Proteomic profiling of Myc-associated proteins

★

☆

SHARE

Overview

Paper Summary

Conflicts of Interest

Identified Weaknesses

Rating Explanation

Good to know

Topic Hierarchy

File Information

Paper Summary

Paperzilla title

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.

Possible Conflicts of Interest

None identified

Identified Weaknesses

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.

Good to know

This is our free standard analysis. Paperzilla Pro fact-checks every citation, researches author backgrounds and funding sources, and uses advanced AI reasoning for more thorough insights.

Explore Pro →