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- W4317366283 abstract "Abstract Alternative translation initiation and alternative splicing may give rise to N-terminal proteoforms, proteins that differ at their N-terminus compared to their canonical counterparts. Such proteoforms can have altered localizations, stabilities and functions. While proteoforms generated from splice variants can be engaged in different protein complexes, it remained to be studied to what extent this applies to N-terminal proteoforms. To address this, we mapped the interactomes of several pairs of N-terminal proteoforms and their canonical counterparts. First, we generated a catalogue of N-terminal proteoforms found in the HEK293T cellular cytosol from which 22 pairs were selected for interactome profiling. Additionally, we provide evidence for the expression of several N-terminal proteoforms, identified in our catalogue, across different human tissues as well as tissue-specific expression, highlighting their biological relevance. Protein-protein interaction profiling revealed that the overlap of the interactomes for both proteoforms is generally high, showing their functional relation. We also showed that N-terminal proteoforms can be engaged in new interactions and/or lose several interactions compared to their canonical counterpart, thus further expanding the functional diversity of proteomes." @default.
- W4317366283 created "2023-01-19" @default.
- W4317366283 creator A5005605525 @default.
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- W4317366283 date "2023-01-18" @default.
- W4317366283 modified "2023-10-02" @default.
- W4317366283 title "N-terminal proteoforms may engage in different protein complexes" @default.
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- W4317366283 doi "https://doi.org/10.1101/2023.01.17.524352" @default.
- W4317366283 hasPublicationYear "2023" @default.
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