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LRGUK-1 Is Required for Basal Body and Manchette Function during Spermatogenesis and Male Fertility


Male infertility affects one in six couples in western societies and approximately half of these are the result of male factor disorders. The most common clinical presentation for male infertility is a complex mixture of abnormal sperm output, shape and motility referred to as oligoasthenoteratozoospermia (OAT). In an effort to define an origin of OAT we have analysed a mouse model of leucine-rich repeats and guanylate kinase-domain containing isoform 1 (LRGUK-1) dysfunction. Herein we show that LRGUK dynamically redistributes during the process of haploid germ cell maturation (spermiogenesis) and that LRGUK-1 function is required for multiple aspects of sperm centriole and tail development and sperm head shaping. Further, we have identified HOOK2 as a novel LRGUK-1 binding partner, thus raising the possibility that several aspects of LRGUK-1 function are achieved in partnership with HOOK2.


Vyšlo v časopise: LRGUK-1 Is Required for Basal Body and Manchette Function during Spermatogenesis and Male Fertility. PLoS Genet 11(3): e32767. doi:10.1371/journal.pgen.1005090
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1005090

Souhrn

Male infertility affects one in six couples in western societies and approximately half of these are the result of male factor disorders. The most common clinical presentation for male infertility is a complex mixture of abnormal sperm output, shape and motility referred to as oligoasthenoteratozoospermia (OAT). In an effort to define an origin of OAT we have analysed a mouse model of leucine-rich repeats and guanylate kinase-domain containing isoform 1 (LRGUK-1) dysfunction. Herein we show that LRGUK dynamically redistributes during the process of haploid germ cell maturation (spermiogenesis) and that LRGUK-1 function is required for multiple aspects of sperm centriole and tail development and sperm head shaping. Further, we have identified HOOK2 as a novel LRGUK-1 binding partner, thus raising the possibility that several aspects of LRGUK-1 function are achieved in partnership with HOOK2.


Zdroje

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