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Identification of an AGO (Argonaute) protein as a prey of TER94/VCP.

Authors
  • Kobayashi, Hotaka1
  • Tomari, Yukihide1, 2
  • 1 Laboratory of RNA Function, Institute for Quantitative Biosciences, The University of Tokyo, Tokyo, Japan. , (Japan)
  • 2 Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Tokyo, Japan. , (Japan)
Type
Published Article
Journal
Autophagy
Publisher
Landes Bioscience
Publication Date
Nov 12, 2019
Pages
1–3
Identifiers
DOI: 10.1080/15548627.2019.1691351
PMID: 31718417
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

VCP (valosin containing protein) recognizes a wide variety of substrates and mediates their degradation via the ubiquitin-proteasome system and macroautophagy/autophagy. The substrate repertoire of VCP, however, is not fully understood. In our recent study, we found that Drosophila TER94/VCP mediates autophagic degradation of an Argonaute subfamily protein (AGO1), which binds microRNAs (miRNAs) and silences the expression of thousands of target genes. In the absence of TER94/VCP, miRNA-mediated gene silencing is globally impaired. Our findings reveal an unexpected connection between VCP and AGO, which may dramatically expand the biological significance of VCP.

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