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ESCRT-III controls nuclear envelope reformation

Author

Listed:
  • Yolanda Olmos

    (Section of Cell Biology and Imaging, King's College London)

  • Lorna Hodgson

    (School of Biochemistry, University of Bristol, Medical Sciences Building, University Walk)

  • Judith Mantell

    (School of Biochemistry, University of Bristol, Medical Sciences Building, University Walk
    Wolfson Bioimaging Facility, University of Bristol)

  • Paul Verkade

    (School of Biochemistry, University of Bristol, Medical Sciences Building, University Walk
    Wolfson Bioimaging Facility, University of Bristol
    School of Physiology & Pharmacology, University of Bristol)

  • Jeremy G. Carlton

    (Section of Cell Biology and Imaging, King's College London)

Abstract

The ESCRT-III complex is implicated in the reformation of the nuclear envelope; the CHMP2A component of ESCRT-III is directed to the forming nuclear envelope through classical ESCRT-assembly mechanisms, with the help of the p97 complex component UFD1, and provides an activity essential for nuclear envelope reformation.

Suggested Citation

  • Yolanda Olmos & Lorna Hodgson & Judith Mantell & Paul Verkade & Jeremy G. Carlton, 2015. "ESCRT-III controls nuclear envelope reformation," Nature, Nature, vol. 522(7555), pages 236-239, June.
    • Handle: RePEc:nat:nature:v:522:y:2015:i:7555:d:10.1038_nature14503
    DOI: 10.1038/nature14503
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    Cited by:

    1. Tomoyuki Hatano & Saravanan Palani & Dimitra Papatziamou & Ralf Salzer & Diorge P. Souza & Daniel Tamarit & Mehul Makwana & Antonia Potter & Alexandra Haig & Wenjue Xu & David Townsend & David Rochest, 2022. "Asgard archaea shed light on the evolutionary origins of the eukaryotic ubiquitin-ESCRT machinery," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Yonglun Zeng & Baiying Li & Shuxian Huang & Hongbo Li & Wenhan Cao & Yixuan Chen & Guoyong Liu & Zhenping Li & Chao Yang & Lei Feng & Jiayang Gao & Sze Wan Lo & Jierui Zhao & Jinbo Shen & Yan Guo & Ca, 2023. "The plant unique ESCRT component FREE1 regulates autophagosome closure," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

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