RIM-BP3 is a manchette-associated protein essential for spermiogenesis

Zhou, Jing; Du, Yongsheng; Qin, Weihua; Hu, Yeguang; Huang, Yan-Nv; Liu, Bao; Han, Daishu; Mansouri, Ahmed; Xu, Guoliang

doi:10.1242/dev.030858

Cited by 73 publications

(61 citation statements)

References 52 publications

(63 reference statements)

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“…Depletion of HOOK1, a protein-linking microtubule to endosomal trafficking, also results in elongated cylindrical shape nucleus in spermatozoa (Mendoza-Lujambio et al 2002). The interaction between HOOK1 and RIMBP3 has been established, which may represent a link between the manchette microtubules and other cellular organelles, e.g., the nuclear envelope (Zhou et al 2009). Hook1 and Rimbp3 KO mouse models also present an ectopic manchette and detached sperm tails.…”

Section: Manchette Removalmentioning

confidence: 99%

Formation and function of the manchette and flagellum during spermatogenesis

Lehti¹,

Sironen²

2016

Reproduction

188

179

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The last phase of spermatogenesis involves spermatid elongation (spermiogenesis), where the nucleus is remodeled by chromatin condensation, the excess cytoplasm is removed and the acrosome and sperm tail are formed. Protein transport during spermatid elongation is required for correct formation of the sperm tail and acrosome and shaping of the head. Two microtubular-based protein delivery platforms transport proteins to the developing head and tail: the manchette and the sperm tail axoneme. The manchette is a transient skirt-like structure surrounding the elongating spermatid head and is only present during spermatid elongation. In this review, we consider current understanding of the assembly, disassembly and function of the manchette and the roles of these processes in spermatid head shaping and sperm tail formation. Recent studies have shown that at least some of the structural proteins of the sperm tail are transported through the intra-manchette transport to the basal body at the base of the developing sperm tail and through the intraflagellar transport to the construction site in the flagellum. This review focuses on the microtubule-based mechanisms involved and the consequences of their disruption in spermatid elongation.Reproduction (2016) 151 R43-R54

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Section: Manchette Removalmentioning

confidence: 99%

Formation and function of the manchette and flagellum during spermatogenesis

Lehti¹,

Sironen²

2016

Reproduction

188

179

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“…30,36 Manchette dysfunction is also seen in a variety of genetically modified mouse models, reviewed in. 3,27,30 Ectopic manchettes are commonly observed (e.g., 25,30,31,37 ) and the position and direction of the microtubules then determine the type of deviations on nuclear surface. A spermatid nuclear phenotype that is observed in a variety of mouse models is an enlarged anterior portion yet a long tapered posterior portion (e.g., 29,31,[38][39][40] ) (see Fig.…”

Section: Abnormal Sperm Head Shapementioning

confidence: 99%

Mechanisms of spermiogenesis and spermiation and how they are disturbed

2014

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Haploid round spermatids undergo a remarkable transformation during spermiogenesis. The nucleus polarizes to one side of the cell as the nucleus condenses and elongates, and the microtubule-based manchette sculpts the nucleus into its species-specific head shape. The assembly of the central component of the sperm flagellum, known as the axoneme, begins early in spermiogenesis, and is followed by the assembly of secondary structures needed for normal flagella. The final remodelling of the mature elongated spermatid occurs during spermiation, when the spermatids line up along the luminal edge, shed their residual cytoplasm and are ultimately released into the lumen. Defects in spermiogenesis and spermiation are manifested as low sperm number, abnormal sperm morphology and poor motility and are commonly observed during reproductive toxicant administration, as well as in genetically modified mouse models of male infertility. This chapter summarizes the major physiological processes and the most commonly observed defects in spermiogenesis and spermiation, to aid in the diagnosis of the potential mechanisms that could be perturbed by experimental manipulation such as reproductive toxicant administration. Signature LesionThere are a number of signature lesions that could indicate a disturbance in spermiogenesis or spermiation. These would include misshapen heads and/or tails of elongating/elongated spermatids. Multinucleated round spermatids may reflect disturbances in spermiogenesis, but could also reflect altered Sertoli cell function. Disruption of spermiation could present itself as spermatid retention at the lumen of post stage VIII tubules, failure of elongated spermatids to ascend to the lumen of stage VII/ VIII tubules, or phagocytosis of mature spermatids at the base of tubules in stages VII through to approximately XII (in mice) or XIV (in rats). The changes might occur in isolation or in combination with one another.

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“…The manchette anchors on a perinuclear ring of actin associated with the marginal ring of the acroplaxome (Kierszenbaum et al, 2003). This microtubular structure is necessary for cargo traffic along the manchette and thus spermiogenesis (Zhou et al, 2009). In Dpy19l2 -/-animals, condensed spermatids with round-nucleus, long microtubular structures corresponding to the manchette, were observed.…”

Section: Mislocalization Of the Manchette And Of Glycoproteins At Thementioning

confidence: 99%

Absence of Dpy19l2, a new inner nuclear membrane protein, causes globozoospermia in mice by preventing the anchoring of the acrosome to the nucleus

et al. 2012

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SUMMARYSperm-head elongation and acrosome formation, which take place during the last stages of spermatogenesis, are essential to produce competent spermatozoa that are able to cross the oocyte zona pellucida and to achieve fertilization. During acrosome biogenesis, acrosome attachment and spreading over the nucleus are still poorly understood and to date no proteins have been described to link the acrosome to the nucleus. We recently demonstrated that a deletion of DPY19L2, a gene coding for an uncharacterized protein, was responsible for a majority of cases of type I globozoospermia, a rare cause of male infertility that is characterized by the exclusive production of round-headed acrosomeless spermatozoa. Here, using Dpy19l2 knockout mice, we describe the cellular function of the Dpy19l2 protein. We demonstrate that the protein is expressed predominantly in spermatids with a very specific localization restricted to the inner nuclear membrane facing the acrosomal vesicle. We show that the absence of Dpy19l2 leads to the destabilization of both the nuclear dense lamina (NDL) and the junction between the acroplaxome and the nuclear envelope. Consequently, the acrosome and the manchette fail to be linked to the nucleus leading to the disruption of vesicular trafficking, failure of sperm nuclear shaping and eventually to the elimination of the unbound acrosomal vesicle. Finally, we show for the first time that Dpy19l3 proteins are also located in the inner nuclear envelope, therefore implying that the Dpy19 proteins constitute a new family of structural transmembrane proteins of the nuclear envelope.KEY WORDS: Dpy19l2, Acrosome biogenesis, Globozoospermia, Nuclear envelope, Nuclear lamina, Spermiogenesis, MouseAbsence of Dpy19l2, a new inner nuclear membrane protein, causes globozoospermia in mice by preventing the anchoring of the acrosome to the nucleus

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RIM-BP3 is a manchette-associated protein essential for spermiogenesis

Cited by 73 publications

References 52 publications

Formation and function of the manchette and flagellum during spermatogenesis

Formation and function of the manchette and flagellum during spermatogenesis

Mechanisms of spermiogenesis and spermiation and how they are disturbed

Absence of Dpy19l2, a new inner nuclear membrane protein, causes globozoospermia in mice by preventing the anchoring of the acrosome to the nucleus

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