Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility

Tokuhiro, Keizo; Ikawa, Masahito; Benham, Adam M.; Okabe, Masaru

doi:10.1073/pnas.1117963109

Cited by 133 publications

(179 citation statements)

References 56 publications

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“…1A). Cumulus cells support fertilization, and in vitro fertilization can be achieved more efficiently with them than without them (Jin et al, 2011;Tokuhiro et al, 2012). The molecular basis of this observation remains obscure; however, a few studies have addressed the function of cumulus cells (Oren-Benaroya et al, 2008;Shimada et al, 2008).…”

Section: The Nature Of Eggsmentioning

confidence: 99%

“…Mice deficient for the testis-specific molecular chaperone PDILT produce spermatozoa that, based on in vitro experiments, exhibit impaired zona-binding ability (Tokuhiro et al, 2012). After crossing with a transgenic fluorescently tagged sperm line (Hasuwa et al, 2010), the failure of sperm migration into the oviduct was indicated by live imaging.…”

Section: The Zona-binding Ability Of Spermatozoamentioning

confidence: 99%

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The cell biology of mammalian fertilization

2013

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Fertilization is the process by which eggs and spermatozoa interact, achieve mutual recognition, and fuse to create a zygote, which then develops to form a new individual, thus allowing for the continuity of a species. Despite numerous studies on mammalian fertilization, the molecular mechanisms underpinning the fertilization event remain largely unknown. However, as I summarize here, recent work using both gene-manipulated animals and in vitro studies has begun to elucidate essential sperm and egg molecules and to establish predictive models of successful fertilization.

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Section: The Nature Of Eggsmentioning

confidence: 99%

Section: The Zona-binding Ability Of Spermatozoamentioning

confidence: 99%

The cell biology of mammalian fertilization

2013

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“…as listed in Table 3, Pdilt-disrupted mice produce spermatozoa with impaired zona binding ability [53]. We crossed this mouse line with another transgenic mouse line with fluorescent proteintagged sperm [20] for visibility in the female reproductive tract.…”

Section: The "Zona-binding Ability" Of Spermatozoa Must Be Reconsideredmentioning

confidence: 99%

Mechanism of Fertilization: A Modern View

Okabe

2014

Exp. Anim.

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Despite numerous studies on mammalian fertilization, the mechanisms of fertilizationincluding the timing of acrosome reaction-remain largely unknown; more accurately described, the classical theory built upon years of layered experimental data is being challenged by recent conflicting evidence provided by gene-manipulated animals. Although in vitro fertilization remains our central research tool, the classical theory's decline reminds us of the importance of in vivo observations. Here, I describe the essential roles of gene-manipulated animals in elucidating the mechanism of fertilization and the pitfalls of in vitro fertilization studies trapping many researchers.

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“…The DNA fragments were inserted to the pNT1.1 vector. 47 The resulting donor plasmid, termed pNT1.1-SUN1, harbors the neomycin resistant gene cassette in between the genomic DNA fragments. HeLa cells co-transfected with px330-SUN1 and pNT1.1-SUN1 were selected for G418-resistance.…”

Section: Establishment Of a Sun1 Knockout Cell Linementioning

confidence: 99%

SUN1 splice variants, SUN1_888, SUN1_785, and predominant SUN1_916, variably function in directional cell migration

Nishioka

Imaizumi

Imada

et al. 2016

Nucleus

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The LINC complex is a multifunctional protein complex that is involved in various processes at the nuclear envelope, such as nuclear migration, mechanotransduction and chromatin tethering in the meiotic phase. However, it remains unknown how these functions are regulated in different cell contexts. An inner nuclear membrane component of the LINC complex, SUN1, is ubiquitously expressed. The human SUN1 gene produces over 10 variants by alternative splicing. Although functions of SUN1 are relatively well characterized, functional differences among SUN1 splice variants are poorly characterized. LINC complex components are associated with a wide range of human diseases; therefore, it is important to understand the functional diversity among SUN1 splice variants. Here, we identified a novel human SUN1 splice variant, SUN1_888. overexpression of the SUN1 splice variants, SUN1_888 or SUN1_785, but not the predominant isoform, SUN1_916, activated directional cell migration. Knockdown of SUN1_888 suppressed cell migration; in contrast depletion of SUN1_916 activated cell migration. In addition, all of investigated SUN1 splicing variants rescued cell migration in SUN1 knock out cell. These results indicate that redundant and non-redundant functions of SUN1 splice variant in directional cell migration and suggest that variable LINC complexes with distinct task may exit. Furthermore, in contrast to previous studies, we showed association between SUN1 and B-type lamins. Interestingly, B-type lamin preferentially interacts with SUN1 but not SUN2. These results suggest that tissue-specific SUN1 variants variably interact with nucleoplasmic partners and allow variable assembly of LINC complexes that can be assigned to distinct tasks.

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Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility

Cited by 133 publications

References 56 publications

The cell biology of mammalian fertilization

The cell biology of mammalian fertilization

Mechanism of Fertilization: A Modern View

SUN1 splice variants, SUN1_888, SUN1_785, and predominant SUN1_916, variably function in directional cell migration

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