Article Synopsis
- Current intracellular protein analysis often requires disrupting organelles or altering the cell's environment, but proteins work best in their natural conditions where they interact with various molecules.
- Researchers introduced a new technique using PLGA nanoparticles to deliver cross-linkers specifically to mitochondria in living cells, allowing for analysis of protein interactions.
- This method identified 74 unique protein-protein interactions, particularly among mitochondrial respiratory chain proteins, matching existing structural data and offering a valuable tool for studying proteins in their native environments.
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Article Abstract
Current methods for intracellular protein analysis mostly require the separation of specific organelles or changes to the intracellular environment. However, the functions of proteins are determined by their native microenvironment as they usually form complexes with ions, nucleic acids, and other proteins. Here, we show a method for in situ cross-linking and analysis of mitochondrial proteins in living cells. By using the poly(lactic-co-glycolic acid) (PLGA) nanoparticles functionalized with dimethyldioctadecylammonium bromide (DDAB) to deliver protein cross-linkers into mitochondria, we subsequently analyze the cross-linked proteins using mass spectrometry. With this method, we identify a total of 74 pairs of protein-protein interactions that do not exist in the STRING database. Interestingly, our data on mitochondrial respiratory chain proteins ( ~ 94%) are also consistent with the experimental or predicted structural analysis of these proteins. Thus, we provide a promising technology platform for in situ defining protein analysis in cellular organelles under their native microenvironment.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10313818 | PMC |
| http://dx.doi.org/10.1038/s41467-023-39485-3 | DOI Listing |