ArticleReproduction (Cambridge, England)2025
Na+,K+-ATPase α isoforms in sperm show a highly structured and distinct pattern of distribution.
Article in Reproduction (Cambridge, England), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- The systems that transport ions and their impact on sperm function and male fertility.Function (Oxford, England) · 2026Review
- The Sperm Acrosomal Reaction Depends on the Function of Both Na,K-ATPase α1 and α4 Isoforms.International journal of molecular sciences · 2026Article
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Authors and funding
4 authors.
Funding
Abstract
In brief: This manuscript shows that the Na+ and K+ transporter Na+,K+-ATPase α4, specific to sperm, is expressed on the surface of the sperm head and flagellum in a very structured manner. This is also true for Na+,K+-ATPase α1, the other Na+,K+-ATPase isoform present in sperm and also in all cells. However, Na+,K+-ATPase α4 distribution changes when the cells are capacitated, an event necessary for fertilization. This dynamic remodeling, along with the distinct functional properties of Na+,K+-ATPase α4 and α1, provides evidence for the refined level of specialization that sperm have developed to achieve the amazing goal of fertilizing the oocyte. Abstract: Na+,K+-ATPase α4 is a unique Na+ and K+ transporter of the plasma membrane of spermatozoa, which is essential for male fertility. While previous studies have found Na+,K+-ATPase α4 to be mainly expressed in the sperm flagellum, less is known about its localization in the sperm head. Moreover, the spatial arrangement of Na+,K+-ATPase α4 at the subcellular level and its relationship to the functional state of the cells are unclear. We studied this using stimulated emission depletion (STED) super-resolution microscopy. We show that, under non-capacitated conditions, Na+,K+-ATPase α4 is distributed in a trilinear pattern along the midpiece and as a scattered single line along the principal piece of the sperm flagellum. Under capacitated conditions, Na+,K+-ATPase α4 pattern undergoes remodeling and its distribution shifts to a single line along the flagellum. On the other hand, Na+,K+-ATPase α1, the somatic isoform of Na+,K+-ATPase also present in sperm, exhibits a similar trilaminar localization at the flagellar midpiece but a bilinear pattern in the principal piece. This distribution, unlike that of Na+,K+-ATPase α4, does not change during sperm capacitation. We also found Na+,K+-ATPase α1 and α4 in the sperm head, where they present a complex distribution under both non-capacitated and capacitated conditions. These differences in the localization pattern and spatial dynamics of Na+,K+-ATPase isoform expression, along with their different functional properties, highlight the distinct roles that both isoforms play to support sperm function.
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