Post-Translational Modifications in Spermatozoa Functions
Summary
Spermatozoa acquire competence for fertilisation through a series of finely tuned biochemical events collectively governed by post-translational modifications (PTMs). These covalent alterations—such as phosphorylation, acetylation, ubiquitination and glycosylation—modulate the stability, activity and interactions of key proteins throughout spermatogenesis, epididymal maturation, capacitation and the acrosome reaction. Glycosylation of surface glycoproteins shapes the sperm glycocalyx, mediating immune evasion in the female tract and enabling precise sperm–egg recognition. Phosphorylation cascades triggered during capacitation regulate flagellar motility and membrane fluidity, while lysine acetylation in mitochondrial and cytoskeletal proteins supports energy metabolism and structural integrity. Ubiquitin-like modifications target defective or excess proteins for degradation, ensuring quality control. Together, these PTMs orchestrate motility, zona-pellucida binding and membrane fusion, with perturbations linked to male infertility. Advances in mass-spectrometry and high-throughput glycoproteomics have begun to map this dynamic landscape, offering novel diagnostic biomarkers and therapeutic targets in assisted reproductive technologies.
Research from Nature Portfolio
Recent studies have employed lectin microarrays to profile the sperm surface glycome in unprecedented detail. This approach revealed altered binding of specific lectins to sperm carrying homozygous mutations in the DEFB126 gene, demonstrating reduced sialylation on the glycocalyx and identifying lectins that serve as potential clinical biomarkers for subfertility arising from this mutation.
Post-Translational Modifications in Spermatozoa Functions publication trend
The graph below shows the total number of articles in post-translational modifications in spermatozoa functions across all publications each year (not limited to Nature Index journals).
Technical terms
Post-translational modification: Chemical alteration of a protein after translation, regulating its function, localisation or interactions.
Glycosylation: Enzymatic attachment of carbohydrate chains to proteins, critical for cell-surface recognition and signalling.
Acetylation: Addition of an acetyl group, often to lysine residues, modulating protein stability and interaction networks.
Phosphorylation: Transfer of a phosphate group to serine, threonine or tyrosine residues, governing signal transduction and enzyme activity.
Capacitation: A maturation process within the female reproductive tract involving biochemical and biophysical changes essential for fertilisation.
References
- Spatial Organization of the Sperm Cell Glycoproteome. Molecular & Cellular Proteomics (2024).
- Precision Glycoproteomics Reveals Distinctive N-Glycosylation in Human Spermatozoa. Molecular & Cellular Proteomics (2022).
- Acetylproteomic Analysis Reveals Functional Implications of Lysine Acetylation in Human Spermatozoa (sperm)* [S]. Molecular & Cellular Proteomics (2015).
- Lectin binding of human sperm associates with DEFB126 mutation and serves as a potential biomarker for subfertility. Scientific Reports (2016).
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