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Updated: Jun 7, 2026
Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
No Time to Fold: Intrinsically Disordered Microproteins in Action
Tianyu Chen1, Kevin Cao1, Thomas F Martinez1,2,3
1Department of Pharmaceutical Sciences, University of California, Irvine, Irvine, California 92617, United States.
Abstract:
Advances in genomics, proteomics, and bioinformatics have uncovered the existence of thousands of translated small open reading frames less than 100-150 codons in length that encode microproteins. In addition to their diminutive size, microproteins are also often predicted to be intrinsically disordered based on their enrichment in disordered-promoting amino acids. Microproteins have since been found to regulate diverse cellular processes, including DNA repair, mRNA decay, mitochondrial metabolism, and ribosome biogenesis, among others. While only a small fraction of microproteins have been functionally characterized, many examples have been found to act as regulators of larger proteins and protein complexes in ways similar to annotated intrinsically disordered proteins (IDPs). In this review, we summarize the functions and mechanisms of several disordered microproteins while exploring the approaches used to study their disordered nature, their regulation by post-translational modifications, and potential strategies to therapeutically target them in disease. These examples underscore how investigations of disordered microproteins deepen our understanding of how biological processes are regulated and emphasize how close collaboration between the microprotein and IDP fields can enhance these efforts.
Insights
Discovered microproteins, small protein regulators, are often intrinsically disordered. Studying these disordered microproteins enhances understanding of cellular processes and disease therapeutics.
Area of Science:
- Molecular Biology
- Genomics
- Proteomics
Background:
- Genomics and proteomics reveal thousands of microproteins encoded by small open reading frames.
- Microproteins are often intrinsically disordered, rich in disorder-promoting amino acids.
- These small proteins regulate key cellular functions like DNA repair and metabolism.
Purpose of the Study:
- To review the functions and mechanisms of disordered microproteins.
- To explore methods for studying their disordered nature.
- To discuss post-translational modifications and therapeutic targeting of microproteins.
Main Methods:
- Bioinformatic analysis of genomic and proteomic data.
- Prediction of intrinsic disorder based on amino acid composition.
- Literature review of characterized microproteins and their functions.
- Analysis of post-translational modifications and therapeutic strategies.
Main Results:
- Microproteins regulate diverse cellular processes, acting similarly to intrinsically disordered proteins (IDPs).
- Many microproteins are intrinsically disordered, influencing protein complex regulation.
- Post-translational modifications impact microprotein function and regulation.
Conclusions:
- Disordered microproteins are crucial regulators of cellular processes.
- Collaborative research between microprotein and IDP fields is vital.
- Targeting disordered microproteins offers potential therapeutic strategies for diseases.
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