Related Experiment Video
Updated: May 15, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Solution structure of the oncogenic MIEN1 protein reveals a thioredoxin-like fold with a redox-active motif
Chun-Hua Hsu1, Tang-Long Shen, Chi-Fon Chang
1Department of Agricultural Chemistry, National Taiwan University, Taipei, Taiwan. andyhsu@ntu.edu.tw
Abstract:
The novel tumor biomarker MIEN1, identified by representational difference analysis, is overexpressed in breast cancer and prostate cancer. MIEN1 is considered an oncogenic protein, because MIEN1 overexpression functionally enhances migration and invasion of tumor cells via modulating the activity of AKT. However, the structure and molecular function of MIEN1 is little understood. Here, we report the solution structure of MIEN1, which adopts a thioredoxin-like fold with a redox-active motif. Comparison of backbone chemical shifts showed that most of the residues for both oxidized and reduced MIEN1 possessed the same backbone conformation, with differences limited to the active motif and regions in proximity. The redox potential of this disulfide bond was measured as -225 mV, which compares well with that of disulfides for other thioredoxin-like proteins. Overall, our results suggest that MIEN1 may have an important regulatory role in phosphorylation of AKT with its redox potential.
More Related Videos
07:16Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
09:58Mapping the Structure-Function Relationships of Disordered Oncogenic Transcription Factors Using Transcriptomic Analysis
Published on: June 27, 2020
Related Concept Videos
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
The Supercomplexes in the Crista Membrane
Transducer Mechanism: Enzyme-Linked Receptors
Major types that are helpful drug targets include:
Mechanisms of Retrovirus-induced Cancers