<i>Oosp1</i> encodes a novel mouse oocyte‐secreted protein

Yan, Changning; Pendola, Frank L.; Jacob, Renu; Lau, Anthony L.; Eppig, John J.; Matzuk, Martin M.

doi:10.1002/gene.10010

Cited by 35 publications

(32 citation statements)

References 21 publications

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“…Other possibilities remain. For example, besides antioxidant genes, several oocyte-specific genes such as Oosp1 and Omt2b (West et al, 1996;Yan et al, 2001) were also downregulated in Kat8…”

Section: Discussionmentioning

confidence: 99%

Histone acetyltransferase KAT8 is essential for mouse oocyte development by regulating ROS levels

Yin

Jiang

et al. 2017

Development

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Proper oocyte development is crucial for female fertility and requires timely and accurate control of gene expression. K (lysine) acetyltransferase 8 (KAT8), an important component of the X chromosome dosage compensation system in Drosophila, regulates gene activity by acetylating histone H4 preferentially at lysine 16. To explore the function of KAT8 during mouse oocyte development, we crossed Kat8 flox/flox mice with Gdf9-Cre mice to specifically delete Kat8 in oocytes. Oocyte Kat8 deletion resulted in female infertility, with follicle development failure in the secondary and preantral follicle stages. RNA-seq analysis revealed that Kat8 deficiency in oocytes results in significant downregulation of antioxidant genes, with a consequent increase in reactive oxygen species. Intraperitoneal injection of the antioxidant N-acetylcysteine rescued defective follicle and oocyte development resulting from Kat8 deficiency. Chromatin immunoprecipitation assays indicated that KAT8 regulates antioxidant gene expression by direct binding to promoter regions. Taken together, our findings demonstrate that KAT8 is essential for female fertility by regulating antioxidant gene expression and identify KAT8 as the first histone acetyltransferase with an essential function in oogenesis.

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Section: Discussionmentioning

confidence: 99%

Histone acetyltransferase KAT8 is essential for mouse oocyte development by regulating ROS levels

Yin

Jiang

et al. 2017

Development

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“…Failure to produce BMP-15 produces a similar early follicular arrest in sheep ovaries (7). The function of OOSP1 is not yet known, although the expression pattern is essentially the same as Gdf9 and Bmp15 in mouse oocytes (26).…”

Section: Discussionmentioning

confidence: 99%

The mammalian oocyte orchestrates the rate of ovarian follicular development

Eppig

Wigglesworth²,

Pendola³

2002

Proc. Natl. Acad. Sci. U.S.A.

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431

267

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The development of both the mammalian oocyte and the somatic cell compartments of the ovarian follicle is highly coordinated; this coordination ensures that the ovulated oocyte is ready to undergo fertilization and subsequent embryogenesis. Disruption of this synchrony results in oocyte developmental failure. Communication between the oocyte and companion somatic cells is essential for successful development of both follicular compartments. However, it was not previously known whether one cell type, either the somatic or the germ cell compartment, determines the overall rate of follicular development. To test the hypothesis that the oocyte orchestrates the rate of follicle development, mid-sized oocytes isolated from secondary follicles were transferred back to primordial follicles, the earliest stage of follicular development. This transfer doubled the rate of follicular development and the differentiation of follicular somatic cells. Oocyte development in these accelerated follicles appeared normal; recovered oocytes were competent to undergo fertilization and embryonic development. These results demonstrate that oocytes orchestrate and coordinate the development of mammalian ovarian follicles and that the rate of follicular development is based on a developmental program intrinsic to the oocyte.C omplex cell-to-cell interactions coordinate the development of ovarian follicles. The pathways of cellular communication include endocrine, autocrine, and paracrine regulators, and gap junctions. Coordination of the development of oocyte and somatic follicular compartments ensures that the ovulated oocyte is ready to undergo fertilization and subsequent embryogenesis. Disruption of this synchrony by inappropriately timed administration of exogenous gonadotropins can produce oocyte developmental failure (1). Communication between the oocyte and companion somatic cells is essential for successful development of both follicular compartments (2). The oocyte depends on its association with companion somatic granulosa cells to support its growth and development and to regulate the progression of meiosis. Likewise, oocytes promote granulosa cell proliferation, differentiation, and function. The communication between granulosa cells and oocytes is, therefore, bidirectional and occurs throughout follicular development (2, 3). In fact, follicular formation itself appears coordinated by a transcription factor, factor in the germline ␣ (FIG␣), expressed by the oocyte (4). Early follicular development depends on oocyte-secreted members of the transforming growth factor ␤ family, growth differentiation factor (GDF)-9, and bone morphogenic protein (BMP)-15 (5-7). These oocyte-derived paracrine factors also promote follicular somatic cell proliferation and steroidogenesis (8-10) and locally regulate gene expression in granulosa cells (10-13). Thus, communication between the oocyte and companion somatic cells is crucial for the development of both cell types, but how this complex interaction is coordinated was not previously known.At...

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“…This finding is supported by the fact that the sequence between the two groups of C residues can be glycosylated (7,8) and is susceptible to protease digestion (34), as expected for a solvent-exposed polypeptide fragment linking independently folded regions. Moreover, PLAC1 (35) and OOSP1 (36) are proteins whose N-terminal sequences share homology with the first half of the ZP3 ZP domain, including C residues 1-4 (Fig. 3B).…”

Section: Discussionmentioning

confidence: 99%

A duplicated motif controls assembly of zona pellucida domain proteins

Jovine

Williams

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

123

170

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Many secreted eukaryotic glycoproteins that play fundamental roles in development, hearing, immunity, and cancer polymerize into filaments and extracellular matrices through zona pellucida (ZP) domains. ZP domain proteins are synthesized as precursors containing C-terminal propeptides that are cleaved at conserved sites. However, the consequences of this processing and the mechanism by which nascent proteins assemble are unclear. By microinjection of mutated DNA constructs into growing oocytes and mammalian cell transfection, we have identified a conserved duplicated motif [EHP (external hydrophobic patch)͞IHP (internal hydrophobic patch)] regulating the assembly of mouse ZP proteins. Whereas the transmembrane domain (TMD) of ZP3 can be functionally replaced by an unrelated TMD, mutations in either EHP or IHP do not hinder secretion of full-length ZP3 but completely abolish its assembly. Because mutants truncated before the TMD are not processed, we conclude that the conserved TMD of mammalian ZP proteins does not engage them in specific interactions but is essential for C-terminal processing. Cleavage of ZP precursors results in loss of the EHP, thereby activating secreted polypeptides to assemble by using the IHP within the ZP domain. Taken together, these findings suggest a general mechanism for assembly of ZP domain proteins.T he zona pellucida (ZP) domain is a protein polymerization module of Ϸ260 aa (1). Since its identification in mouse ZP glycoproteins (2), this domain has been found in many extracellular eukaryotic proteins of diverse molecular architecture and biological function (2, 3). These include egg coat proteins, inner ear proteins, urinary and pancreatic proteins, transforming growth factor-␤ receptors, immune defense proteins, nematode cuticle components, and fly proteins involved in transmission of mechanical stimuli and in wing and tracheal morphogenesis (4).We study the ZP (3), an extracellular coat secreted by growing mouse oocytes, as a model for ZP domain protein maturation and assembly. The ZP consists of long filaments composed of ZP2 and ZP3, crosslinked by a third ZP domain protein, ZP1. Nascent ZP polypeptides have features in common with other ZP domain proteins (2-4) that include an N-terminal signal sequence (SP), a ZP domain, and a consensus furin cleavage site (CFCS). The latter is followed by a C-terminal propeptide containing a transmembrane domain (TMD) and short cytoplasmic tail (Fig. 1A) that are replaced by a glycosyl phosphatidylinositol anchor in some ZP domain proteins. During secretion, but before incorporation into the ZP, a furin-like enzyme excises the propeptide from ZP precursors by cleavage at the CFCS (5-8). C-terminal processing of precursors also occurs for ZP homologues from fish to birds (9-11), as well as for other . Recombinant ZP proteins synthesized from cDNAs mutated at the CFCS are not secreted and accumulate in the endoplasmic reticulum of transfected cells (15)(16)(17). Recently, assembly of ZP proteins was studied by microinjection of epitope-tagge...

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Oosp1 encodes a novel mouse oocyte‐secreted protein

Cited by 35 publications

References 21 publications

Histone acetyltransferase KAT8 is essential for mouse oocyte development by regulating ROS levels

Histone acetyltransferase KAT8 is essential for mouse oocyte development by regulating ROS levels

The mammalian oocyte orchestrates the rate of ovarian follicular development

A duplicated motif controls assembly of zona pellucida domain proteins

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