Quantifying protein dynamics and stability in a living organism

Ruopei Feng, Martin Gruebele, Caitlin M. Davis

Research output: Contribution to journalArticle

Abstract

As an integral part of modern cell biology, fluorescence microscopy enables quantification of the stability and dynamics of fluorescence-labeled biomolecules inside cultured cells. However, obtaining time-resolved data from individual cells within a live vertebrate organism remains challenging. Here we demonstrate a customized pipeline that integrates meganuclease-mediated mosaic transformation with fluorescence-detected temperature-jump microscopy to probe dynamics and stability of endogenously expressed proteins in different tissues of living multicellular organisms.

Original languageEnglish (US)
Article number1179
JournalNature communications
Volume10
Issue number1
DOIs
StatePublished - Dec 1 2019

Fingerprint

Protein Stability
organisms
Fluorescence
Cytology
proteins
fluorescence
Fluorescence microscopy
Biomolecules
Fluorescence Microscopy
microscopy
Cell Biology
Vertebrates
Microscopy
Cultured Cells
vertebrates
Microscopic examination
Proteins
Pipelines
Cells
Tissue

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

Cite this

Quantifying protein dynamics and stability in a living organism. / Feng, Ruopei; Gruebele, Martin; Davis, Caitlin M.

In: Nature communications, Vol. 10, No. 1, 1179, 01.12.2019.

Research output: Contribution to journalArticle

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