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Expression data from testis of two-month-old WT and Ccnyl1 KO mice

ABSTRACT: Ccnyl1 is a newly identified genes, but the founction of which remained unclear, here we used the Ccnyl1 knockout mice to finding clues for its functional roles We used microarrays to screen the expression differences of genes in testis of WT and Ccnyl1 KO mice

ORGANISM(S): Mus musculus

PROVIDER: GSE67391 | GEO | 2015/03/30

SECONDARY ACCESSION(S): PRJNA279802

REPOSITORIES: GEO

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Expression data from testis of two-month-old WT and Ccnyl1 KO mice

Project description:Ccnyl1 is a newly identified genes, but the founction of which remained unclear, here we used the Ccnyl1 knockout mice to finding clues for its functional roles We used microarrays to screen the expression differences of genes in testis of WT and Ccnyl1 KO mice We used testis tissues from two month old mice, which were of adult age, and two mice per group

2015-03-30 | E-GEOD-67391 | biostudies-arrayexpress

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Project description:Signal peptide peptidase (SPP) and the four homologous SPP-like (SPPL) proteases constitute a family of intramembrane aspartyl proteases with selectivity for type II-oriented transmembrane segments. Here, we have analysed the physiological function of the orphan protease SPPL2c, previously considered to represent a non-expressed pseudogene. We identified proteolytic activity of SPPL2c towards selected tail-anchored proteins. Despite shared ER localization, SPPL2c and SPP exhibit distinct, though partially overlapping substrate spectra and inhibitory profiles and are organised in different high molecular-weight complexes. Unexpectedly, SPPL2c is specifically expressed in murine and human testis where it is primarily localised in spermatids. In mice, SPPL2c-deficiency leads to a loss of elongated spermatids and reduced motility of mature spermatozoa, but preserved fertility. Additionally, matings of male and female SPPL2c-/- mice exhibit reduced litter sizes. Using proteomics we identified the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA2)-regulating protein phospholamban (PLN) as a physiological SPPL2c substrate. Accumulation of PLN correlates with a decrease of intracellular Ca2+ levels in elongated spermatids that likely contributes to the compromised male germ cell differentiation and function of SPPL2c-/- mice.

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