Are Src family kinases involved in cell cycle resumption in rat eggs?

Talmor-Cohen, A; Tomashov-Matar, R; Eliyahu, Efrat; Shapiro, Richard A.; Shalgi, Ruth

doi:10.1530/rep.1.00104

Cited by 55 publications

(62 citation statements)

References 55 publications

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“…Expression of Fyn, a member of Src kinase family (SFKs), is demonstrated and its activity is detected in rat eggs, which represents the first demonstration of a PTK in mammalian eggs (Talmor et al 1998). Furthermore, other members of SFKs, including Src and Yes, were detected in rat eggs (Talmor-Cohen et al 2004). In the present study, for the first time, we detected Pyk2 expression in mammalian eggs.…”

Section: Discussionsupporting

confidence: 59%

“…Protein tyrosine kinases (PTKs) are essential in extracellular signaling and actin cytoskeleton organization. A small group of PTKs have been identified in eggs of invertebrates, lower vertebrates and some mammals, and inhibitor studies have suggested that they are involved in egg activation (Sato et al 2000, Runft et al 2002, Talmor-Cohen et al 2004. It has been suggested that protein tyrosine phosphorylation may be implicated in the regulation of mouse oocyte maturation.…”

Section: Introductionmentioning

confidence: 99%

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Proline-rich tyrosine kinase2 is involved in F-actin organization during in vitro maturation of rat oocyte

Meng¹,

Zheng²,

Yang³

et al. 2006

Reproduction

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Microfilaments (actin filaments) regulate various dynamic events during meiotic maturation. Relatively, little is known about the regulation of microfilament organization in mammalian oocytes. Proline-rich tyrosine kinase2 (Pyk2), a protein tyrosine kinase related to focal adhesion kinase (FAK) is essential in actin filaments organization. The present study was to examine the expression and localization of Pyk2, and in particular, its function during rat oocyte maturation. For the first time, by using Western blot and confocal laser scanning microscopy, we detected the expression of Pyk2 in rat oocytes and found that Pyk2 and Try402 phosphoPyk2 were localized uniformly at the cell cortex and surrounded the germinal vesicle (GV) or the condensed chromosomes at the GV stage or after GV breakdown. At the metaphase and the beginning of anaphase, Pyk2 distributed asymmetrically both in the ooplasm and the cortex with a marked staining associated with the chromosomes and the region overlying the meiotic spindle. At telophase, Pyk2 was observed in the cleavage furrows in addition to its cortex and cytoplasm localization. The dynamics of Pyk2 were similar to that of F-actin, and this kinase was found to co-localize with microfilaments in several developmental stages during rat oocyte maturation. Microinjection of Pyk2 antibody demolished the microfilaments assembly and also inhibited the first polar body (PB1) emission. These findings suggest an important role of Pyk2 for rat oocyte maturation by regulating the organization of actin filaments.

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Section: Discussionsupporting

confidence: 59%

Section: Introductionmentioning

confidence: 99%

Proline-rich tyrosine kinase2 is involved in F-actin organization during in vitro maturation of rat oocyte

Meng¹,

Zheng²,

Yang³

et al. 2006

Reproduction

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“…In cases of spontaneous activation none of these indicators of activation were found. Interestingly, in ionomycin-activated rat eggs, it was demonstrated that resumption of meiosis and PN development were significantly hindered by Src family tyrosine kinase inhibitors, while cortical granule exocytosis was not (43). Another study in mouse demonstrated that during sequential fractionation of freeze-thaw sperm extracts, the ability to support pronuclear formation was lost before Ca 2ϩ -releasing ability (44).…”

Section: Discussionmentioning

confidence: 99%

PAWP, a Sperm-specific WW Domain-binding Protein, Promotes Meiotic Resumption and Pronuclear Development during Fertilization

Šutovský

Manandhar

et al. 2007

Journal of Biological Chemistry

164

181

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We report a novel alkaline extractable protein of the sperm head that exclusively resides in the post-acrosomal sheath region of the perinuclear theca (PT) and is expressed and assembled in elongating spermatids. It is a protein that shares sequence homology to the N-terminal half of WW domainbinding protein 2, while the C-terminal half is unique and rich in proline. A functional PPXY consensus binding site for group-I WW domain-containing proteins, and numerous unique repeating motifs, YGXPPXG, are identified in the proline-rich region. Considering these molecular characteristics, we designated this protein PAWP for postacrosomal sheath WW domain-binding protein. Microinjection of recombinant PAWP or alkaline PT extract into metaphase II-arrested porcine, bovine, macaque, and Xenopus oocytes induced a high rate of pronuclear formation, which was prevented by co-injection of a competitive PPXY motif containing peptide derived from PAWP but not by co-injection of the point-mutated peptide. Intracytoplasmic sperm injection (ICSI) of porcine oocytes combined with co-injection of the competitive PPXY peptide or an anti-recombinant PAWP antiserum prevented pronuclear formation and arrested fertilization. Conversely, co-injection of the modified PPXY peptide, when the tyrosine residue of PPXY was either phosphorylated or substituted with phenylalanine, did not prevent ICSI-induced fertilization. This study uncovers a group I WW domain module signal transduction event within the fertilized egg that appears compulsory for meiotic resumption and pronuclear development during egg activation and provides compelling evidence that a PPXY motif of spermcontributed PAWP can trigger these events. The perinuclear theca (PT)3 of the mammalian sperm head is a condensed cytosolic structure layered between the sperm acrosome and nucleus and, continuing caudally, between the plasmalemma and nucleus. On a compositional basis, the PT can be subdivided into three structurally continuous regions, the subacrosomal layer, the outer periacrosomal layer on the outer aspect of the equatorial segment and the post-acrosomal sheath (PAS) (1, 2). Traditionally, PT has been considered as a cytoskeletal scaffold responsible for maintaining the overall architecture of the mature sperm head. However, recent studies indicate that the bulk of proteins making up the PT are not traditional cytoskeletal proteins but rather a variety of cytosolic proteins linked together and susceptible to extraction under different regimens (3). For example, alkaline extractable SubH2Bv, exclusive to the subacrosomal layer, is implicated in acrosome-nuclear docking during spermiogenesis (1). Salt-extractable non-nuclear somatic core histones, residing in the PAS, may be involved in stabilizing the chromatin of the decondensing sperm nucleus soon after oocyte entry (4, 5). The DTT salt or alkaline extractable calicin and cylicin II share a basic pI with the histones and bind to actin in vitro (6 -8). Detergentand salt-resistant fraction, "calyx fraction" of the PT, contain...

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“…Inhibitor studies performed in oocytes from mouse and rat have implicated Src-family PTKs in events required for MII resumption following parthenogenetic activation (Sette et al 2002, Talmor-Cohen et al 2004a. After fertilization, PTK inhibitors have been shown to block zygote development during or just prior to DNA synthesis resulting in an arrest of development prior to the two-cell stage (Besterman & Schultz 1990, Jacquet et al 1995.…”

Section: Role Of Src-family Kinases During Zygotic Developmentmentioning

confidence: 99%

“…For example, while mammalian eggs express Fyn, Yes, and in some cases, Src (Talmor et al 1998, Talmor-Cohen et al 2004a), the results of two different studies indicate that these kinases are not required for the unique sperm-induced calcium oscillations (Kurokawa et al 2004a, Mehlmann & Jaffe 2005, which trigger egg activation in mammals (Carroll 2001). Instead, these calcium oscillations are triggered directly by a sperm-borne phospholipase that does not require PTK regulation (Cox et al 2002).…”

Section: Introductionmentioning

confidence: 99%

Role of Src homology 2 domain-mediated PTK signaling in mouse zygotic development

Meng

Luo²,

Li³

et al. 2006

Reproduction

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Fyn and other Src-family kinases play an essential role at several steps during egg activation following fertilization of externally fertilizing species, such as marine invertebrates, fish, and frogs. Recent studies demonstrate that the requirement for Src-family kinases in activation of the mammalian egg is different from lower species, and the objective of this study was to test the role of the Fyn kinase in the mouse egg activated by intracytoplasmic sperm injection (ICSI). An Src homology 2 (SH2) domain containing fusion protein was used to suppress Fyn function in the mouse zygote following ICSI. Eggs injected with the Fyn SH2 domain at an intracellular concentration of 4-8 mM exhibited reduced developmental potential with 100% of the zygotes being arrested following the first or the second cleavage. At higher concentrations, the protein blocked pronuclear congression and the zygotes remained at the pronuclear stage. The SH2 domain had no effect on sperm-induced calcium oscillations in distinct contrast to its effect on the eggs of lower species. The results indicate that the SH2 domain of Fyn kinase plays an important role in pronuclear congression as well as early cleavage events and that this effect appears not to involve disruption of calcium oscillations.

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Are Src family kinases involved in cell cycle resumption in rat eggs?

Abstract: The earliest visible indications for the transition to embryos in mammalian eggs, known as egg activation, are cortical granules exocytosis (CGE) and resumption of meiosis (RM); these events are triggered by the fertilizing spermatozoon through a series

Cited by 55 publications

References 55 publications

Proline-rich tyrosine kinase2 is involved in F-actin organization during in vitro maturation of rat oocyte

Proline-rich tyrosine kinase2 is involved in F-actin organization during in vitro maturation of rat oocyte

PAWP, a Sperm-specific WW Domain-binding Protein, Promotes Meiotic Resumption and Pronuclear Development during Fertilization

Role of Src homology 2 domain-mediated PTK signaling in mouse zygotic development

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