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Paper Summary
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Uncovering Myc's Social Network: Hundreds of New Friends for the Cancer-Linked Protein, Studied in Immortalized Cells
This paper utilized advanced proteomics to identify 418 proteins interacting with c-Myc, a pivotal protein linked to cancer, in immortalized human and rat fibroblast cells, revealing 389 previously unknown interactors. The findings underscore c-Myc's diverse involvement in cellular processes, including transcription and cytoskeletal organization, by forming various large protein complexes.
Explain Like I'm Five
Scientists found many new partner proteins for c-Myc, a protein often linked to cancer, by carefully studying special lab-grown cells. This helps us understand all the different jobs c-Myc performs inside our cells.
Possible Conflicts of Interest
None identified
Identified Limitations
Immortalized and Transformed Cell Lines
The study primarily used telomerase-immortalized human fibroblasts and Rat-1 fibroblast cells. While valuable for mechanistic studies, these cell lines are not primary human cancer cells or normal human tissues, which limits the direct applicability of findings to complex human in vivo physiological or pathological contexts.
Challenging Experimental Setup
The authors reported significant inefficiencies, material losses, and the necessity of performing the entire purification in a single 36-hour run due to the fragility of protein interactions with freezing. This indicates the experimental conditions might not fully preserve all native in vivo interactions or maintain accurate stoichiometry.
Low Confidence for Some Protein Identifications
A substantial portion of the total identified proteins (1,469 out of 5,603) were based on only a single unique peptide. While the focused 'enriched' interactors typically had more, single-peptide identifications generally carry lower confidence and could lead to false positives in the broader dataset.
Limited Overlap with Previous Studies
The newly generated dataset showed low overlap (8-12%) with previously annotated c-Myc interactors or those identified in other large-scale studies. Although methodological differences are cited, this suggests the interactome might be highly context-dependent, and a universally defined c-Myc interactome remains elusive, making cross-validation challenging.
Rating Explanation
This paper represents strong research, employing robust proteomic techniques to significantly expand the known interactome of the crucial proto-oncogene c-Myc. The use of near-physiological expression levels in human and rat fibroblast cell lines, while not primary human disease models, provides valuable insights into c-Myc's cellular functions. The authors also acknowledge the inherent experimental challenges and limitations, contributing to the study's transparency.
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File Information
Original Title:
Proteomic profiling of Myc-associated proteins
Uploaded:
October 02, 2025 at 04:18 PM
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Public