Supplementary Fig. S3. from MILIP Binding to tRNAs Promotes Protein Synthesis to Drive Triple-Negative Breast Cancer

Si Min Zheng; Yuchen Feng; Qin Zhu; Ruo Qi Li; Qian Qian Yan; Liu Teng; Yi Meng Yue; Man Man Han; Kaihong Ye; Sheng Nan Zhang; Teng Fei Qi; Cai Xia Tang; Xiao Hong Zhao; Yuan Yuan Zhang; Liang Xu; Ran Xu; Jun Xing; Mark A. Baker; Tao Liu; Rick F. Thorne; Lei Jin; Thomas Preiß; Xu Dong Zhang; Shundong Cang; Jin Nan Gao

doi:10.1158/0008-5472.25735746.v1

Key Points

MILIP does not bind to mutant p53 in triple-negative breast cancer cells, demonstrating that its oncogenic activity bypasses direct mutant p53 binding.
Comparative sequence analysis identifies distinct amino acid variations in eEF1a1 relative to corresponding domains of eEF1a2 in this breast cancer context.
Structural evaluation highlights divergent translation elongation factor motifs, which may influence protein synthesis; preclinical cell model limits apply.

Implication

Molecular analysis reveals absence of MILIP binding to mutant p53 in TNBC, indicating distinct translation elongation factor interactions.

Abstract

MILIP does not bind to mutant p53 in TNBC, whereas there are distinct amino acid sequences in eEF1a1 compared with the corresponding regions in eEF1a2.

Discussion

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Cite This Study

Zheng et al. (2024) studied this question.

synapsesocial.com/papers/68e6be94b6db64358763e77b https://doi.org/10.1158/0008-5472.25735746.v1

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Supplementary Fig. S3. from MILIP Binding to tRNAs Promotes Protein Synthesis to Drive Triple-Negative Breast Cancer

Key Points

Implication

Abstract

Discussion

Cite This Study

Supplementary Fig. S3. from MILIP Binding to tRNAs Promotes Protein Synthesis to Drive Triple-Negative Breast Cancer

Key Points

Implication

Abstract

Discussion

Cite This Study

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