Characterization of mouse sperm TMEM190, a small transmembrane protein with the trefoil domain: evidence for co-localization with IZUMO1 and complex formation with other sperm proteins

Nishimura, Hitoshi; Gupta, Surabhi; Myles, Diana G.; Primàkoff, Paul

doi:10.1530/rep-10-0391

Cited by 23 publications

(12 citation statements)

References 49 publications

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“…For example, several proteins exhibit altered localization after the process of capacitation in mice (Miranda et al, 2009). During capacitation, a transmembrane protein TMEM 190 partly relocates and forms protein complexes on the region of the sperm that participates in sperm-oocyte interaction in mouse (Nishimura et al, 2011). Similarly, dynamic localization of Ran-binding protein 17 is observed during spermatogenesis and spermiogenesis in mice (Bao et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

The sperm surface localization of the TRP-3/SPE-41 Ca2+-permeable channel depends on SPE-38 function in Caenorhabditis elegans

Singaravelu¹,

Chatterjee²,

Rahimi³

et al. 2012

Developmental Biology

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Despite undergoing normal development and acquiring normal morphology and motility, mutations in spe-38 or trp-3/spe-41 cause identical phenotypes in Caenorhabditis elegans – mutant sperm fail to fertilize oocytes despite direct contact. SPE-38 is a novel, four-pass transmembrane protein and TRP-3/SPE-41 is a Ca2+-permeable channel. Localization of both of these proteins is confined to the membranous organelles (MOs) in undifferentiated spermatids. In mature spermatozoa, SPE-38 is localized to the pseudopod and TRP-3/SPE-41 is localized to the whole plasma membrane. Here we show that the dynamic redistribution of TRP-3/SPE-41 from MOs to the plasma membrane is dependent on SPE-38. In spe-38 mutant spermatozoa, TRP-3/SPE-41 is trapped within the MOs and fails to reach the cell surface despite MO fusion with the plasma membrane. Split-ubiquitin yeast-two-hybrid analyses revealed that the cell surface localization of TRP-3/SPE-41 is likely regulated by SPE-38 through a direct protein-protein interaction mechanism. We have identified sequences that influence the physical interaction between SPE-38 and TRP-3/SPE-41, and show that these sequences in SPE-38 are required for fertility in transgenic animals. Despite the mislocalization of TRP-3/SPE-41 in spe-38 mutant spermatozoa, ionomycin or thapsigargin induced influx of Ca2+ remains unperturbed. This work reveals a new paradigm for the regulated surface localization of a Ca2+-permeable channel.

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Section: Discussionmentioning

confidence: 99%

The sperm surface localization of the TRP-3/SPE-41 Ca2+-permeable channel depends on SPE-38 function in Caenorhabditis elegans

Singaravelu¹,

Chatterjee²,

Rahimi³

et al. 2012

Developmental Biology

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“…mature) spermatozoa. Peanut agglutinin (PNA), which binds to the glycosylated proteins of the acrosomal region of post-meiotic germ cells including mature sperm2930, was co-stained to determine the spermatogenic stages (Fig. 2a).…”

Section: Resultsmentioning

confidence: 99%

Identification of a variant-specific phosphorylation of TH2A during spermiogenesis

Hada

Masuda

Yamaguchi

et al. 2017

Sci Rep

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Tissue-specific histone variant incorporation into chromatin plays dynamic and important roles in tissue development. Testis is one such tissue, and a number of testis-specific histone variants are expressed that have unique roles. While it is expected that such variants acquire post-transcriptional modifications to be functional, identification of variant-specific histone modifications is challenging because of the high similarity of amino acid sequences between canonical and variant versions. Here we identified a novel phosphorylation on TH2A, a germ cell-specific histone H2A variant. TH2A-Thr127 is unique to the variant and phosphorylated concomitant with chromatin condensation including spermiogenesis and early embryonic mitosis. In sperm chromatin, phosphorylated TH2A-Thr127 (=pTH2A) is co-localized with H3.3 at transcriptional starting sites of the genome, and subsequently becomes absent from the paternal genome upon fertilization. Notably, pTH2A is recurrent and accumulated in the pericentromeric heterochromatin of both paternal and maternal chromosomes in the first mitosis of embryos, suggesting its unique regulation during spermiogenesis and early embryogenesis.

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“…Reverse transcription polymerase chain reaction Testicular germ cells were purified by a 52% (v/v) gradient of Percoll (GE Healthcare Life Sciences, Piscataway, NJ, USA) according to the method previously described (Nishimura et al 2011). Motile epididymal spermatozoa were isolated by a swimup procedure (Fang et al 2014).…”

Section: Preparation Of Spermatozoamentioning

confidence: 99%

Different locations of RANTES and its receptors on mouse epididymal spermatozoa

Wei

Feng

Sun

et al. 2016

Reprod. Fertil. Dev.

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Our previous study showed that the chemokine regulated upon activation normal T-cell expressed and secreted (RANTES) originating from the mouse epididymis bound to the midpiece of luminal spermatozoa. The present study was undertaken to investigate the association between RANTES and epididymal spermatozoa and to determine whether the association is mediated by the RANTES receptors CCR1, CCR3 or CCR5. The use of reverse transcription polymerase chain reaction (RT-PCR), immunohistochemical staining and immunofluorescent staining demonstrated that RANTES secreted by apical and narrow cells of mouse epididymal ducts was associated with luminal spermatozoa. Flow cytometric analysis and immunofluorescent labelling revealed that the association between RANTES and spermatozoa of different regions weakened gradually as the spermatozoa moved along the epididymis. Moreover, CCR1, CCR3 and CCR5 were expressed in epididymal spermatozoa and located on the head of epididymal spermatozoa, while RANTES was generally located at the midpiece. In conclusion, RANTES and its receptors were not in the same sperm location, suggesting that RANTES binding to mouse epididymal spermatozoa is independent of CCR1, CCR3 and CCR5.

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Characterization of mouse sperm TMEM190, a small transmembrane protein with the trefoil domain: evidence for co-localization with IZUMO1 and complex formation with other sperm proteins

Cited by 23 publications

References 49 publications

The sperm surface localization of the TRP-3/SPE-41 Ca2+-permeable channel depends on SPE-38 function in Caenorhabditis elegans

The sperm surface localization of the TRP-3/SPE-41 Ca2+-permeable channel depends on SPE-38 function in Caenorhabditis elegans

Identification of a variant-specific phosphorylation of TH2A during spermiogenesis

Different locations of RANTES and its receptors on mouse epididymal spermatozoa

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