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FerriTag is a new genetically-encoded inducible tag for correlative light-electron microscopy

Author

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  • Nicholas I. Clarke

    (Warwick Medical School)

  • Stephen J. Royle

    (Warwick Medical School)

Abstract

A current challenge is to develop tags to precisely visualize proteins in cells by light and electron microscopy. Here, we introduce FerriTag, a genetically-encoded chemically-inducible tag for correlative light-electron microscopy. FerriTag is a fluorescent recombinant electron-dense ferritin particle that can be attached to a protein-of-interest using rapamycin-induced heterodimerization. We demonstrate the utility of FerriTag for correlative light-electron microscopy by labeling proteins associated with various intracellular structures including mitochondria, plasma membrane, and clathrin-coated pits and vesicles. FerriTagging has a good signal-to-noise ratio and a labeling resolution of approximately 10 nm. We demonstrate how FerriTagging allows nanoscale mapping of protein location relative to a subcellular structure, and use it to detail the distribution and conformation of huntingtin-interacting protein 1 related (HIP1R) in and around clathrin-coated pits.

Suggested Citation

  • Nicholas I. Clarke & Stephen J. Royle, 2018. "FerriTag is a new genetically-encoded inducible tag for correlative light-electron microscopy," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04993-0
    DOI: 10.1038/s41467-018-04993-0
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    Cited by:

    1. Changsong Yang & Patricia Colosi & Siewert Hugelier & Daniel Zabezhinsky & Melike Lakadamyali & Tatyana Svitkina, 2022. "Actin polymerization promotes invagination of flat clathrin-coated lattices in mammalian cells by pushing at lattice edges," Nature Communications, Nature, vol. 13(1), pages 1-20, December.
    2. Kazuki Obashi & Kem A. Sochacki & Marie-Paule Strub & Justin W. Taraska, 2023. "A conformational switch in clathrin light chain regulates lattice structure and endocytosis at the plasma membrane of mammalian cells," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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