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Control of the localization and function of a miRNA silencing component TNRC6A by Argonaute protein

Kenji Nishi1, Tomoko Takahashi1, Masataka Suzawa1

  • 1Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan.

Nucleic Acids Research
|October 9, 2015
PubMed

Insights

GW182 proteins like TNRC6A regulate microRNA (miRNA) silencing. Their location in processing bodies is controlled by Argonaute (Ago) protein interactions, impacting RNA silencing activity.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • GW182 family proteins are crucial for microRNA (miRNA)-mediated RNA silencing.
  • These proteins interact with Argonaute (Ago) proteins within processing bodies (P bodies), key sites for mRNA decay and storage.
  • TNRC6A, a human GW182 protein, shuttles between the nucleus and cytoplasm, with localization governed by its signals.

Purpose of the Study:

  • To investigate the regulatory mechanisms controlling TNRC6A subcellular localization.
  • To understand how TNRC6A interacts with Argonaute proteins and its impact on RNA silencing.

Main Methods:

  • Studied TNRC6A as a nuclear-cytoplasmic shuttling protein.
  • Investigated TNRC6A interaction with Ago2 under overexpression conditions in HeLa cells.
  • Examined the role of Ago-bound small RNAs in tethering Ago proteins to P bodies.

Main Results:

  • TNRC6A is tethered to P bodies through direct interaction with Ago2 when Ago2 is overexpressed.
  • Ago proteins appear to be strongly anchored in P bodies via Ago-bound small RNAs.
  • TNRC6A subcellular localization significantly influences its RNA silencing efficacy.

Conclusions:

  • TNRC6A subcellular localization is primarily controlled by interactions with Argonaute proteins.
  • The interplay between TNRC6A, Ago proteins, and small RNAs dictates RNA silencing activity.

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