Key result
Spatial proteomic technologies can measure and define protein interactomes within living cells, as demonstrated by recent work defining the novel cardiac-interactome of caveolin 3.
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Design
Editorial
This editorial highlights the importance of spatial proteomic technologies in defining protein interactomes, specifically discussing recent work on the cardiac-interactome of caveolin 3.
Protein isoforms have highly similar amino acid sequences which can lead to similar biological roles. However in some cases, such as cell specific or enriched isoforms, they can assume distinct functions. This editorial discusses the work by Peper et. al., that defined the novel cardiac-interactome of caveolin 3 and the downstream functional consequences. Proteins live in a closely controlled communities where their complexes are highly regulated as are their location within a cell. There is a suite of ever-growing proteomic technologies capable of quantifying the chemical and biological diversity of the proteome including protein interactomes. This editorial discusses cutting-edge spatial proteomic technologies able to measure and define protein interactomes within living cells and precisely explore the immense landscape of the proteome.
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Jennifer E. Van Eyk (2021) reported an editorial. Spatial proteomic technologies can measure and define protein interactomes within living cells, as demonstrated by recent work defining the novel cardiac-interactome of caveolin 3.
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