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Kirfel, G.

Publications and source records attributed to Kirfel, G..

2 recordsLinked to original sources

Cylicins are a structural component of the sperm calyx being indispensable for male fertility in mice and human

Cylicins are testis-specific proteins, which are exclusively expressed during spermiogenesis. In mice and humans, two Cylicins, the gonosomal X-linked Cylicin 1 (Cylc1/CYLC1) and the autosomal Cylicin 2 (Cylc2/CYLC2) genes have been identified. Cylicins are cytoskeletal proteins with an overall positive charge due to lysine-rich repeats. While Cylicins have been localized in the acrosomal region of round spermatids, they resemble a major component of the calyx within the perinuclear theca at the posterior part of mature sperm nuclei. However, the role of Cylicins during spermiogenesis has not yet been investigated. Here, we applied CRISPR/Cas9-mediated gene-editing in zygotes to establish Cylc1- and Cylc2-deficient mouse lines as a model to study the function of these proteins. Cylc1 deficiency resulted in male subfertility, whereas Cylc2-/-, Cylc1-/y Cylc2+/-, and Cylc1-/y Cylc2-/- males were infertile. Phenotypical characterization revealed that loss of Cylicins prevents proper calyx assembly during spermiogenesis. This results in decreased epididymal sperm counts, impaired shedding of excess cytoplasm, and severe structural malformations, ultimately resulting in impaired sperm motility. Furthermore, exome sequencing identified an infertile man with a hemizygous variant in CYLC1 and a heterozygous variant in CYLC2, displaying morphological abnormalities of the sperm including the absence of the acrosome. Thus, our study highlights the relevance and importance of Cylicins for spermiogenic remodeling and male fertility in human and mouse, and provides the basis for further studies on unraveling the complex molecular interactions between perinuclear theca proteins required during spermiogenesis.

developmental biology↗

1-Deoxysphingolipids Tempt Autophagy Resulting in Lysosomal Lipid Substrate Accumulation: Tracing the Impact of 1-Deoxysphingolipids on Ultra-Structural Level using a Novel Click-Chemistry Detection

Sphingolipids (SLs) are pivotal components of biological membranes essentially contributing to their physiological functions. 1-deoxysphingolipids (deoxySLs), an atypical cytotoxic acting sub-class of SLs, is relevant for cellular energy homeostasis and is known to be connected to neurodegenerative disorders including diabetic neuropathy and hereditary sensory neuropathy type 1 (HSAN1). High levels of deoxySLs affect lipid membrane integrity in artificial liposomes. Accordingly, recent reports questioned the impact of deoxySLs on physiological lipid membrane and organelle functions leading to impaired cellular energy homeostasis. However, DeoxySL-related structural effects on cell membranes resulting in organelle dysfunction are still obscure. To illuminate disease-relevant sub-cellular targets of deoxySLs, we traced alkyne-containing 1-deoxysphinganine (alkyne-DOXSA) and resulting metabolites on ultra-structural level using a new labeling approach for electron microscopy (EM) termed "Golden-Click-Method" (GCM). To complement high-resolution analysis with membrane dynamics, selected intracellular compartments were traced using fluorescent live dyes. Our results conclusively linked accumulating cytotoxic deoxySLs with mitochondria and endoplasmic reticulum (ER) damage triggering Autophagy of mitochondria and membrane cisterna of the ER. The induced autophagic flux ultimately leads to accumulating deoxySL containing intra-lysosomal lipid crystals. Lysosomal lipid substrate accumulation impaired physiological lysosome functions and caused cellular starvation. Lysosomal exocytosis appeared as a mechanism for cellular clearance of cytotoxic deoxySLs. In sum, our data define new ultra-structural targets of deoxySLs and link membrane damage to autophagy and abnormal lysosomal lipid accumulation. These insights may support new conclusions about diabetes type 2 and HSNA1 related tissue damage.

cell biology↗