Colocalization of CaM KII and MAP kinase on architectural elements of the mouse egg: Potentiation of MAP kinase activity by CaM KII

Hatch, Kimberly R.; Capco, David G.

doi:10.1002/1098-2795(200101)58:1<69::aid-mrd10>3.0.co;2-o

Cited by 42 publications

(25 citation statements)

References 35 publications

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“…The activated APC/C, with its E3 ligase activity, leads to subsequent proteolysis of target proteins via the 2 6 S p r o t e a s o m e c o m p l e x ; p 3 4 c d c 2 k i n a s e inactivation via the destruction of cyclin B and securing occur via this mechanism [7][8][9]. In mammals, intracellular Ca 2+ elevation induced by electrical pulse triggers the destruction of cyclin B and meiotic resumption from MII arrest, but the treatment of these oocytes with myristoylatedautocamtide-2-related inhibitory peptide (AIP) prevents decrease of p34 cdc2 kinase activity [10][11][12]. Furthermore, it has been reported that injection of a constitutively active CaMKII construct is sufficient to induce activation in mouse oocytes [13].…”

mentioning

confidence: 99%

The Regulation of Calcium/Calmodulin-dependent Protein Kinase II during Oocyte Activation in the Rat

Ito

Kaneko

Hirabayashi

2006

Journal of Reproduction and Development

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Abstract. Increases in intracellular Ca2+ are required for oocyte activation and subsequent development. Calmodulin-dependent protein kinase II (CaMKII) plays a crucial role in oocyte activation. However, how CaMKII is regulated during this process is not well characterized. We show here for the first time in rat oocytes that CaMKII is phosphorylated during oocyte activation. CaMKII phosphorylation was suppressed by KN93, a CaMKII inhibitor, but not KN92, which is the inactive analogue of KN93. Electrical stimulation of rat oocytes resulted in degradation of both cyclin B and Mos, presumably due a rise in Ca 2+ induced by the electrical pulse. KN93 blocked the degradation of both proteins induced by the electrical pulse. Addition of a protein phosphatase inhibitor, okadaic acid (OA), further increased the amount of CaMKII and also increased the amount of phosphorylated enzyme. Importantly, in oocytes undergoing spontaneous activation, accumulation and phosphorylation of CaMKII also occurs in a time-dependent manner. Consistent with this, addition of KN93 inhibited spontaneous activation. Collectively, our results show that CaMKII is phosphorylated during oocyte activation and that this phosphorylation is involved in inactivation of p34 cdc2 kinase and somewhat involved in degradation of Mos. Furthermore, CaMKII phosphorylation is negatively regulated by a protein phosphatase.

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mentioning

confidence: 99%

The Regulation of Calcium/Calmodulin-dependent Protein Kinase II during Oocyte Activation in the Rat

Ito

Kaneko

Hirabayashi

2006

Journal of Reproduction and Development

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“…From these results, Fan & Sun (2004) hypothesized that CaMKII could serve to potentiate MAP kinase and p90 ribosomal S6 kinase activity after egg activation because the primary sequence of ERK2 indicates the consensus phosphorylation site for CaMKII at Thr92 (GeneBank Accession no. X58712) (Hatch & Capco 2001). Since our present study demonstrated that IVF oocytes treated with KN-93 showed significant lower levels of MAP kinase activity as compared with that in oocytes treated without KN-93, it is possible that CaMKII induces MAP kinase activation.…”

Section: Discussionmentioning

confidence: 54%

“…Fan et al (2003) demonstrated that MAP kinase was dephosphorylated after artificial activation and the amount was also dramatically decreased. Co-localization of MAP kinase and CaMKII in mouse (Hatch & Capco 2001) and pig (Fan et al 2003) oocytes could directly interact in specialized areas in the cell. From these results, Fan & Sun (2004) hypothesized that CaMKII could serve to potentiate MAP kinase and p90 ribosomal S6 kinase activity after egg activation because the primary sequence of ERK2 indicates the consensus phosphorylation site for CaMKII at Thr92 (GeneBank Accession no.…”

Section: Discussionmentioning

confidence: 99%

“…In the matured oocytes, intracellular Ca 2þ elevation induced the destruction of cyclin B corresponding with the decrease in p34 cdc2 kinase activity, but injection of the CaMKII inhibitory peptide, autocamtide2 inhibitory peptide, into the oocytes failed to decrease histone H1 kinase activity which corresponded with p34 cdc2 kinase activity (Tatone et al 2002). Suppression of CaMKII activity also results in a reduction in the amount of MAP kinase as well as a decreased level of activity of MAP kinase in mice and pigs (Hatch & Capco 2001, Fan & Sun 2004. Fan et al (2003) reported that electrical pulse-induced inactivation of p34 cdc2 kinase was prevented by treatment with the CaMKII inhibitor, KN-93, in porcine oocytes.…”

Section: Introductionmentioning

confidence: 99%

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The role of calcium/calmodulin-dependent protein kinase II on the inactivation of MAP kinase and p34cdc2 kinase during fertilization and activation in pig oocytes

Ito¹,

Kawano²,

Hirabayashi³

et al. 2004

Reproduction

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The objective of this study was to investigate the role of calmodulin-dependent protein kinase II (CaMKII) during fertilization in the pig. Since it has been reported that CaMKII is involved in the capacitation and acrosome reaction of spermatozoa, we tested whether supplementation with the CaMKII inhibitor, KN-93, in the fertilization medium affected sperm penetration. The results showed that the addition of KN-93 in the fertilization medium significantly reduced the rate of sperm penetration into oocytes. However, pre-treatment with KN-93 before in vitro fertilization (IVF) did not significantly affect sperm penetration, but it did affect pronuclear formation in a dose-dependent manner. In the oocytes pre-treated with KN-93 before IVF and then co-cultured with spermatozoa without the drug, the decrease in p34 cdc2 kinase and the cyclin B1 level were significantly suppressed as compared with those in penetrated oocytes without treatment with KN-93. However, the decrease in MAP kinase activity was not affected by . Additional treatment with KN-93 after Ca 21 ionophore treatment also inhibited the reduction in p34 cdc2 kinase activity and the cyclin B1 level, but not MAP kinase activity. Treatment with KN-92, an inactive KN-93 analogue, did not significantly affect sperm penetration and pronuclear formation. In conclusion, the activation of CaMKII by artificial stimuli or sperm stimulated the disruption of cyclin B1 and the inactivation of p34 cdc2 kinase, but did not affect MAP kinase inactivation during oocyte activation in pigs.

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“…[g-32 P]ATP (data not shown) as well as the ex vivo translation and distribution of the CA-aCaMKII cRNA, 3 h after microinjecting the eggs, in order to ensure that mutated proteins maintain their original intracellular localization (Hatch & Capco 2001). Control, noninjected MII eggs exhibited a very pale staining ( Fig.…”

Section: Marcks Mediates Cortical Granules Exocytosismentioning

confidence: 98%

Myristoylated alanine-rich C kinase substrate, but not Ca2+/calmodulin-dependent protein kinase II, is the mediator in cortical granules exocytosis

Tsaadon¹,

Kaplan-Kraicer²,

Shalgi³

2008

Reproduction

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Sperm-egg fusion induces cortical granules exocytosis (CGE), a process that ensures the block to polyspermy. CGE can be induced independently by either a rise in intracellular calcium concentration or protein kinase C (PKC) activation. We have previously shown that myristoylated alanine-rich C kinase substrate (MARCKS) cross-links filamentous actin (F-actin) and regulates its reorganization. This activity is reduced either by PKC-induced MARCKS phosphorylation (PKC pathway) or by its direct binding to calmodulin (CaM; CaM pathway), both inducing MARCKS translocation, F-actin reorganization, and CGE. Currently, we examine the involvement of Ca 2C /CaM-dependent protein kinase II (CaMKII) and MARCKS in promoting CGE and show that PKC pathway can compensate for lack of Ca 2C /CaM pathway. Microinjecting eggs with either overexpressed protein or complementary RNA of constitutively active aCaMKII triggered resumption of second meiotic division, but induced CGE of an insignificant magnitude compared with CGE induced by wt aCaMKII. Microinjecting eggs with mutant-unphosphorylatable MARCKS reduced the intensity of 12-O-tetradecanoylphorbol 13-acetate or ionomycin-induced CGE by 50%, indicating that phosphorylation of MARCKS by novel and/or conventional PKCs (n/cPKCs) is a pivotal event associated with CGE. Moreover, we were able to demonstrate cPKCs involvement in ionomycin-induced MARCKS translocation and CGE. These results led us to propose that MARCKS, rather than CaMKII, as a key mediator of CGE. Reproduction (2008) 135 613-624

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Colocalization of CaM KII and MAP kinase on architectural elements of the mouse egg: Potentiation of MAP kinase activity by CaM KII

Cited by 42 publications

References 35 publications

The Regulation of Calcium/Calmodulin-dependent Protein Kinase II during Oocyte Activation in the Rat

The Regulation of Calcium/Calmodulin-dependent Protein Kinase II during Oocyte Activation in the Rat

The role of calcium/calmodulin-dependent protein kinase II on the inactivation of MAP kinase and p34cdc2 kinase during fertilization and activation in pig oocytes

Myristoylated alanine-rich C kinase substrate, but not Ca2+/calmodulin-dependent protein kinase II, is the mediator in cortical granules exocytosis

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