet another fraction paradoxically accumulates in ribosome-free processing bodies (PBs) in the cytoplasm. In this report, we give a quantitative account of the Argonaute protein localization and dynamics in living cells in different cellular states. We find that the majority of Argonaute is distributed diffusely in the cytoplasm, and, when cells are subjected to stress. Argonaute proteins accumulate to newly assembled structures known as stress granules (SGs) in addition to PBs. Argonaute proteins displayed distinct kinetics at different structures: exchange faster at SGs and much slower at PBs. Further, miRNAs are required for the Argonaute protein localization to SGs but not PBs. These quantitative kinetic data provide insights into miRNA-mediated repression.

Original languageEnglish (US)
Pages (from-to)18125-18130
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume103
Issue number48
DOIs
StatePublished - Nov 28 2006
Externally publishedYes

Keywords

  • Dynamics
  • Fluorescence microscopy
  • Post-transcriptional control
  • Processing bodies

ASJC Scopus subject areas

  • General

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