Mammalian Sperm Head Formation Involves Different Polarization of Two Novel LINC Complexes
Mammalian Sperm Head Formation Involves Different Polarization of Two Novel LINC Complexes
LINC complexes are nuclear envelope bridging protein structures formed by interaction of SUN and KASH proteins. They physically connect the nucleus with the peripheral cytoskeleton and are critically involved in a variety of dynamic processes, such as nuclear anchorage, movement and positioning and meiotic chromosome dynamics. Moreover, they are shown to be essential for maintaining nuclear shape.Based on detailed expression analysis and biochemical approaches, we show here that during mouse sperm development, a terminal cell differentiation process characterized by profound morphogenic restructuring, two novel distinctive LINC complexes are established. They consist either of spermiogenesis-specific Sun3 and Nesprin1 or Sun1eta, a novel non-nuclear Sun1 isoform, and Nesprin3. We could find that these two LINC complexes specifically polarize to opposite spermatid poles likely linking to sperm-specific cytoskeletal structures. Although, as shown in co-transfection/immunoprecipitation experiments, SUN proteins appear to arbitrarily interact with various KASH partners, our study demonstrates that they actually are able to confine their binding to form distinct LINC complexes.Formation of the mammalian sperm head involves assembly and different polarization of two novel spermiogenesis-specific LINC complexes. Together, our findings suggest that theses LINC complexes connect the differentiating spermatid nucleus to surrounding cytoskeletal structures to enable its well-directed shaping and elongation, which in turn is a critical parameter for male fertility.
- University of Würzburg Germany
- University Hospital of Zurich Switzerland
Male, Nuclear Envelope, Science, Molecular Sequence Data, Nerve Tissue Proteins, Mice, Sperma, Animals, Humans, Protein Isoforms, Amino Acid Sequence, Spermatogenesis, Cytoskeleton, Q, R, Membrane Proteins, Nuclear Proteins, Spermatids, Cytoskeletal Proteins, Meiosis, Protein Transport, Gene Expression Regulation, Organ Specificity, Medicine, Sperm Head, ddc:570, Research Article
Male, Nuclear Envelope, Science, Molecular Sequence Data, Nerve Tissue Proteins, Mice, Sperma, Animals, Humans, Protein Isoforms, Amino Acid Sequence, Spermatogenesis, Cytoskeleton, Q, R, Membrane Proteins, Nuclear Proteins, Spermatids, Cytoskeletal Proteins, Meiosis, Protein Transport, Gene Expression Regulation, Organ Specificity, Medicine, Sperm Head, ddc:570, Research Article
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